HSP90 / Heat Shock Protein 90 alpha Antibody (3G3)

HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody for Western blot, IF, IHC, IP

>> See 12 other antibodies for HSP90AA1 (HSP86; HSP89A; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; Hsp89; Hsp90; LAP2; HSP 86; heat shock 86 kDa; heat shock 90kD protein 1; alpha; heat shock 90kD protein 1; alpha-like 4; heat shock 90kD protein; alpha-like 4; heat shock 90kDa protein 1; alpha; heat shock protein HSP 90-alpha; renal carcinoma antigen NY-REN-38)
Synonyms:
HSP86; HSP89A; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; Hsp89; Hsp90; LAP2; HSP 86; heat shock 86 kDa; heat shock 90kD protein 1; alpha; heat shock 90kD protein 1; alpha-like 4; heat shock 90kD protein; alpha-like 4; heat shock 90kDa protein 1; alpha; heat shock protein HSP 90-alpha; renal carcinoma antigen NY-REN-38
Details
Host / Isotype: Mouse / IgM
Class: Monoclonal
Type: Antibody
Clone: 3G3
Tested Species Reactivity: Human (Hu), Mouse (Ms), Rat (Rt), Chicken (Ck), Fish (Fs), Non-human primate (Nhp)
Published Species Reactivity: Bovine (Bv), Drosophila (Dm), Human (Hu), Mouse (Ms), Non-human primate (Nhp), Porcine (Po), Rabbit (Rb), Rat (Rt), Virus (Vs)
Immunogen: Purified mouse HSP90.
Ordering Information
Pierce HSP90 / Heat Shock Protein 90 alpha Antibody (3G3)
Product #
MA3-011
Size
400 µl
Price
$316.00
Purchase
Add HSP90 / Heat Shock Protein 90 alpha Antibody (3G3) to your cart.
Tested Applications Dilution *
Western Blot (WB) 1:200 - 1:1000
Immunofluorescence (IF) 1:50 - 1:200
Immunohistochemistry (IHC) 1:200
Immunoprecipitation (IP) 1:500 - 1:1000
Published Applications Dilution
Western Blot (WB) See publications below
Immunocytochemistry (ICC) See publications below
Immunoprecipitation (IP) See publications below
ELISA (ELISA) See publications below
Blocking Assay (BLOCK) See publications below
* Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.
Form Information
Form: Liquid
Storage Buffer: ascites with Ammonium sulfate
Preservative: no preservative
Storage Conditions: -20° C, Avoid Freeze/Thaw Cycles
Product Specific Information
MA3-011 detects heat shock protein 90 kDa (HSP90) from human, mouse, rat, rainbow trout, and chicken tissues.

MA3-011 has been successfully used in Western blot, immunofluorescence, immunohistochemistry, and immunoprecipitation procedures. By Western blot, this antibody detects a 90 kDa protein representing HSP90 from Hepa 1 cell extract. It has been reported that up to 90% of cytosolic HSP90 can be immunoprecipitated with this product under low ionic strength conditions.

For Western blots using MA3-011, nitrocellulose is recommended. PVDF membranes typically do not yield acceptable results with this antibody.

Before use, centrifuge suspension (4000 g for 15 minutes) and discard supernatant. Resuspend pellet in 200µl of PBS, pH 7.2. If desired, 0.05% sodium azide may be added to resuspended solution. Removal of residual ammonium sulfate is not usually necessary for immunoprecipitation and Western blot procedures, however, any other uses may require its removal by dialysis or equivalent method. Stable for 6 months after PBS resuspension.

The MA3-011 antigen is purified HSP90 from Hepa 1 cytosol.
General Information
Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat. HSP90 is a 90 kDa protein that is induced under stress conditions, but is also one of the most abundant cellular proteins found under non-stress conditions. HSP90 has been found to be associated with a number of other intracellular proteins, including steroid receptors, actin, tubulin, and some kinases. It has been suggested that HSP90 is necessary to maintain structural integrity of at least some steroid receptors to allow for ligand binding during receptor activation.
Product Images
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in WB
    HSP90_Antibody_MA3-011_Western-Blot_1.jpg

    Western Blot with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (HSP90_Antibody_MA3-011_Western-Blot_1.jpg)

