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SRP6039

Sigma-Aldrich

Pro-MMP-13 human

recombinant, expressed in Sf9 cells, ≥95% (SDS-PAGE)

Synonym(s):

MMP recombinant, MMP13, Matrix metalloproteinase-13, procollagenase 3

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in Sf9 cells

assay

≥95% (SDS-PAGE)

form

liquid

mol wt

53.820 kDa

packaging

pkg of 10 μg

concentration

~100 μg/mL

impurities

Endotoxin, tested

NCBI accession no.

shipped in

wet ice

Storage temp.

−70°C

Gene Information

human ... MMP13(4322)

General description

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.[1] 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.[2] MMP13 gene is localized to the human chromosome location 11q14.3–23.2, which houses the nine MMP genes.[3]

Biochem/physiol Actions

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.[1] MMP13 expression is absent in normal breast tissue, but is present in breast carcinoma suggesting its role in tumorigenesis.[2] 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.[4] 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.[3]

Physical form

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

hcodes

Hazard Classifications

Aquatic Chronic 3

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas.
Freije JM, et al.
The Journal of Biological Chemistry, 269(24), 16766-16773 (1994)
Matrix metalloproteinase 13 activity is associated with poor prognosis in colorectal cancer.
Leeman MF, et al.
Journal of Clinical Pathology, 55(10), 758-762 (2002)
MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMD(MO).
Kennedy AM, et al.
The Journal of Clinical Investigation, 115(10), 2832-2842 (2005)
M F Leeman et al.
Journal of clinical pathology, 55(10), 758-762 (2002-10-02)
The matrix metalloproteinases (MMPs) are a family of proteolytic enzymes collectively capable of degrading all extracellular matrix components, in particular fibrillar collagen. The importance of this group of proteins in the processes of tumour invasion and metastasis is now widely
A Matrix Metalloproteinase Gene Expressed in Human T Lymphocytes is identical with Collagenase 3 from Breast Carcinomas.
Willmroth, Frank, et al.
Immunobiol., 198, 375-384 (1998)

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