MMP 1 Human, HEK
Description
MMP-1 Structure and Function
MMP-1 belongs to the peptidase M10 family and contains a prodomain, catalytic domain (with a zinc-binding site), and C-terminal hemopexin-like domain . Key features include:
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Substrate Specificity: Degrades collagens (types I, II, III, VII, X), gelatin, L-selectin, pro-TNF-α, and proteoglycans .
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Activation: Secreted as a proenzyme (52 kDa), requiring proteolytic cleavage or chemical activation (e.g., APMA) .
Table 1: MMP-1 Substrates and Biological Targets
| Substrate Category | Specific Examples |
|---|---|
| Collagens | I, II, III, VII, VIII, X |
| ECM Proteins | Gelatin, nidogen, versican |
| