HSP90AA1 Mouse Monoclonal Antibody [Clone ID: 4F3.E8]

Specifications

Product Data
Clone Name	4F3.E8
Applications	IF, WB
Recommend Dilution	WB: 1:2000
Reactivity	Human, Mouse, Rat
Host	Mouse
Clonality	Monoclonal
Immunogen	Recombinant Human Hsp90 purified from E.coli
Formulation	PBS pH7.2, 50% glycerol
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 A member 1
Database Link	NP_001017963 Entrez Gene 15519 MouseEntrez Gene 299331 RatEntrez Gene 3320 Human UniProt ID P07900
Background	HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms and , which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment . Despite the similarities, HSP90 exists predominantly as a homodimer while HSP90 exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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	EL52; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP-2; LAP2
Note	This antibody detects both a and β forms of Hsp90 equally well.
Reference Data
Protein Families	Druggable Genome
Protein Pathways	Antigen processing and presentation, NOD-like receptor signaling pathway, Pathways in cancer, Progesterone-mediated oocyte maturation, Prostate cancer

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