    Western Blot with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Western blot analysis of Heat Shock Protein 90 (Hsp90) was performed by loading 50ug of various whole cell lysates and 15ul PageRuler Prestained Protein Ladder (Product # 26616) onto a 4-20% Tris-HCl polyacrylamide gel. Proteins were transferred to a nitrocellulose membrane and blocked with 5% BSA/TBST for at least 1 hour. The membrane was probed with a Hsp90 monoclonal antibody (Product # MA3-011) at a dilution of 1:1000 overnight at 4°C on a rocking platform, washed in TBS-0.1%Tween-20, and probed with a goat anti-mouse IgG + IgM secondary antibody (Product # 31446) at a dilution of 1:40,000 for 30 minutes. Chemiluminescent detection was performed using SuperSignal West Dura (Product # 34075).
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in WB
    Hsp90_Antibody_MA3-011_Western-blot_2_20131210095657.jpg

    Western Blot with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (Hsp90_Antibody_MA3-011_Western-blot_2_20131210095657.jpg)

    Western Blot with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Western blot analysis of Heat Shock Protein 90 (Hsp90) was performed by loading 30ug of HEK293T whole cell lysate per well onto an SDS-PAGE gel. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 1 hour at room temperature. The membrane was probed with an Hsp90 monoclonal antibody (Product # MA3-011) at a dilution of 1:200 overnight at 4°C, washed in TBST, and probed with an HRP-conjugated goat anti-mouse IgG (H + L) secondary antibody at a dilution of 1:40,000 for 1 hour at room temperature. Chemiluminescent detection was performed using ECL substrate. Data courtesy of the Innovators Program.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IF
    MA3-011_IF_C6.jpg

    Immunofluorescence with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IF_C6.jpg)

    Immunofluorescence with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunofluorescent analysis of Heat Shock Protein 90 using Heat Shock Protein 90 Monoclonal antibody (3G3) (Product# MA3-011) shows staining in C6 glioma cells. Heat Shock Protein 90 staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with or an antibody recognizing Heat Shock Protein 90 (Product# MA3-011) at a dilution of 1:200 over night at 4 C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product# 35552 for GAR, Product# 35503 for GAM). Images were taken at 60X magnification.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IF
    MA3-011_IF_Hela.jpg

    Immunofluorescence with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IF_Hela.jpg)

    Immunofluorescence with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunofluorescent analysis of Heat Shock Protein 90 using Heat Shock Protein 90 Monoclonal antibody (3G3) (Product# MA3-011) shows staining in HeLa cells. Heat Shock Protein 90 staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with or an antibody recognizing Heat Shock Protein 90 (Product# MA3-011) at a dilution of 1:200 over night at 4 C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product# 35552 for GAR, Product# 35503 for GAM). Images were taken at 60X magnification.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IF
    MA3-011_IF_WiDr.jpg

    Immunofluorescence with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IF_WiDr.jpg)

    Immunofluorescence with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunofluorescent analysis of Heat Shock Protein 90 using Heat Shock Protein 90 Monoclonal antibody (3G3) (Product# MA3-011) shows staining in WiDr colon carcinoma cells. Heat Shock Protein 90 staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with or an antibody recognizing Heat Shock Protein 90 (Product# MA3-011) at a dilution of 1:200 over night at 4 C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product# 35552 for GAR, Product# 35503 for GAM). Images were taken at 60X magnification.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IF
    HSP90_Antibody_MA3-011_Immunofluorescence_4.jpg

    Immunofluorescence with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (HSP90_Antibody_MA3-011_Immunofluorescence_4.jpg)

    Immunofluorescence with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunofluorescent analysis of Heat Shock Protein 90 (Hsp90) (green) in HeLa cells. Formalin fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 10 minutes at room temperature and blocked with 1% Blocker BSA (Product # 37525) for 15 minutes at room temperature. Cells were probed without (left panel) or with (right panel) a Hsp90 monoclonal antibody (Product # MA3-011), at a dilution of 1:100 for at least 1 hour at room temperature, washed with PBS, and incubated with a fluorescently-conjugated goat anti-mouse IgM secondary antibody at a dilution of 1:400 for 30 minutes at room temperature. F-Actin (red) was stained with DyLight-554 Phalloidin (Product # 21834) and nuclei (blue) were stained with Hoechst 33342 dye (Product# 62249). Images were taken on a Thermo Scientific ArrayScan at 20X magnification.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IHC
    MA3-011_IHC_breast_carcinoma _tissue.jpg

    Immunohistochemistry with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IHC_breast_carcinoma _tissue.jpg)

