Human PCSK9 ELISA Kit

Detection Principle:

This kit uses double antibody sandwich ELISA technology. The specific anti human PCSK9 capture antibody was pre coated on a high affinity microplate. Add the standard, the sample to be tested and the biotin labeled detection antibody into the wells of the enzyme plate in turn, shake well and mix well, and then place it at room temperature for 2 hours of incubation process. The LH existing in the sample is combined with the solid-phase antibody and the detection antibody. After washing sufficiently to remove free and unbound components, streptavidin HRP (sa-hrp) labeled with horseradish peroxidase was added. After washing again, TMB chromogenic substrate was added and incubated at room temperature in the dark to develop color. The depth of color response is positively correlated with the concentration of PCSK9 in the sample. Add stop solution to stop the reaction, and use a microplate reader to measure the absorbance value at 450 nm detection wavelength (correction wavelength 570-630 nm)

Detection Type: Double antibody sandwich method

Form: Pre coated 96 well plate

Test Sample Type: cell supernatant, serum, plasma

Loading Amount: 100 μ L

Kit Components: a copy of pre coated 96 well plate, standard, PCSK9 detection antibody, standard dilution, detection buffer, TMB chromogenic substrate, washing solution, termination solution, sa-hrp, plate sealing membrane and instructions

Sensitivity: 3.39pg/ml

Detection Range: 62.5-4000 pg/ml

Recovery Range: 94-110%

Storage Method: 2-8 ℃

Standard Curve:

Background:

Proprotein convertase subtilisin (PCSK9) is a member of the proteinase K subfamily of the secreted subtilisin family. It undergoes intramolecular autocatalytic processing in the endoplasmic reticulum and is synthesized as a soluble zymogen. PCSK9 and low density lipoprotein (LDL)Cholesterol receptor binding, inducing LDLR degradation. PCSK9 variants can reduce or elevate circulating cholesterol. Other variants are associated with very rare autosomal dominant familial hypercholesterolemia (hchola3). The mutation enhances its protease activity, reduces LDLR levels, and prevents cholesterol absorption by cells.