|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|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP9085b was selected from the C-term region of human HSPCA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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. 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.|
|Cellular Location||Cytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
HSPCA are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSPCA proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress.
Ni,L., et.al., Mol. Cell. Biol. 30 (5), 1243-1253 (2010)Dempsey,N.C., et.al., J. Leukoc. Biol. 87 (3), 467-476 (2010)
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