    Immunohistochemistry with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunohistochemistry was performed on cancer biopsies of deparaffinized Human breast carcinoma tissue. To expose target proteins, heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer, microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:200 with a mouse monoclonal antibody recognizing Heat Shock Protein 90 (MA3-011) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IHC
    MA3-011_IHC_placenta_tissue.jpg

    Immunohistochemistry with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IHC_placenta_tissue.jpg)

    Immunohistochemistry with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunohistochemistry was performed on normal biopsies of deparaffinized Human placenta tissue. To expose target proteins, heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer, microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:200 with a mouse monoclonal antibody recognizing Heat Shock Protein 90 (MA3-011) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IHC
    MA3-011_IHC_Tonsil_tissue.jpg

    Immunohistochemistry with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (MA3-011_IHC_Tonsil_tissue.jpg)

    Immunohistochemistry with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunohistochemistry was performed on normal biopsies of deparaffinized Human tonsil tissue. To expose target proteins, heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer, microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:200 with a mouse monoclonal antibody recognizing Heat Shock Protein 90 (MA3-011) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
  • HSP90 / Heat Shock Protein 90 alpha Antibody (MA3-011) in IP
    HSP90_Antibody_MA3-011_Immunoprecipitation_1.jpg

    Immunoprecipitation with anti-HSP90  /  Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011) (HSP90_Antibody_MA3-011_Immunoprecipitation_1.jpg)

    Immunoprecipitation with anti-HSP90 / Heat Shock Protein 90 alpha Monoclonal Antibody [3G3] (MA3-011)

    Immunoprecipitation of Heat Shock Protein 90 (Hsp90) was performed on K562 cells. Antigen-antibody complexes were formed by incubating 500ug of whole cell lysate with 3ug of a HSP90 monoclonal antibody (Product # MA3-011) overnight on a rocking platform at 4°C. The immune complexes were captured on 50ul Protein A/G Agarose (Product # 20421), washed extensively, and eluted with Lane Marker Reducing Sample Buffer (Product # 39000). Samples were resolved on a 4-20% Tris-HCl polyacrylamide gel, transferred to a PVDF membrane, and blocked with 5% BSA/TBST for at least 1 hour. The membrane was probed with a Hsp90 monoclonal antibody (Product # MA3-011) at a dilution of 1:500 overnight rotating at 4°C, washed in TBST, and probed with an HRP-conjugated goat anti-mouse IgM secondary antibody (Product # 31440) at a dilution of 1:20,000 for at least 1 hour. Chemiluminescent detection was performed using SuperSignal West Dura (Product # 34075).
Publications:
Western Blot
  Species / Dilution Summary
  Bv / Not Cited
MA3-011 was used in western blot to study the mechanism for the p50 (cdc37) association with Raf and hsp90

J Biol Chem. 1998 Aug 7;273(32):20090-5.
"p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site."
Author(s): Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB
Number of Citations: 17
(See PubMed article )
  Hu / 0
MA3-011 was used in western blot to investigate the effect of 17-allylamino-17-demethoxygeldanamycin on heat shock protein 90 chaperone function

Cancer Chemother Pharmacol. 1998;42(4):273-9.
"The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin."
Author(s): Schulte TW, Neckers LM
Number of Citations: 33
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the role of the redox during the nuclear import of the glucocorticoid receptor

J Biol Chem. 1999 Apr 9;274(15):10363-71.
"Redox-dependent regulation of nuclear import of the glucocorticoid receptor."
Author(s): Okamoto K, Tanaka H, Ogawa H, Makino Y, Eguchi H, Hayashi S, Yoshikawa N, Poellinger L, Umesono K, Makino I
Number of Citations: 10
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in western blot to investigate the mechanism of KF25706 for its in vivo antitumor activity

Cancer Res. 1999 Jun 15;59(12):2931-8.
"KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules."
Author(s): Soga S, Neckers LM, Schulte TW, Shiotsu Y, Akasaka K, Narumi H, Agatsuma T, Ikuina Y, Murakata C, Tamaoki T, Akinaga S
Number of Citations: 9
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the protein components of the HSP90 complex

J Biol Chem. 1991 Apr 15;266(11):6708-13.
"Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000."
Author(s): Perdew GH, Whitelaw ML
Number of Citations: 21
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the role of self-sufficient protein folding structure, a "foldosome" during assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90

