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HSP90β Monoclonal Antibody(M2)

     
  • 1 - HSP90β Monoclonal Antibody(M2) AP63371
    Immunohistochemical analysis of paraffin-embedded Human-Tonsil tissue. 1,HSP90β Monoclonal Antibody(M2) was diluted at 1:200(4°C,overnight). 2, Sodium citrate pH 6.0 was used for antibody retrieval(>98°C,20min). 3,Secondary antibody was diluted at 1:200(room tempeRature, 30min). Negative control was used by secondary antibody only.
  • 14 - HSP90β Monoclonal Antibody(M2) AP63371
    Immunohistochemical analysis of paraffin-embedded Rat-heart tissue. 1,HSP90β Monoclonal Antibody(M2) was diluted at 1:200(4°C,overnight). 2, Sodium citrate pH 6.0 was used for antibody retrieval(>98°C,20min). 3,Secondary antibody was diluted at 1:200(room tempeRature, 30min). Negative control was used by secondary antibody only.
  • 14 - HSP90β Monoclonal Antibody(M2) AP63371
    Immunohistochemical analysis of paraffin-embedded Mouse-testis tissue. 1,HSP90β Monoclonal Antibody(M2) was diluted at 1:200(4°C,overnight). 2, Sodium citrate pH 6.0 was used for antibody retrieval(>98°C,20min). 3,Secondary antibody was diluted at 1:200(room tempeRature, 30min). Negative control was used by secondary antibody only.
  • 14 - HSP90β Monoclonal Antibody(M2) AP63371
    Immunofluorescence analysis of Mouse-spleen tissue. 1,HSP90β Monoclonal Antibody(M2)(red) was diluted at 1:200(4°C,overnight). 2, Cy3 labled Secondary antibody was diluted at 1:300(room temperature, 50min).3, Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B
  • 14 - HSP90β Monoclonal Antibody(M2) AP63371
    Immunofluorescence analysis of Rat-lung tissue. 1,HSP90β Monoclonal Antibody(M2)(red) was diluted at 1:200(4°C,overnight). 2, Cy3 labled Secondary antibody was diluted at 1:300(room temperature, 50min).3, Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B
  • 1 - HSP90β Monoclonal Antibody(M2) AP63371
    Western blot analysis of 1) Hela, 2) Mouse Brain tissue, 3) Rat Brain tissue, diluted at 1:2000.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IF
Primary Accession P08238
Reactivity Human, Mouse, Rat
Host Mouse
Clonality Monoclonal
Calculated MW 83264 Da
Additional Information
Gene ID 3326
Other Names HSP90AB1; HSP90B; HSPC2; HSPCB; Heat shock protein HSP 90-beta; HSP 90; Heat shock 84 kDa; HSP 84; HSP84
Dilution WB~~WB: 1:1000-3000 IF 1:200 IHC 1:50-300
IHC-P~~WB: 1:1000-3000 IF 1:200 IHC 1:50-300
IF~~1:50~200
Format PBS, pH 7.4, containing 0.09% (W/V) sodium azide as Preservative and 50% Glycerol.
Storage Conditions-20℃
Protein Information
Name HSP90AB1 (HGNC:5258)
Function Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1- mediated inhibition of TGF-beta signaling via inhibition of STUB1- mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
Cellular Location Cytoplasm. Melanosome Nucleus. Secreted. Cell membrane. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065) Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co- chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).

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