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Antigenic Specificity | HSP90 alpha/beta |
Clone | polyclonal |
Host Species | Llama |
Reactive Species | human, mouse, rat |
Isotype | n/a |
Format | APC-Cy7 conjugate |
Size | 0.1 mg |
Concentration | 1 mg/ml |
Applications | Western Blot (WB), ELISA (EIA) |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Detects 90 kDa. Detects HSP90 alpha and beta. HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and |
Immunogen | Immunogen: Synthetic human HSP90 alpha full length protein |
Other Names | [Llama Human HSP90 alpha/beta; Heat shock 84 kDa; Heat shock 86 kDa; Heat shock protein HSP 90-alpha; Heat shock protein HSP 90-beta; HSP 84; HSP 86; HSP 90; HSP84; HSP86; HSP90A; HSP90AA1; HSP90AB1; HSP90B; HSPC1; HSPC2; HSPCA; HSPCB; LAP-2; Lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38; HSP90 alpha/beta] |
Gene, Accession # | [HSP90AB1], Gene ID: 3320, NCBI: NP_001017963.2, UniProt: P07900 |
Catalog # | MBS8005183 |
Price | $530 |
Order / More Info | HSP90 alpha/beta Antibody from MYBIOSOURCE INC. |
Product Specific References | 1. Nemoto, T. et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami Y, et al. (1991), J.Biol Chem. 266: 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8: S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228: 111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18: 306-360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420-434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324-8328. 10. Kishimoto J, et al. (2005). Cell Stress and Chaperones. 10 (4): 296-311. |