J Biol Chem. 1994 Nov 11;269(45):27894-9.
"All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"."
Author(s): Hutchison KA, Dittmar KD, Pratt WB
Number of Citations: 12
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in western blot to study the immunogenicity of gp96, hsp90 and hsp70 derived from Met A sarcoma

J Immunol. 1994 Jun 1;152(11):5398-403.
"Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70."
Author(s): Udono H, Srivastava PK
Number of Citations: 45
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in western blot to investigate the role of tetratricopeptide repeat (TPR) domain of protein phosphatase 5 (PP5) in GR signaling

J Biol Chem. 1996 Dec 13;271(50):32315-20.
"The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant."
Author(s): Chen MS, Silverstein AM, Pratt WB, Chinkers M
Number of Citations: 38
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in western blot to determine the association of heat shock proteins with MHC class I-restricted tumor antigen precursors

J Immunol. 1999 Feb 1;162(3):1303-9.
"Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96."
Author(s): Ishii T, Udono H, Yamano T, Ohta H, Uenaka A, Ono T, Hizuta A, Tanaka N, Srivastava PK, Nakayama E
Number of Citations: 17
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the role of tumor-derived, chaperone-rich cell lysate for dendritic cells and potent antitumor immunity activation

Blood. 2003 Jun 1;101(11):4485-91.
"Tumor-derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity."
Author(s): Zeng Y, Feng H, Graner MW, Katsanis E
Number of Citations: 1
(See PubMed article )
  Nhp / 0
MA3-011 was used in immunoprecipitation and western blot to study teh role of LXXLL motifs in human glucocorticoid receptor function

J Steroid Biochem Mol Biol. 2006 Oct;101(2-3):106-17.
"Functional analysis of the LXXLL motifs of the human glucocorticoid receptor: association with altered ligand affinity."
Author(s): Dong DD, Jewell CM, Bienstock RJ, Cidlowski JA
Number of Citations: 1
(See PubMed article )
  Po / Not Cited
MA3-011 was used in immunoprecipitation and western blot to study the mechanism for the interaction of neuropeptide Y and Hsp90

Biochemistry. 2003 Nov 11;42(44):12972-80.
"Interaction of neuropeptide Y and Hsp90 through a novel peptide binding region."
Author(s): Ishiwatari-Hayasaka H, Maruya M, Sreedhar AS, Nemoto TK, Csermely P, Yahara I
Number of Citations: 1
(See PubMed article )
  Rb / 1:2,000
MA3-011 was used in immunoprecipitation and western blot to study the function of p23 during the process of receptor activation by hsp foldosome

J Biol Chem. 1995 Aug 11;270(32):18841-7.
"The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90."
Author(s): Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB
Number of Citations: 21
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in western blot to investigate the role of chaperone components for energy-dependent protein refolding activity

FEBS Lett. 1993 Sep 27;331(1-2):25-30.
"ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components."
Author(s): Nimmesgern E, Hartl FU
Number of Citations: 7
(See PubMed article )
  Rb / 1:500
MA3-011 was used in western blot to investigate the role of HSP90 in the proper folding of mutated p53

Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8379-83.
"Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90."
Author(s): Blagosklonny MV, Toretsky J, Bohen S, Neckers L
Number of Citations: 25
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in western blot to study the mechanism for the p50 (cdc37) association with Raf and hsp90

J Biol Chem. 1998 Aug 7;273(32):20090-5.
"p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site."
Author(s): Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB
Number of Citations: 17
(See PubMed article )
  Rb / 1:1,000
MA3-011 was used in western blot to study the binding site for the association between the FKBP52/dimer and hsp90

J Biol Chem. 1999 Dec 24;274(52):36980-6.
"Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein."
Author(s): Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB
Number of Citations: 19
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in western blot to demonstrate that the two chaperone proteins cooperate with each other to open up the steroid binding site.

