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Name :
Recombinant Human HSP90AA1, His-tagged

Specification :
| Cat. No. : HSP90AA1-1461H | Description : HSP90α is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins. HSP90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL and mutated p53. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2. | Source : Sf9 insect cells using baculovirus | Sequence : Full-length. | Applications : Western Blot. | Storage And Stability : Store product at -70℃. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Gene Information :
| Gene Name : HSP90AA1 heat shock protein 90kDa alpha (cytosolic), class A member 1 [ Homo sapiens ] | Synonyms : HSP90AA1; heat shock protein 90kDa alpha (cytosolic), class A member 1; Hsp90 α; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; FLJ31884; HSP90AA1; Renal carcinoma antigen NY-REN-38; heat shock 90kD protein 1, alpha; heat shock 90kD protein 1, alpha-like 4; heat shock 90kD protein, alpha-like 4; heat shock 90kDa protein 1, alpha; heat shock protein 90kDa alpha (cytosolic), class A member 1 | Gene ID : 3320 | mRNA Refseq : NM_001017963 | Protein Refseq : NP_001017963 | MIM : 140571 | UniProt ID : Q86SX1 | Chromosome Location : 14q32.33 | Pathway : Antigen processing and presentation; Prostate cancer; Cell Cycle, Mitotic; Metabolism of nitric oxide | Function : ATP binding; TPR domain binding; TPR domain binding; nitric-oxide synthase regulator activity; nucleotide binding; protein homodimerization activity; unfolded protein binding

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Author: Cholesterol Absorption Inhibitors