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Hsp90 alpha Antibody

Purified Mouse Monoclonal Antibody (Mab)

     
  • 1 - Hsp90 alpha Antibody AP52868
    Western blot detection of Hsp90 alpha in R Brain,Jurkat,CHO-K1,COS7,C6,3T3 and Hela cell lysates using Hsp90 alpha mouse mAb (1:1000 diluted). Predicted band size:90KDa. Observed band size:90KDa.
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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
Primary Accession P07900
Reactivity Human, Mouse
Host Mouse
Clonality Monoclonal
Isotype IgG1
Calculated MW 90 KDa
Additional Information
Gene ID 3320
Other Names Heat shock 86 kDa; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; heat shock protein 90kDa alpha (cytosolic), class A member 2; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 86; HSP 86; HSP 86; HSP86; Hsp89; HSP89A; HSP90A; HSP90AA1; HSP90ALPHA; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL3; HSPCAL4; HSPN; LAP2; Renal carcinoma antigen NY REN 38; Renal carcinoma antigen NY-REN-38.
Dilution WB~~1:1000
Format Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.02% sodium azide,1mg/ml BSA and 50% glycerol.
Storage Store at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name HSP90AA1
Synonyms HSP90A, HSPC1, HSPCA
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 that is linked to its ATPase activity which is essential for its chaperone 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:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). 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 (PubMed:29127155). 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 (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). 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 (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1- mediated inhibition of TGF-beta signaling via inhibition of STUB1- mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
Cellular Location Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV
Research Areas

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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.

REFERENCES

Soeda E.,et al.Nucleic Acids Res. 17:7108-7108(1989).
Yamazaki M.,et al.Agric. Biol. Chem. 54:3163-3170(1990).
Hickey E.,et al.Mol. Cell. Biol. 9:2615-2626(1989).
Chen B.,et al.Genomics 86:627-637(2005).
Ota T.,et al.Nat. Genet. 36:40-45(2004).

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