J Biol Chem. 2001 Aug 10;276(32):30092-8.
"Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate."
Author(s): Murphy PJ, Kanelakis KC, Galigniana MD, Morishima Y, Pratt WB
Number of Citations: 1
(See PubMed article )
  Rt / Not Cited
MA3-011 was used in immunocytochemistry and western blot to study the subcellular localization of alpha internexin and neurofilament triplet proteins

J Neurocytol. 1996 Mar;25(3):181-96.
"Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons."
Author(s): Benson DL, Mandell JW, Shaw G, Banker G
Number of Citations: 2
(See PubMed article )
Immunocytochemistry
  Species / Dilution Summary
  Hu / Not Cited
MA3-011 was used in immunocytochemistry to study the role of Hsp90 and CHIP in the retrograde transport of the glucocorticoid receptor in neurites

Brain Res Mol Brain Res. 2004 Apr 7;123(1-2):27-36.
"Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation."
Author(s): Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB
Number of Citations: 16
(See PubMed article )
  Rt / 1:200
MA3-011 was used in immunocytochemistry and western blot to study the subcellular localization of alpha internexin and neurofilament triplet proteins

J Neurocytol. 1996 Mar;25(3):181-96.
"Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons."
Author(s): Benson DL, Mandell JW, Shaw G, Banker G
Number of Citations: 2
(See PubMed article )
Immunoprecipitation
  Species / Dilution Summary
  Dm / Not Cited
MA3-011 was used in immunoprecipitation to study the interaction between Sim and hsp90

J Biol Chem. 1995 Dec 29;270(52):31353-7.
"The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors."
Author(s): McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L
Number of Citations: 9
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation to investigate the role of a tyrosine kinase-dependent pathway during ligand-dependent activation of the dioxin receptor in human keratinocytes

J Biol Chem. 1994 Sep 23;269(38):23800-7.
"A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes."
Author(s): Gradin K, Whitelaw ML, Toftgård R, Poellinger L, Berghard A
Number of Citations: 3
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation to study the hypoxia-inducible factor 1 alpha expression under hypoxia.

Proc Natl Acad Sci U S A. 1997 May 27;94(11):5667-72.
"Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor."
Author(s): Kallio PJ, Pongratz I, Gradin K, McGuire J, Poellinger L
Number of Citations: 23
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the role of the redox during the nuclear import of the glucocorticoid receptor

J Biol Chem. 1999 Apr 9;274(15):10363-71.
"Redox-dependent regulation of nuclear import of the glucocorticoid receptor."
Author(s): Okamoto K, Tanaka H, Ogawa H, Makino Y, Eguchi H, Hayashi S, Yoshikawa N, Poellinger L, Umesono K, Makino I
Number of Citations: 10
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation to investigate the role of the hsp90 molecular chaperone complex in the intracellular localization of the dioxin receptor.

Mol Cell Biol. 2001 Apr;21(7):2594-607.
"The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor."
Author(s): Kazlauskas A, Sundström S, Poellinger L, Pongratz I
Number of Citations: 1
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation to investigate the effect of cytoplasmic constitutive active/androstane receptor retention protein (CCRP) on pregnane X receptor localization.

J Biol Chem. 2004 Nov 19;279(47):49307-14.
"Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver."
Author(s): Squires EJ, Sueyoshi T, Negishi M
Number of Citations: 1
(See PubMed article )
  Hu / Not Cited
MA3-011 was used in immunoprecipitation to investigate the role of Hsp90 in the PI3K/SGK-1 pathway.

J Biol Chem. 2008 Jul 4;283(27):18821-31.
"Hsp90 regulates the phosphorylation and activity of serum- and glucocorticoid-regulated kinase-1."
Author(s): Belova L, Brickley DR, Ky B, Sharma SK, Conzen SD
Number of Citations: 1
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the protein components of the HSP90 complex

J Biol Chem. 1991 Apr 15;266(11):6708-13.
"Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000."
Author(s): Perdew GH, Whitelaw ML
Number of Citations: 21
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to investigate the functional domains of mouse aryl hydrocarbon receptor

J Biol Chem. 1995 Dec 8;270(49):29270-8.
"Identification of functional domains of the aryl hydrocarbon receptor."
Author(s): Fukunaga BN, Probst MR, Reisz-Porszasz S, Hankinson O
Number of Citations: 25
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to detect the interaction between the dioxin receptor and Hsp90

J Biol Chem. 1995 Oct 20;270(42):25291-300.
"Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity."
Author(s): Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML
Number of Citations: 22
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation and western blot to investigate the role of self-sufficient protein folding structure, a "foldosome" during assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90

J Biol Chem. 1994 Nov 11;269(45):27894-9.
"All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"."
Author(s): Hutchison KA, Dittmar KD, Pratt WB
Number of Citations: 12
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to investigate the role of Arnt for release of hsp90 from the dioxin receptor in the presence of dioxin

