Hsp90 alpha cDNA ORF Clone, Mouse, N-HA tag General Information
Full length Clone DNA of Mouse heat shock protein 90, alpha (cytosolic), class A member 1 with N terminal HA tag.
Enhanced CMV promoter
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Antibiotic in Mammalian cell
Stable or Transient mammalian expression
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
Hsp90 alpha cDNA ORF Clone, Mouse, N-HA tag Alternative Names
86kDa cDNA ORF Clone, Mouse;89kDa cDNA ORF Clone, Mouse;AL024080 cDNA ORF Clone, Mouse;AL024147 cDNA ORF Clone, Mouse;hsp4 cDNA ORF Clone, Mouse;Hsp86-1 cDNA ORF Clone, Mouse;Hsp89 cDNA ORF Clone, Mouse;Hsp90 cDNA ORF Clone, Mouse;Hspca cDNA ORF Clone, Mouse
Hsp90 alpha Background Information
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.
heat shock protein 90kDa alpha (cytosolic), class A member 1
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.