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
Ferritin light chain qPCR Primer Pairs, Human: Alternative Names
LFTD qPCR Primer Pairs, Human; MGC71996 qPCR Primer Pairs, Human; NBIA3 qPCR Primer Pairs, Human
Ferritin light chain Background Information
Ferritin, light polypeptide (FTL) is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Storage of iron in the tissues occurs in the form of ferritin and hemosiderin. The latter originates from ferritin that has undergone intracellular digestion of its protein shell, leaving the iron core. Ferritin and hemosiderin are components of a continuum. Ferritin has been identified in all types of living organisms: animals, plants, molds, and bacteria. Whithin the protein shell of ferritin, iron is first oxidized to the ferric state for storage as ferric oxyhdroxide. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms.