Human MMP-9(Matrix Metalloproteinase 9) Introduciton

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. In humans the MMP9 gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain. MMP9, along with elastase, appears to be a regulatory factor in neutrophil migration across the basement membrane. MMP9 plays several important functions within neutrophil action, such as degrading extracellular matrix, activation of IL-1β, and cleavage of several chemokines. In a mouse model, MMP9 deficiency resulted in resistance to endotoxin shock, suggesting that MMP9 is important in sepsis.

Human MMP-9(Matrix Metalloproteinase 9) ELISA Kit Test method

This kit uses sandwich ELISA to detect the concentration of Human MMP-9.

Human MMP-9-specific monoclonal antibody has been pre-coated in the wells of the supplied microplate. Standards samples and controls are added to interact with the immobilized antibody. A sandwich complex is formed by additional anti-Human MMP-9 antibody with HRP-Streptavidin. TMB solution is added to react with the sandwich for ming optical signal measured by microplate reader. The concentration of Human MMP-9in the sample can be calculated by comparing the absorbance of the sample with the standard curve.

Reference:

1. GRCh38: Ensembl release 89: ENSG00000100985 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)".