Recombinant Human MMP13, N-His

Reference: YHE45101
Product nameRecombinant Human MMP13, N-His
Uniprot IDP45452
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsMMP-13, MMP13, Matrix metalloproteinase-13, Collagenase 3
NoteFor research use only

Description of Recombinant Human MMP13, N-His


Recombinant Human MMP13, N-His is a protein that has gained significant attention in the field of drug discovery and development. It belongs to the matrix metalloproteinase (MMP) family, which plays a crucial role in regulating the extracellular matrix (ECM) and tissue remodeling. MMP13, also known as collagenase-3, is specifically involved in the degradation of type II collagen, the main structural component of cartilage in joints. Therefore, it has been identified as a potential therapeutic target for musculoskeletal diseases such as osteoarthritis and rheumatoid arthritis.

Structure of Recombinant Human MMP13, N-His

The gene encoding MMP13 is located on chromosome 11 in humans and consists of 11 exons. The protein is composed of 471 amino acids with a molecular weight of approximately 53 kDa. It contains a signal peptide, a prodomain, a catalytic domain, a hinge region, and a hemopexin-like domain. The catalytic domain is responsible for the proteolytic activity of MMP13, while the hemopexin-like domain is involved in substrate recognition and binding.

Activity of this protein

MMP13 is a zinc-dependent endopeptidase that cleaves the triple helical structure of type II collagen, leading to its degradation. It also has the ability to degrade other ECM components such as aggrecan, fibronectin, and laminin. This activity is tightly regulated by the prodomain, which maintains the enzyme in an inactive form until it is activated by proteolytic cleavage or binding to other molecules. MMP13 is primarily expressed in chondrocytes, the cells responsible for producing and maintaining cartilage, and its activity is essential for maintaining the integrity of the ECM in joints.

Application of Recombinant Human MMP13, N-His

The role of MMP13 in the pathogenesis of musculoskeletal diseases has made it a promising drug target for the treatment of conditions such as osteoarthritis and rheumatoid arthritis. In osteoarthritis, the degradation of type II collagen by MMP13 leads to the loss of cartilage, resulting in joint pain and stiffness. In rheumatoid arthritis, MMP13 is involved in the destruction of both cartilage and bone, contributing to joint damage and deformity. Therefore, inhibiting the activity of MMP13 has the potential to slow down or prevent the progression of these diseases.

Recombinant Human MMP13, N-His has been extensively studied in preclinical and clinical trials as a potential therapeutic target. Several inhibitors targeting MMP13 have been developed, and some have shown promising results in animal models of osteoarthritis and rheumatoid arthritis. These inhibitors can be administered topically or systemically, and some have even reached clinical trials in humans.


In conclusion, Recombinant Human MMP13, N-His is a protein with a crucial role in regulating the ECM and tissue remodeling. Its activity in degrading type II collagen makes it a potential drug target for treating musculoskeletal diseases such as osteoarthritis and rheumatoid arthritis. Further research and development of inhibitors targeting MMP13 could lead to the development of effective therapies for these debilitating conditions.


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