MMP1 (ready-to-use)

GWB-D88824

Synthetic peptide (unfortunately the amino acid sequence is considered to be commercially sensitive) (Human) (C terminal).

Placenta bladder Breast and ovarian carcinoma

Secreted

PBS pH 7. 4 containing 1%BSA and 0. 1% sodium azide

Secreted The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively these enzymes can degrade all the components of the extracellular matrix including fibrillar and non-fibrillar collagens fibronectin laminin and basement membrane glycoproteins. In general a signal peptide a propeptide and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition fibronectin-like repeats a hinge region and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase gelatinase stomelysin and membrane-type MMP subfamilies. All MMPs are synthesized as proenzymes and most of them are secreted from the cells as proenzymes. Thus the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing apoptosis bone elongation embryo development uterine involution angiogenesis and tissue remodeling and in diseases such as multiple sclerosis Alzheimer\' s malignant gliomas lupus arthritis periodontis glumerulonephritis atherosclerosis tissue ulceration and in cancer cell invasion and metastasis.

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1\' is a hydrophobic residue. Cofactor: Binds 4 calcium ions per subunit. Cofactor: Binds 2 zinc ions per subunit.

Interacts with HIV-1 Tat.

There are two distinct domains in this protein; the catalytic N-terminal and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).

Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.

Contains 4 hemopexin-like domains.