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HSP90AA1 recombinant protein :: Heat shock protein HSP 90-alpha (HSP90AA1) Recombinant Protein

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Catalog # MBS1257521
Unit / Price
Scan QR to view Datasheet
  0.01 mg (Baculovirus)  /  $235 +1 FREE 8GB USB
  0.02 mg (Baculovirus)  /  $355 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $680 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $940 +1 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $1,325 +1 FREE 8GB USB
  1 mg (Baculovirus)  /  $1,845 +2 FREE 8GB USB
SDS-Page
Product Name

Heat shock protein HSP 90-alpha (HSP90AA1), Recombinant Protein

Popular Item
Full Product Name

Recombinant Pig Heat shock protein HSP 90-alpha (HSP90AA1), partial

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
MBS1257521 COA
Sequence Positions
222-367
Sequence
VEKERDKEVS DDEAEEKEDK EEEKEKEEKE SEDKPEIEDV GSDEEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN IKLYVR
3D Structure
ModBase 3D Structure for O02705
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
>85% (SDS-PAGE) (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Species
Sus scrofa (Pig)
Storage Buffer
Tris-based buffer, 50% glycerol
Tag Information
Tag type will be determined during the manufacturing process
Preparation and Storage
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of HSP90AA1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

HSP90AA1 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for HSP90AA1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Related Accession #
Molecular Weight
84,775 Da
NCBI Official Full Name
heat shock protein HSP 90-alpha
NCBI Official Symbol
HSP90AA1  [Similar Products]
NCBI Official Synonym Symbols
HSP90; Hspca
  [Similar Products]
NCBI Protein Information
heat shock protein HSP 90-alpha
UniProt Protein Name
Heat shock protein HSP 90-alpha
Protein Family
UniProt Gene Name
HSP90AA1  [Similar Products]
UniProt Synonym Gene Names
HSP90A; HSPCA  [Similar Products]
UniProt Comments for HSP90AA1
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 which is essential for its chaperone 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Interacts with HECTD1 (via N-terminus) ().
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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