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The Human PIIINP (N-Terminal Procollagen III Propeptide) ELISA quantitates PIIINP in serum and plasma.
Principle of the method
The Human N-Terminal Procollagen III Propeptide (PIIINP) solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the concentration of N-Terminal Procollagen III Propeptide (PIIINP) in biological samples. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are added into these wells and bind to the immobilized (capture) antibody.
The sandwich complex is formed by the addition of a second (HRP-linked) detection antibody specific to N-Terminal Procollagen III Propeptide (PIIINP). Excess reagents are washed from the plate.
A substrate solution is added that reacts with the enzyme-antibody-target complex to produce a measurable signal. The enzyme-substrate reaction is terminated by the addition of stop solution. The intensity of the signal, measured spectrophotometrically at 450 ± 2 nm, is directly proportional to the concentration of N-Terminal Procollagen III Propeptide (PIIINP) present in the original specimen.
Rigorous validation:
Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Collagen type III is synthesized as a homo-trimeric pro-collagen (Procollagen III) comprising three identical pro-alpha(III)-chains. It has been reported that procollagen type III is processed extracellularly at the ECM and can be found by immunostaining intracellular as well as extracellular. Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Gene aliases : EDS4A, EDSVASC, PMGEDSV
Gene ID : (Human) 1281
Gene symbol : COL3A1
Protein Aliases : alpha-1 type III collagen, alpha-1(III) procollagen, alpha1 (III) collagen, collagen, fetal, type III, alpha 1, Ehlers-Danlos syndrome type IV, autosomal dominant, unnamed protein product
UniProt ID (Human) P02461
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