Pro-MMP-13 human

NA.32

MMP13 (matrix metalloproteinase13) was first identified in 1994 in human breast cancer. It is produced as an inactive proenzyme, and is activated by the cleavage of its N-terminal region. MMPs constitute a single protein superfamily, which are further classified as collagenases, gelatinases, and stromelysins. Humans contain nine MMPs, and MMP13 is a member of the collagenases subfamily, and is also known as collagenase 3. MMP13 gene is localized to the human chromosome location 11q14.3–23.2, which houses the nine MMP genes.

MMP13 (matrix metalloproteinase13) functions against different types of ECM (extracellular matrix) components. It gets activated by and activates multiple MMPs, and hence, has a central role in the MMP cascade. This protein is frequently expressed in colorectal cancer (CRC), and this expression is linked with poor survival in CRC. MMP13 expression is absent in normal breast tissue, but is present in breast carcinoma suggesting its role in tumorigenesis. The expression of this protein can serve as a marker for tumor invasiveness, as its expression is induced during metastasis of multiple types of cancers, including squamous cell carcinomas of the head and neck, and this expression is usually linked to poor prognosis. Missense mutation in this gene results in the autosomal dominant disorder called Missouri type of human spondyloepimetaphyseal dysplasia (SEMDMO), which is characterized by abnormal growth and modeling of vertebrae and long bones.

In 50 mM Tris-HCl, pH 7; 250 mM NaCl; 5 mM CaCl₂; 1 mM ZnCl₂

human

expressed in Sf9 cells

≥95% (SDS-PAGE)

liquid

53.820 kDa

pkg of 10 μg

~100 μg/mL

Endotoxin, tested

P45452

wet ice

−70℃

human ... MMP13(4322)

H412

P273 - P501

Aquatic Chronic 3

12 - Non Combustible Liquids

WGK 3