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小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体)

  • other Green fluorescent protein / GFP Gene Plasmid Map 5613
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小鼠 HSP90AA1 cDNA Clone产品信息
NCBI注册码:BC046614.1
参考序列ORF长度:2202bp
cDNA基因描述:Full length Clone DNA of Mus musculus heat shock protein 90, alpha (cytosolic), class A member 1.
分子别称:hsp4, 86kDa, 89kDa, Hsp89, Hsp90, Hspca, Hsp86-1, AL024080, AL024147
分子种属:Mouse
载体:pCMV3-untagged
质粒:pCMV3-mHSP90AA1
限制性酶切位点:KpnI + XbaI(6.1kb+2.2kb)
Tag序列:
序列信息:Identical with the Gene Bank Ref. ID sequence.
测序引物:T7(TAATACGACTCACTATAGGG) BGH(TAGAAGGCACAGTCGAGG)
( We provide with HSP90AA1 qPCR primers for gene expression analysis, MP201868 )
启动子:Enhanced CMV mammalian cell promoter
Application:Stable or Transient mammalian expression
抗生素(大肠杆菌):Ampicillin
抗生素(哺乳动物细胞):Hygromycin
运输方式:Each tube contains lyophilized plasmid.
储存方法:The lyophilized plasmid can be stored at room temperature for three months.
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研究背景

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.

参考资料
  • 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.
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    货号: MG51995-UT
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