Hydroxylated collagen α-1(III) chain (696-707) Heavy

Ref. 3D-CRB1301297

Product Information

• Name: Hydroxylated collagen α-1(III) chain (696-707) Heavy
• Synonyms: H-GGAGP^(hyP)GPEGGK-OH, hyP is HydroxyprolineGGAG-[U-13C5,15N-Pro]-Hyp-GPEGGK-acidH-Gly-Gly-Ala-Gly-[U-13C5,15N-Pro]-Hyp-Gly-Pro-G lu-Gly-Gly-Lys-OH
• Brand: Biosynth
• Description: Residues 696-707 of collagen III alpha 1 chain (α1(III)). Type III collagen represents about 20% of the collagen present in the dermis, although it is more abundant in the walls of distensible (expandable) organs and blood vessels. This peptide contains a hydroxylated proline residue, 4-hydroxyproline (4Hyp). 4Hyp residues help stabilize the collagen triple helix through water-bridged intramolecular hydrogen bonding.Type III collagen is a homotrimer, consisting of three α1(III) chains, that are cross-linked in a staggered array through lysine residues to form microfibrils. Collagen III fibrils assume a 'flexi-rod' structure with flexible zones interspersed with rod-like domains, essential for maintaining flexibility in young, pliable tissues and distensible organs. Collagen III has a nearly identical structural arrangement and charge distribution pattern as collagen I, allowing for its substitution by collagen I in embryonic development and wound healing.Collagen III participates in a variety of biological functions including: cell-binding- haemostasis and angiogenesis- tissue remodelling- foetal development, and wound healing. Collagen III is coded for by the COL3A1 gene and COL3A1 disease-causing sequence variants can result in vascular Ehlers-Danlos syndrome (EDS type IV), cerebral aneurysms, gastroesophageal reflux disease, and pelvic organ prolapse.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.

Chemical properties

• Molecular weight: 1,001.5 g/mol
• Purity: Min. 95%