Human Type I collagen helical peptide (HELIX-1) ELISA Kit

In collagen, the collagen helix, or type-2 helix, is a major shape in secondary structure. It consists of a triple helix made of the repetitious amino acid sequence glycine - X - Y, where X and Y are frequently proline or hydroxyproline. A collagen triple helix has 3.3 residues per turn. Each of the three chains is stabilized by the steric repulsion due to the pyrrolidine rings of proline and hydroxyproline residues. The pyrrolidine rings keep out of each otherвЂ™s way when the polypeptide chain assumes this extended helical form, which is much more open than the tightly coiled form of the alpha helix. The three chains are hydrogen bonded to each other. The hydrogen bond donors are the peptide NH groups of glycine residues. The hydrogen bond acceptors are the CO groups of residues on the other chains. The OH group of hydroxyproline also participates in hydrogen bonding. The rise of the collagen helix (superhelix) is 2.9 Г… (0.29 nm) per residue.

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SPECIFICATIONS

Catalog Number

KTE62541

Size

48T, 96T, 96T*5, 96T*50

Applications

ELISA

Reactivities

Hum

Additional Info

Human Type I collagen helical peptide (HELIX-1) ELISA Kit has high sensitivity and excellent specificity for detection of Human HELIX-1. No significant cross-reactivity or interference between Human HELIX-1 and analogues was observed.