SDS-PAGE
(The purity was determined to be >90% by densitometry . Approx. MW 94 kDa)
HSP90 alpha recombinant protein
HSP90 alpha recombinant protein
Stability: 1yr at -70 degree C from date of shipment.
SDS-PAGE
(The purity was determined to be >90% by densitometry . Approx. MW 94 kDa)
SDS-PAGE
(The purity was determined to be >90% by densitometry . Approx. MW 94 kDa)
Scientific Background: 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 (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. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2).
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.
NCBI and Uniprot Product Information
NCBI Description
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]
Uniprot Description
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.
Research Articles on HSP90 alpha
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Product Notes
The HSP90 alpha hsp90aa1 (Catalog #AAA515368) is a Recombinant Protein produced from Sf9 insect cells and is intended for research purposes only. The product is available for immediate purchase. The tag for this protein is 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. AAA Biotech's HSP90 alpha can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB). Researchers should empirically determine the suitability of the HSP90 alpha hsp90aa1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "HSP90 alpha, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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