Mouse Hsp90 alpha Monoclonal Antibody | anti-Hsp90 alpha antibody

Anti-Hsp90 alpha Monoclonal Antibody

Cat. Num. AAA190539

• Gene Names: HSP90AA1; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; FLJ31884
• Reactivity: Human, mouse, rat
• Applications: ELISA, Immunoblot, Immunocytochemistry, Immunohistochemistry, Western Blot
• Synonyms: Hsp90 alpha; Monoclonal Antibody; Anti-Hsp90 alpha Monoclonal Antibody; anti-Hsp90 alpha antibody

• Host: Mouse
• Reactivity: Human, mouse, rat
• Clonality: Monoclonal
• Isotype: IgG1
• Clone Number: 2G5.G3
• Specificity: Hsp90 alpha; This antibody recognizes human, mouse, and rat Hsp90alpha. Other species have not been tested. It does not crossreact with Hsp90beta in ELISA.
• Form/Format: 100ug Protein G-purified antibody in PBS, pH 7.4.

• Applicable Applications for anti-Hsp90 alpha antibody: ELISA; Immunoblot; Immunohistochemistry; Immunocytochemistry
• Application Notes: Immunoblotting: use at 0.5-1ug/ml. A band of ~90 kDa is detected. ELISA Immunohistochemistry/ Immunocytochemistry Imunoprecipitation. User should determine optimal concentrations for their application. Positive control: HeLa cell lysate.
• Antigen: Human Hsp90 alpha
• Preservative: None.
• Dilution Instructions: Dilute in PBS or medium which is identical to that used in the assay system.
• Preparation and Storage: This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

Related Product Information for anti-Hsp90 alpha antibody

Hsp90 is an abundantly and ubiquitously expressed heat shock protein found in all eukaryotic cells. It exists in two principal forms, alpha and beta, which share 85% sequence homology. Both forms are expressed in the cytosol. Hsp90alpha exists primarily as a homodimer while Hsp90beta exists mainly as a monomer. Hsp90 plays a role in folding, assembly, maturation, and stabilization of specific proteins as a key component of a chaperone complex. Most of the Hsp90-regulated proteins that have been identified are involved in cell signaling; kinases, v-Src, Wee1, c-Raf, and p53 are some examples. When bound to ATP, Hsp90 interacts with cochaperones Cdc37, p23, and various immunophilin-like proteins to form complexes that stabilize and protect target proteins from proteasomal degradation.

NCBI and Uniprot Product Information

• NCBI GI #: 154146191
• NCBI GeneID: 3320
• NCBI Accession #: NP_005339.3
• NCBI GenBank Nucleotide #: NM_005348.3
• UniProt Accession #: P07900; Q2PP14; Q5CAQ6; Q5CAQ7; Q9BVQ5; A8K500; B3KPJ9; O75322; Q2VPJ6; Q86SX1; Q86U12; Q8TBA7; Q96HX7
• Molecular Weight: 84,660 Da
• NCBI Official Full Name: heat shock protein HSP 90-alpha isoform 2
• NCBI Official Synonym Full Names: heat shock protein 90kDa alpha (cytosolic), class A member 1
• NCBI Official Symbol: HSP90AA1
• NCBI Official Synonym Symbols: HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; FLJ31884
• 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; heat shock 90kD protein 1, alpha-like 4
• UniProt Protein Name: Heat shock protein HSP 90-alpha
• UniProt Gene Name: HSP90AA1
• UniProt Synonym Gene Names: HSP90A; HSPC1; HSPCA
• UniProt Entry Name: HS90A_HUMAN

NCBI Description

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]

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: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 14q32.33

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

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; TPR domain binding; ATPase activity; unfolded protein binding; nitric-oxide synthase regulator 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; nitric oxide metabolic process; protein import into mitochondrial outer membrane; response to unfolded protein; mitochondrial transport; innate immune response; protein refolding; mitotic cell cycle; regulation of nitric-oxide synthase activity; chaperone-mediated protein complex assembly; vascular endothelial growth factor receptor signaling pathway; G2/M transition of mitotic cell cycle