Name :
Recombinant Human Hsp90 alpha Protein, HPLC-verified
Biological Activity :
Background :
Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with ‘client proteins’, including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_005339.3
NCBI Gene ID :
Synonyms :
Synonyms :
heat shock protein 90kDa alpha (cytosolic), class A member 1
Amino Acid Sequence :
Molecular Weight :
The recombinant human HSP90 (aa 535-732) consisting of 200 amino acids and has a calculated molecular mass of 22.6 kDa. It migrates as an 24 kDa band in SDS-PAGE under reducing conditions.
Purity :
≥ 90 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the human HSP90 isoform 2 (NP_005339.3) C-terminal segment, corresponding to amino acid sequence (Glu 535-Asp 732) was expressed and purified, with two additonal aa (Gly & Pro) at the N terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
EL52 Protein, Human; HSP86 Protein, Human; Hsp89 Protein, Human; HSP89A Protein, Human; Hsp90 Protein, Human; HSP90A Protein, Human; HSP90N Protein, Human; HSPC1 Protein, Human; HSPCA Protein, Human; HSPCAL1 Protein, Human; HSPCAL4 Protein, Human; HSPN Protein, Human; LAP-2 Protein, Human; LAP2 Protein, Human Hsp90 alpha 背景信息 Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with ‘client proteins’, including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.
References & Citations :
Pearl LH, et al. (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 410(3): 439-53.Hahn JS. (2009) The Hsp90 chaperone machinery: from structure to drug development. BMB Rep. 42(10): 623-30.Holzbeierlein JM, et al. (2010) Hsp90: a drug target? Curr Oncol Rep. 12(2): 95-101.Trepel J, et al. (2010) Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer. 10(8): 537-49.
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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