Collagen α-2(I) chain (90-) Heavy GDQG-[U-13C5,15N-Pro]-VGR-acid


Alpha 2 chain from type I collagen containing proline residue labelled with 13C and 15N stable isotopes

See full description

Catalogue number crb1301296
Sequence (one letter code) GDQG-[U-13C5,15N-Pro]-VGR-acid
Sequence (three letter code) H-Gly-Asp-Gln-Gly-[U-13C5,15N-Pro]-Val-Gly-Arg-OH
Purity >95%
Storage -20°C
Molecular Weight 790.4

Alfieri, M., Barbaro, F., Consolini, E., Bassi, E., Dallatana, D., Bergonzi, C., Bianchera, A., Bettini, R., Toni, R. and Elviri, L. (2019). A targeted mass spectrometry method to screen collagen types I-V in the decellularized 3D extracellular matrix of the adult male rat thyroid. Talanta, 193, 1-8. PMID: 30368276

Collagens are the most abundant family of extra cellular matrix (ECM) proteins, accounting for two-thirds of the dry mass of adult articular cartilage. Several subtypes have been identified including type II, IX, X, XI, VI, XII, and XIV collagen, however 80 – 90% of the collagen in the body consists of types I, II, and III. Type I collagen is a long thin protein which consists of three coiled subunits: two alpha 1 (I) (α1(I)) chains and one α2(I). Type I collagen forms part of the major structure of the bone, and mutations in the α1(I) or α2(I) genes lead to osteogenesis imperfecta, or brittle-bone disease.

The proline residue at position 5 of this peptide is isotopically labelled with carbon-13 (5) and nitrogen-15 (1), giving this peptide a mass increase of 6 compared to the unlabelled peptide

Collagen α-2(I) chain (90-) Heavy

Cat No. Pack Size Price Qty