Product Description

Recombinant ProMatrix Metalloproteinase-7 (ProMMP-7) is a member of the matrix metalloproteinase (MMP) family, which plays a critical role in extracellular matrix remodeling. With a molecular weight of approximately 28 kDa, ProMMP-7 is involved in various physiological and pathological processes, including tissue development, wound healing, and cancer progression. As a proteolytic enzyme, ProMMP-7 functions by cleaving components of the extracellular matrix, such as collagen and elastin, thereby facilitating tissue remodeling and cellular migration. This recombinant protein is widely utilized in research and pharmaceutical applications to study the mechanisms underlying matrix degradation and to develop therapeutic strategies targeting MMP-7 activity.

Current Lead Time

7-14 Days

Product Specifications

*For Research Use Only

If your product is within its expiration period, and has not performed according to expectations, fill out the sample return form. Return the unused sample frozen, with the auto generated packing slip to the address on the instructions. You will receive a full refund along with a replacement of the unused portion (inclusive of the failed test). Damages do not cover any additional costs incurred for failed experimentation. 

Reconstituted store at -20°C or -80°C.We recommend that single use aliquots are prepared to avoid freeze-thaw cycles.

1. Thaw the vial on ice, spin briefly
2. Prepare single-use or stock aliquots. This stage will depend on your final application so please adapt as appropriate. All our proteins are supplied carrier protein-free. If compatible with your work and you are storing at lower concentrations (<50 ug/ml) adding carrier protein is highly advised (usually 1% w/v high purity BSA or equivalent – ensure all buffers are sterile-filtered).
3. Prepare single-use aliquots whenever possible to avoid freeze-thaw cycles which can damage the proteins and reduce bioactivity. Store aliquots at -70 °C (or -20 °C)
4. We recommend sterile filtering after dilution in media or the final working solution
​

Not Available