MMP2 Human

Matrix Metalloproteinase-2 (MMP-2), also known as gelatinase A or 72 kDa type IV collagenase, is a member of the matrix metalloproteinase (MMP) family. MMPs are zinc and calcium-dependent endopeptidases that play a crucial role in the degradation of extracellular matrix (ECM) components. This function is essential for various physiological processes, including embryonic development, tissue remodeling, and wound healing, as well as pathological processes such as arthritis and metastasis .

MMP-2 is a secreted enzyme with specificity towards type IV, V, VII, and X collagens . The human MMP-2 gene is located on chromosome 16q12.2 . The enzyme consists of several domains, including a pro-domain, a catalytic domain, and a hemopexin-like C-terminal domain. The pro-domain maintains the enzyme in an inactive form, which can be activated by proteolytic cleavage.

Recombinant human MMP-2 is produced using various expression systems, including Chinese Hamster Ovary (CHO) cells and HEK293 cells . The recombinant protein is typically purified to a high degree of purity (>90%) and is available in both carrier-free and carrier-containing formulations . The carrier-free version is often preferred for applications where the presence of carrier proteins like Bovine Serum Albumin (BSA) could interfere with experimental results .

Recombinant MMP-2 is widely used in research to study its role in ECM degradation and its involvement in various diseases. It is also used in assays to measure its enzymatic activity, typically using fluorogenic peptide substrates . The enzyme’s activity can be quantified by its ability to cleave these substrates, providing insights into its function and regulation.

Recombinant MMP-2 is generally stable for up to twelve months when stored at -20°C to -80°C under sterile conditions . It is recommended to aliquot the protein to avoid repeated freeze-thaw cycles, which can degrade its activity .