SILu^™Prot COL1A1 N-terminal propeptide human

Collagen type I is present in soft connective tissues and bone, where it constitutes more than 90% of the organic matrix.1 During bone formation collagen type I is synthesized from pro-collagen type I, which is secreted from fibroblasts and osteoblasts 2 Pro-collagen type I contains N-and C-terminal extensions, which are removed by specific proteases during the conversion of procollagen to collagen.3 Measurements of N- terminal propeptides of procollagen type I (PINP) can be of value in assessing bone formation.Recent evidence indicates that PINP can serve as a serum biomarker of bone formation, as it accurately identifies those patients who are responding to anabolic or antiresorptive therapy within 3 months of the start of treatment.4 The use of this biomarker in patients being treated for osteoporosis may significantly improve therapy adherence and clinical outcomes.4

QEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPDYKDDDDKGHHHHHHHHGGQ

SILu^™Prot COL1A1 is a recombinant, stable isotope-labeled human COL1A1 which incorporates [¹³C₆, ¹⁵N₄]-Arginine and [¹³C₆, ¹⁵N₂]-Lysine. Expressed in human 293 cells, it is designed to be used as an internal standard for bioanalysis of COL1A1 in mass-spectrometry. SILu Prot COL1A1 is a protein of 159 amino acids (Q23-P161 and including C-terminal polyhistidine and FLAG^® tags) with a calculated molecular mass of 16 kDa.

Supplied as a lyophilized powder containing phosphate buffered saline.

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