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HSP90A Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - HSP90A Antibody AP50205
    Western blot analysis of extracts from NIH/3T3 cells (Lane 1), A549 cells (Lane 2) and Hela cells (Lane 3), using HSP90A Antibody. The lane on the left is treated with synthesized peptide.
  • 3 - HSP90A Antibody AP50205
    Immunofluorescence analysis of NIH/3T3 cells, using HSP90 cyto antibody .
  • 2 - HSP90A Antibody AP50205
    Immunohistochemical analysis of paraffin-embedded human lung carcinoma tissue using HSP90 cyto antibody .
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Product info
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, IF, IHC
Primary Accession P07900
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality polyclonal
Calculated MW 85,98 KDa
Additional info
Gene ID 3320
Other Names Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP90AA1, HSP90A, HSPC1, HSPCA
Dilution WB~~ 1:1000
IF~~1:100
IHC~~1:50-1:100
Format Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage Conditions-20℃
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.

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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