Hsp90 alpha qPCR Primer Pairs, Mouse 基本信息
Target Details
Product Details
Component:
1 vial of lyophilized qPCR primer mix (1 nmol each primer, sufficient for 200 numbers of 25 μl reactions).
QPCR Primer Description:
Verified forward and reverse primers for analyzing the quantitative expression of gene.
Application & Quality
应用:
SYBR® Green-based quantitative real-time PCR (qPCR).
质控:
The primer mix has been verified to generate satisfactory qPCR data on Roche Applied-science LightCycler® 480 Ⅱ.
储存 & 运输
运输:
Lyophilized qPCR primer mix is shipped at ambiente temperatura
储存:
The lyophilized product is stable for one year from date of receipt when stored at -20℃. The suspended product is stable for six months from date of receipt when stored at -20℃.
***Sino biological qEASY qPCR primer pairs are used for SYBR Green-based real-time RT-PCR, The primers are designed by using SBI's proprietary primer design algorithm. Our primer collection covers the entire human genomes. It can be widely applied in the quantitative analysis of gene expression.***
Features and Advantages
Unique Primer Design
To avoid genomic DNA amplification, at least one primer is designed crosses the junction of exons according to the conserved region of a specific gene with all variants.
Strict Validation Process
Confirmed in positive organizations; screened the primer with high specificity and high sensitivity.
Uniform PCR conditions, Saving time and cost
~100% amplification curve, ensuring the accuracy of the RNA quantitative
Hsp90 alpha qPCR Primer Pairs, Mouse Alternative Names
86kDa qPCR Primer Pairs, Mouse;89kDa qPCR Primer Pairs, Mouse;AL024080 qPCR Primer Pairs, Mouse;AL024147 qPCR Primer Pairs, Mouse;hsp4 qPCR Primer Pairs, Mouse;Hsp86-1 qPCR Primer Pairs, Mouse;Hsp89 qPCR Primer Pairs, Mouse;Hsp90 qPCR Primer Pairs, Mouse;Hspca qPCR Primer Pairs, Mouse
Hsp90 alpha Background Information
Heat shock protein 9 (9 kDa heat-shock protein, HSP9) 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. HSP9 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, HSP9 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP9 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP9 leads to client protein degradation and often cell death. Under stressful conditions, HSP9 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP9 client proteins and tumor cells require higher HSP9 activity than normal cells to maintain their malignancy. For this reason, Hsp9 has emerged as a promising target for anti-cancer drug development.
Full Name
heat shock protein 90kDa alpha (cytosolic), class A member 1
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.
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