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

Colorimetric

Sandwich ELISA (quantitative)

Human Type I collagen helical peptide microplate
Human Type I collagen helical peptide standard
Human Type I collagen helical peptide detect antibody
Streptavidin-HRP
Standard diluent
Assay buffer
HRP substrate
Stop solution
Wash buffer
Plate covers

Do not mix components from different kit lots or use reagents beyond the kit expiration date.
Allow all reagents to warm to room temperature for at least 30 minutes before opening.
Pre-rinse the pipet tip with reagent, use fresh pipet tips for each sample, standard and reagent to avoid contamination.
Unused wells must be kept desiccated at 4 C in the sealed bag provided.
Mix Thoroughly is very important for the result. It is recommended using low frequency oscillator or slight hand shaking every 10 minutes.
It is recommended that all samples and standards be assayed in duplicate or triplicate.

Gel pack with blue ice.

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 other’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 Å (0.29 nm) per residue.