Rabbit Heat Shock Protein 90, Co-chaperone p23 Polyclonal Antibody | anti-HSP90AA1 antibody

Heat Shock Protein 90, Co-chaperone p23 (HSP90, Telomerase-Binding Protein p23, Progesterone Receptor Complex p23)

Cat. Num. AAA615877

• Gene Names: HSP90AA1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot
• Purity: Purified; Purified by ammonium sulfate precipitation.
• Synonyms: Heat Shock Protein 90; Co-chaperone p23; Polyclonal Antibody; Co-chaperone p23 (HSP90; Telomerase-Binding Protein p23; Progesterone Receptor Complex p23); Anti -Heat Shock Protein 90; anti-HSP90AA1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Specificity: Detects an ~23kD protein, corresponding to the apparent molecular mass of p23 on SDS-PAGE Western Blots, in samples from human, mouse and rat origins.
• Purity/Purification: Purified; Purified by ammonium sulfate precipitation.
• Form/Format: Supplied as a liquid in PBS, 0.1mM PMSF, 50% glycerol.

• Applicable Applications for anti-HSP90AA1 antibody: Western Blot (WB)
• Application Notes: Suitable for use in Western Blotting.; Dilution: Western Blotting: 1:5000
• Immunogen: Human p23 expressed in E. coli.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.; Sold under license from Geron

Western Blot (WB)

(Western blot analysis of p23: Lane 1: MW, Lane 2: p23, Lane 3: HeLa (Heat Shocked), Lane 4: mouse testes, and Lane 5: rat testes probed with MBS615877)

Related Product Information for anti-HSP90AA1 antibody

p23 is a 23kD ubiquitous, highly conserved co-chaperone for Hsp90. p23 binds Hsp90 and participates in the folding of a number of cell regulatory proteins (1). p23 is thought to modulate Hsp90 activity in the last stages of the chaperoning pathway and only binds Hsp90 that is in turn bound to ATP which stablizes this state of Hsp90 (1,4). Hsp90 binds both ATP and p23 at its N-terminus (3). p23 was first identified as a component of hsp90 complexes with the progesterone receptor. It has since been observed in hsp90 complexes with such diverse proteins as Fes kinase, Hsf1, telomerase, and hepadnavirus polymerase. p23 has been shown to stabilize hsp90 complexes with progesterone receptor (PR) or glucocorticoid receptor (GR). Although not strictly required for the interaction of these client proteins with hsp90, p23 dramatically increases the proportion of PR or GR in a mature complex able to bind hormone. It has also been indicated that p23 may have a role in the turnover or dissociation of GR-hsp90 complexes. p23 also has the ability to function as a passive chaperone in vitro because it can prevent the aggregation of denatured proteins. In addition, cellular studies indicate that it can modulate the activities of nuclear receptors even after they have been activated and presumed to be dissociated from hsp90 (4). p23 is also a prominent target in leukemic cell apoptosis. In leukemic cells, geldanamycin enhanced p23 cleavage by rendering p23 more susceptible to caspases-3 and -7 and by enhancing chemotherapy-induced caspase activation. p23 is cleaved at Asp142 and Asp145 by caspase-7 and caspase-3, which results in a 17kD fragment. These findings underscore the importance of the Hsp90-complex in antileukemic treatment, and suggest that p23 may have a role in survival signalling (2).

Product Categories/Family for anti-HSP90AA1 antibody

Antibodies; Abs to Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 92090606
• NCBI GeneID: 3320
• UniProt Accession #: P07900; Q2PP14; Q5CAQ6; Q5CAQ7; Q9BVQ5; A8K500; B3KPJ9
• Molecular Weight: 84,660 Da
• NCBI Official Full Name: Heat shock protein HSP 90-alpha
• NCBI Official Synonym Full Names: heat shock protein 90kDa alpha (cytosolic), class A member 1
• NCBI Official Symbol: HSP90AA1
• NCBI Official Synonym Symbols: EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4
• NCBI Protein Information: heat shock protein HSP 90-alpha; HSP 86; heat shock 86 kDa; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; renal carcinoma antigen NY-REN-38; heat shock 90kD protein, alpha-like 4; epididymis luminal secretory protein 52; heat shock 90kD protein 1, alpha-like 4
• UniProt Protein Name: Heat shock protein HSP 90-alpha
• Protein Family: Heat shock protein
• UniProt Gene Name: HSP90AA1
• UniProt Synonym Gene Names: HSP90A; HSPC1; HSPCA; HSP 86; HSP86
• UniProt Entry Name: HS90A_HUMAN

NCBI Description

The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

Uniprot Description

HSP90A: a molecular chaperone of the heat shock protein 90 family. Has ATPase activity. Known to interact with a wide variety of proteins including steroid hormone receptors, neuropeptide Y, FKBP51/54, and FKBP52. G protein-coupled receptor kinases are stabilized by interacting with HSP 90. Hsp70 and Hsp90 promote tau solubility and tau binding to microtubules, reducing insoluble tau phosphorylation of tau.

Protein type: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 14q32.33

Cellular Component: nucleoplasm; mitochondrion; membrane; cytoplasm; melanosome; extracellular region; plasma membrane; nucleus; cytosol

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; TPR domain binding; nitric-oxide synthase regulator activity; unfolded protein binding; ATPase activity; nucleotide binding; ATP binding

Biological Process: axon guidance; receptor-mediated endocytosis; positive regulation of nitric oxide biosynthetic process; organelle organization and biogenesis; signal transduction; protein import into mitochondrial outer membrane; nitric oxide metabolic process; response to unfolded protein; mitochondrial transport; innate immune response; protein refolding; regulation of nitric-oxide synthase activity; mitotic cell cycle; chaperone-mediated protein complex assembly; G2/M transition of mitotic cell cycle; vascular endothelial growth factor receptor signaling pathway