HSP90AA1 Mouse Monoclonal Antibody [Clone ID: Hyb-K41009]

Specifications

Product Data
Clone Name	Hyb-K41009
Applications	IHC, WB
Recommend Dilution	1ug/ml was sufficient for detection of hsp90alpha by Western Blot in 20ug of HeLa lysate.
Reactivity	Human (Alpha specific)
Host	Mouse
Clonality	Monoclonal
Immunogen	Recombinant human Hsp90alpha; Specificity mapped to amino acids 604-731
Formulation	PBS pH7.2, 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 A member 1
Database Link	NP_001017963 Entrez Gene 3320 Human UniProt ID P07900
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 (1-2% 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	Detects 90kDa proteins corresponding to the molecular mass of Hsp90a.
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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