Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband®

Heat shock protein HSP 90-alpha?is a?protein?that in humans is encoded by the?HSP90AA1?gene. The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A) . Complemented by the constitutively expressed paralog Hsp90B which shares over 85% amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation.

Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSP 86; HSP86; Lipopolysaccharide-associated protein 2; LAP-2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38; HSP90AA1; HSP90A, HSPC1, HSPCA

E.coli-derived human Hsp90 alpha recombinant protein (Position: P2-V365) . Human Hsp90 alpha shares 99% amino acid (aa) sequence identity with both mouse and rat Hsp90 alpha.

Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non- proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle) . .

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. .

1. Csermely P, Schnaider T, Soti C, Prohászka Z, Nardai G (August 1998) . The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79 (2) : 129–68. 2. Sollars, V., Lu, X., Xiao, L., Wang, X., Garfinkel, M. D., Ruden, D. M. Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution. Nature Genet. 33: 70-74, 2003. 3. Solit, D. B., Zheng, F. F., Drobnjak, M., Munster, P. N., Higgins, B., Verbel, D., Heller, G., Tong, W., Cordon-Cardo, C., Agus, D. B., Scher, H. I., Rosen, N. 7-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin. Cancer Res. 8: 986-993, 2002.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.