Mol Cell Biol. 1994 Apr;14(4):2438-46.
"A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor."
Author(s): McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Number of Citations: 18
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to study the folding of hormone binding domain of glucocorticoid receptor in vitro using reconstituted receptor-hsp90 heterocomplex assembly system with purified components

J Biol Chem. 1997 May 16;272(20):13047-54.
"Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation."
Author(s): Dittmar KD, Pratt WB
Number of Citations: 26
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to evaluate the effect of peptidic antiglucocorticoid on the interaction between glucocorticoid receptor and heat shock protein 90

Mol Endocrinol. 1997 Jun;11(7):962-72.
"Disruption of the glucocorticoid receptor assembly with heat shock protein 90 by a peptidic antiglucocorticoid."
Author(s): Dao-Phan HP, Formstecher P, Lefebvre P
Number of Citations: 1
(See PubMed article )
  Ms / Not Cited
MA3-011 was used in immunoprecipitation to study pp60src activation by 2,3,7,8-tetrachlorodibenzo-p-dioxin

Mol Pharmacol. 1997 Oct;52(4):667-75.
"2,3,7,8-Tetrachlorodibenzo-p-dioxin-induced activation of a protein tyrosine kinase, pp60src, in murine hepatic cytosol using a cell-free system."
Author(s): Blankenship A, Matsumura F
Number of Citations: 2
(See PubMed article )
  Ms / 1:200-1:500
MA3-011 was used in immunoprecipitation and western blot to investigate the role of tumor-derived, chaperone-rich cell lysate for dendritic cells and potent antitumor immunity activation

Blood. 2003 Jun 1;101(11):4485-91.
"Tumor-derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity."
Author(s): Zeng Y, Feng H, Graner MW, Katsanis E
Number of Citations: 1
(See PubMed article )
  Nhp / Not Cited
MA3-011 was used in immunoprecipitation to study the role of the beta-isoform of human glucocorticoid receptor

J Biol Chem. 1997 Oct 17;272(42):26659-64.
"Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor."
Author(s): Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström AC
Number of Citations: 6
(See PubMed article )
  Nhp / Not Cited
MA3-011 was used in immunoprecipitation to demonstrate mechanism of dominant negative activity of the human glucocorticoid receptor beta isoform

J Biol Chem. 1999 Sep 24;274(39):27857-66.
"The dominant negative activity of the human glucocorticoid receptor beta isoform. Specificity and mechanisms of action."
Author(s): Oakley RH, Jewell CM, Yudt MR, Bofetiado DM, Cidlowski JA
Number of Citations: 27
(See PubMed article )
  Nhp / Not Cited
MA3-011 was used in immunoprecipitation to study the mechanism for differential actions of various synthetic steroids on glucocorticoid receptor.

Mol Endocrinol. 2005 May;19(5):1110-24.
"The distinct agonistic properties of the phenylpyrazolosteroid cortivazol reveal interdomain communication within the glucocorticoid receptor."
Author(s): Yoshikawa N, Yamamoto K, Shimizu N, Yamada S, Morimoto C, Tanaka H
Number of Citations: 1
(See PubMed article )
  Nhp / 0
MA3-011 was used in immunoprecipitation and western blot to study teh role of LXXLL motifs in human glucocorticoid receptor function

J Steroid Biochem Mol Biol. 2006 Oct;101(2-3):106-17.
"Functional analysis of the LXXLL motifs of the human glucocorticoid receptor: association with altered ligand affinity."
Author(s): Dong DD, Jewell CM, Bienstock RJ, Cidlowski JA
Number of Citations: 1
(See PubMed article )
  Po / Not Cited
MA3-011 was used in immunoprecipitation and western blot to study the mechanism for the interaction of neuropeptide Y and Hsp90

Biochemistry. 2003 Nov 11;42(44):12972-80.
"Interaction of neuropeptide Y and Hsp90 through a novel peptide binding region."
Author(s): Ishiwatari-Hayasaka H, Maruya M, Sreedhar AS, Nemoto TK, Csermely P, Yahara I
Number of Citations: 1
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation and western blot to study the function of p23 during the process of receptor activation by hsp foldosome

J Biol Chem. 1995 Aug 11;270(32):18841-7.
"The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90."
Author(s): Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB
Number of Citations: 21
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to study the mechanisms for transcriptional activation by dioxin receptor and Arnt

