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Specifications
- Assay duration:Multiple steps
- Assay Type:Sandwich
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Pig
- Target protein:C5a
- 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 5a (C5a) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:3 h
- Shelf Life:12 Months
- Detection Range:0.156 - 10 ng/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:100 µl
- Sensitivity:0.057 ng/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-SEA388PO
- No. of tests:96 wells
Specifications
About this item
This assay has high sensitivity and excellent specificity for detecting Pig C5a (Complement Component 5a). The assay range is from 0.156 to 10 ng/ml (Sandwich kit) with a sensitivity of 0.057 ng/ml. There is no detectable cross to 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%
C5a is a protein fragment released from complement component C5. In humans, the polypeptide contains 74 amino acids. NMR spectroscopy proved that the molecule is composed of four helices and loops connecting the helices. On the N terminus a short 1.5 turn helix is also present. The longest helix -IV- develops three disulfide bonds with helix II and III. C5a is rapidly metabolised by a serum enzyme, carboxypeptidase B to a 73 amino acid form, C5a des-Arg.
C5a binds to a receptor protein on the surface of target cells, C5aR or CD88. This is a member of the G-protein-coupled receptor superfamily of proteins, predicted to have seven transmembrane helical domains of largely hydrophobic amino acid residues, forming three intra- and three extra-cellular loops, with an extracellular N-terminus and an intracellular C-terminus.