Human PINP(N-terminal propeptide of Collagen alpha-1(I) chain) ELISA Kit Basic Information

Feiyue's Human  PINP(N-terminal propeptide of Collagen alpha-1(I) chain) ELISA Kit 

is an ELISA reagent for detection of PINP  in human serum, plasma or cell with sensitivity, specificity and consistency.

PINP(N-terminal propeptide of Collagen alpha-1(I) chain) Introduction

Pre-pro-peptide to pro-collagen: Three modifications of the pre-pro-peptide occur leading to the formation of the alpha peptide:

1, The signal peptide on the N-terminal is removed, and the molecule is now known as propeptide (not procollagen).

2, Hydroxylation of lysines and prolines on propeptide by the enzymes 'prolyl hydroxylase' and 'lysyl hydroxylase' (to produce hydroxyproline and hydroxylysine) occurs to aid cross-linking of the alpha peptides. This enzymatic step requires vitamin C as a cofactor. In scurvy, the lack of hydroxylation of prolines and lysines causes a looser triple helix (which is formed by three alpha peptides).

3, Glycosylation occurs by adding either glucose or galactose monomers onto the hydroxyl groups that were placed onto lysines, but not on prolines.

4, Once these modifications have taken place, three of the hydroxylated and glycosylated propeptides twist into a triple helix forming procollagen. Procollagen still has unwound ends, which will be later trimmed. At this point, the procollagen is packaged into a transfer vesicle destined for the Golgi apparatus.

Human PINP(N-terminal propeptide of Collagen alpha-1(I) chain) ELISA Kit Test method

This kit uses sandwich ELISA to detect the concentration of PINP(N-terminal propeptide of Collagen alpha-1(I) chain). PINP(N-terminal propeptide of Collagen alpha-1(I) chain) ELISA Kit allows for the in vitro quantitative determination of PINP(N-terminal propeptide of Collagen alpha-1(I) chain) concentrations in serum, plasma, tissue homogenates and other biological fluids. The concentration gradients of the kit standards or positive controls render a theoretical kit detection range in biological research samples containing PINP(N-terminal propeptide of Collagen alpha-1(I) chain). 

Reference:

1, Zylberberg, L.; Laurin, M. (2011). "Analysis of fossil bone organic matrix by transmission electron microscopy". Comptes Rendus Palevol. 11 (5–6): 357–66. doi:10.1016/j.crpv.2011.04.004.

2,Penn Medicine (4 November 2018). "4 Head-To-Toe Ways That Collagen Can Improve Your Health". Penn Medicine. Philadelphia, PA: Trustees of the University of Pennsylvania. Retrieved 7 June 2021.