Text Size:AAA

Cynomolgus monkey HSP90AA1 Gene cDNA clone plasmid

DatasheetSpecific ReferencesReviewsRelated ProductsProtocols
HSP90AA1cDNA Clone Product Information
Gene_bank_ref_id:unsubmitted
RefSeq ORF Size:2202bp
cDNA Description:Full length Clone DNA of Macaca mulatta heat shock protein 90kDa alpha (cytosolic), class A member 1.
Gene Synonym:HSP90AA1
Species:Cynomolgus
Vector:pGEM-T Vector
Plasmid:pGEM-cynoHSP90AA1
Restriction Site:
Tag Sequence:
Sequence Description:Identical with NM_001195667.1 [ Macaca mulatta (Rhesus monkey) ]: 930T/C, 1362A/T and 2097C/T not causing the amino acid variation. Please check the sequence information before order.
Sequencing primers:SP6 and T7 or M13-47 and RV-M
Promoter:
Application:
Antibiotic in E.coli:
Antibiotic in mammalian cell:
Shipping_carrier:Each tube contains lyophilized plasmid.
Storage:The lyophilized plasmid can be stored at room temperature for three months.
Other HSP90AA1 Protein Products
pGEM-T Vector Information

The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.

pGEM-T Simple Usage Suggestion:

The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.

Vector Sequence Download
Related Products
Product nameProduct name
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 in 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 remodelling 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 provides protection to 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
  • 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.
  • Size / Price
    Catalog:CG90401-G
    List Price: JPY12130.00  (Save JPY0.00)
    Price:JPY12130.00      [How to order]
    AvailabilityIn Stock
    Images
      Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"