The primer mix has been verified to generate satisfactory qPCR data on Roche Applied-science LightCycler® 480 Ⅱ.
Storage & Shipping
Lyophilized qPCR primer mix is shipped at ambiente temperatura
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
HSP70 qPCR Primer Pairs, Human: Alternative Names
HEL-S-103 qPCR Primer Pairs, Human; HSP70-1 qPCR Primer Pairs, Human; HSP70-1A qPCR Primer Pairs, Human; HSP70I qPCR Primer Pairs, Human; HSP72 qPCR Primer Pairs, Human; HSPA1 qPCR Primer Pairs, Human
HSP70 Background Information
HSPA1A is a member of the Hsp7 protein family. The 7 kilodalton heat shock proteins (Hsp7s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates presentation of antigen peptide to T cells. Molecular chaperones of the Hsp7 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp7 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp7 chaperones use the same mechanism of ATP-driven polypeptide binding and release.
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