HSP90AB1 Mouse Monoclonal Antibody [Clone ID: AC-16]

Specifications

Product Data
Clone Name	AC-16
Applications	IHC
Recommend Dilution	1ug/ml was sufficient for detection of hsp90 by Western Blot in 20ug of HeLa lysate.
Reactivity	Human, Rabbit, Rat, Mouse, Chicken, Achyla, Wheat Germ, Sf9 cell line
Host	Mouse
Clonality	Monoclonal
Immunogen	Heat shock protein 900 from the water mold Achyla ambisexualis
Formulation	PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration	lot specific
Purification	Protein G Purified
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Gene Name	heat shock protein 90kDa alpha family class B member 1
Database Link	NP_031381 Entrez Gene 15516 MouseEntrez Gene 301252 RatEntrez Gene 3326 Human UniProt ID P08238
Background	Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex . Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling . The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function .
Synonyms	D6S182; HSP84; HSP90B; HSPC2; HSPCB
Note	This antibody is reactive with both the constitutive and the inducible form of Hsp90. It does not bind to the native form and does not recognize Hsp90 from E.coli or yeast.
Reference Data
Protein Families	Druggable Genome, Stem cell - Pluripotency
Protein Pathways	Antigen processing and presentation, NOD-like receptor signaling pathway, Pathways in cancer, Progesterone-mediated oocyte maturation, Prostate cancer

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