protein

HSP90 alpha recombinant protein

MBS515368

0.02 mg

260 USD

Recombinant Protein

HSP90 alpha recombinant protein

HSP90 alpha

HSP90AA1; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP90N; HSPCAL1; HSPCAL4; FLJ31884; HSP90alpha Protein; HSP90a Protein

Homo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 2, mRNA; Heat shock protein HSP 90-alpha; 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; heat shock protein 90kDa alpha (cytosolic), class A member 1; Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38

HSP90 alpha

HSP90AA1; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP90N; HSPCAL1; HSPCAL4; FLJ31884

HSP90AA1; HSP90AA1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; HSP90A; HSPC1; HSPCA; HSP 86; HSP86

HS90A_HUMAN

Sf9 insect cells

3366

>90%

50mM MOPS, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

0.2ug/ul

Store product at -70 degree C. 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. Stability: 1yr at -70 degree C from date of shipment.

Western Blot (WB)

Type: Recombinant Fusion Protein. Species: Human. Tag Information: His tag. Expression System: Sf9 insect cells using baculovirus. Source Note: Recombinant full length human HSP90alpha was expressed by baculovirus in Sf9 insect cells. Accession Number: NM 005348

Cell Stress & Chaperone Proteins; Signaling Proteins - Cell Stress & Chaperone Proteins

Recombinant full-length human HSP90 alpha was expressed by baculovirus in Sf9 insect cells using a C-terminal His tag. Scientific Background: HSP90 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 (1). 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. HSP90 is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2).

1. Csermely, P. et al: The 90-kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol Ther. 1998 Aug;79(2):129-68. 2. Eustace, B. K. et al:Functional proteomic screens reveal an essential extracellular role for hsp90-alpha in cancer cell invasiveness. Nature Cell Biol. 6: 507-514, 2004.

154146190

NP_005339.3

NM_005348

P07900

~94 kDa

AhR Pathway (755436); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Axon Guidance Pathway (105688); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Centrosome Maturation Pathway (105807); Class I PI3K Signaling Events Pathway (138022); Class I PI3K Signaling Events Mediated By Akt Pathway (138020)

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]

Function: 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. Ref.15 Ref.22 Ref.28. Subunit structure: Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.40 Ref.43 Ref.50 Ref.51. Subcellular location: Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.42. Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1. Post-translational modification: ISGylated. Ref.41S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. Sequence similarities: Belongs to the heat shock protein 90 family.

0.02 mg

260 USD

0.05 mg

415