Specifications
- Assay duration:Multiple steps
- Assay Type (ELISA with LOV):Sandwich
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Human
- Target protein:LCAT
- Size:1 kit
- Sample Type:Serum, plasma and other biological fluids
- Cross Reactivity:No significant cross-reactivity or interference between Lecithin Cholesterol Acyltransferase (LCAT) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:3 h
- Shelf Life:12 Months
- Detection Range:0.94 - 60 ng/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:100 µl
- Sensitivity:0.41 ng/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-SEJ516HU
- No. of tests:96 wells
Specifications
About this item
This assay has high sensitivity and excellent specificity for detecting Human LCAT (Lecithin Cholesterol Acyltransferase). The assay range is from 0.94 to 60 ng/ml (Sandwich kit) with a sensitivity of 0.41 ng/ml. There is no detectable cross-reactivity with other relevant proteins. Activity loss rate and accelerated stability test ect have been conducted to guarantee the best performance of the products after long storage and delivery.
- High sensitivity and specificity
- Perfect reproducibility and consistency across batches
- Quality control with three-level inspections
- Wide range of targets/species available
- Intra-assay: CV<10%; Inter-assay: CV<12%
Lecithin-cholesterol acyltransferase is an enzyme that converts free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol), which is then sequestered into the core of a lipoprotein particle, eventually making the newly synthesized HDL spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. The enzyme is bound to high-density lipoproteins (HDLs) and low-density lipoproteins in the blood plasma. An unusual feature of the message is that the poly(A) signal appears to overlap the COOH-terminal glutamic acid and stop codons. The protein has several extended sequences of hydrophobic amino acids, one of which is similar to sequences in pancreatic lipase and lingual lipase.