Specifications
- Assay duration:Multiple steps
- Assay Type:Sandwich
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Human
- Target protein:C1qA
- Size:1 kit
- Sample Type:Serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids
- Cross Reactivity:No significant cross-reactivity or interference between Complement Component 1, Q Subcomponent A (C1qA) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:3 h
- Shelf Life:12 Months
- Detection Range:78 - 5000 pg/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:100 µl
- Sensitivity:35 pg/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-SED207HU
- No. of tests:96 wells
Specifications
About this item
This assay has high sensitivity and excellent specificity for detecting Human C1qA (Complement Component 1, Q Subcomponent A). The assay range is from 78 to 5000 pg/ml (Sandwich kit) with a sensitivity of 35 pg/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%
Reid (1974) reported a partial amino acid sequence of 95 residues of the 191 residues in the oxidized A chain of human subcomponent C1q. This region of the A chain contains a repeating sequence of glycine-X-Y, where X is often proline and Y is often hydroxyproline, for 78 residues. The 5 hydroxylysine residues and 5 hydroxyproline residues in the oxidized A chain are all in these 78 residues and only in the Y position of the repeating sequence. Prolonged collagenase digestion of the oxidized A chain yielded a large, apparently C-terminal peptide containing most of the noncollagenous sequences present in the chain. Reid (1974) concluded that the A chain of C1q contains a collagen-like region that constitutes most of the N-terminal half of the chain.