MMP9 (ready-to-use)

GWB-AD618E

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

Placenta or breast carcinoma

Cytoplasmic

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

Secreted All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins termed matrix metalloproteinases (MMPs) are involved in the modulation of cell-matrix interactions. MMPs are Zn(2+)-binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes wound healing angiogenesis and tumor invasion. These enzymes are very potent when active and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). TIMPs have been shown to block tumor cell invasion suggesting that they act as metastasis suppressor genes.

Cleavage of gelatin types I and V and collagen types IV and V. Cofactor: Binds 2 zinc ions per subunit. Cofactor: Binds 3 calcium ions per subunit.

Exists as monomer disulfide-linked homodimer and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form.

Produced by normal alveolar macrophages and granulocytes.

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM:603932]. LDH is the predominant cause of low-back pain and unilateral leg pain.

Belongs to the peptidase M10A family [view classification].

Contains 4 hemopexin-like domains.