|Application ||WB, E|
|Other Accession||P34058, P11499, Q4R4T5, P08238, O57521, Q76LV1, P82995, P30946, O02705, P07901, Q4R4P1, P46633, P11501, Q76LV2, Q58FF7, Q9GKX7, Q9GKX8|
|Reactivity||Human, Mouse, Rat|
|Predicted||Bovine, Chicken, Hamster, Horse, Monkey, Pig, Rabbit, Zebrafish|
|Calculated MW||84660 Da|
|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||This HSP90 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 644-677 amino acids from the C-terminal region of human HSP90.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP90 Antibody (C-term) is for research use only and 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 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11274138, PubMed:11276205, PubMed:15577939, PubMed:15937123, PubMed:27353360).|
|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.
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.
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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