Mol Cell Biol. 1994 Dec;14(12):8343-55.
"Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation."
Author(s): Whitelaw ML, Gustafsson JA, Poellinger L
Number of Citations: 17
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to investigate the interaction of different protein components of the heat shock protein heterocomplex

J Biol Chem. 1994 Apr 15;269(15):11155-61.
"Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex."
Author(s): Czar MJ, Owens-Grillo JK, Dittmar KD, Hutchison KA, Zacharek AM, Leach KL, Deibel MR Jr, Pratt WB
Number of Citations: 11
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to study the mechanisms of immunophilin-mediated protein targeting

J Biol Chem. 1996 Jun 7;271(23):13468-75.
"A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains."
Author(s): Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB
Number of Citations: 26
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to show HIF-1a is associated with the molecular chaperone hsp90 in vitro

Mol Cell Biol. 1996 Oct;16(10):5221-31.
"Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor."
Author(s): Gradin K, McGuire J, Wenger RH, Kvietikova I, fhitelaw ML, Toftgård R, Tora L, Gassmann M, Poellinger L
Number of Citations: 38
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to identify PP5 as an important component of glucocorticoid receptor-hsp90 complexes and investigate its functional properties

J Biol Chem. 1997 Jun 27;272(26):16224-30.
"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
Author(s): Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB
Number of Citations: 33
(See PubMed article )
  Rb / 1:35
MA3-011 was used in immunoprecipitation to demonstrate that chaperones play an important role in the regulation of general protein folding and of steroid receptor activation

J Biol Chem. 1998 Jun 12;273(24):15227-33.
"Active participation of Hsp90 in the biogenesis of the trimeric reovirus cell attachment protein sigma1."
Author(s): Gilmore R, Coffey MC, Lee PW
Number of Citations: 3
(See PubMed article )
  Rb / Not Cited
MA3-011 was used in immunoprecipitation to study the effect of XAP2 on dioxin receptor ubiquitination and subcellular localization.

J Biol Chem. 2000 Dec 29;275(52):41317-24.
"The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor."
Author(s): Kazlauskas A, Poellinger L, Pongratz I
Number of Citations: 1
(See PubMed article )
  Rt / 30 ug/time
MA3-011 was used in immunoprecipitation to study the role of an essential lysine residue in determining the hormone specificity of the mineralcorticoid receptor

Biochim Biophys Acta. 2002 Feb 13;1589(1):31-48.
"Modification of an essential amino group in the mineralocorticoid receptor evidences a differential conformational change of the receptor protein upon binding of antagonists, natural agonists and the synthetic agonist 11,19-oxidoprogesterone."
Author(s): Piwien-Pilipuk G, Kanelakis KC, Ghini AA, Lantos CP, Litwack G, Burton G, Galigniana MD
Number of Citations: 2
(See PubMed article )
  Vs / Not Cited
MA3-011 was used in immunoprecipitation to investigate the role of Hsp90 during the activation of the reverse transcriptase.

J Virol. 2000 Dec;74(24):11447-55.
"In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90."
Author(s): Hu J, Anselmo D
Number of Citations: 22
(See PubMed article )
ELISA
  Species / Dilution Summary
  Ms / 0.2 ug/ml
MA3-011 was used in ELISA to study the commonality of steroid-receptor-HSP90-immunophilin heterocomplex interactions with cytoplasmic dynein in plant and animal cells

Biochemistry. 2002 Apr 30;41(17):5581-7.
"All of the protein interactions that link steroid receptor.hsp90.immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells."
Author(s): Harrell JM, Kurek I, Breiman A, Radanyi C, Renoir JM, Pratt WB, Galigniana MD
Number of Citations: 8
(See PubMed article )
  Rt / Not Cited
MA3-011 was used in ELISA to study the binding menchanism of hsp90 to the glucocorticoid receptor

J Biol Chem. 1998 May 29;273(22):13918-24.
"Binding of hsp90 to the glucocorticoid receptor requires a specific 7-amino acid sequence at the amino terminus of the hormone-binding domain."
Author(s): Xu M, Dittmar KD, Giannoukos G, Pratt WB, Simons SS Jr
Number of Citations: 3
(See PubMed article )
Blocking Assay
  Species / Dilution Summary
  Vs / Not Cited
MA3-011 was used in blocking/activating experiment to investigate the role of Hsp90 on the activity of a hepatitis B virus reverse transcriptase

Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1060-4.
"Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase."
Author(s): Hu J, Seeger C
Number of Citations: 66
(See PubMed article )
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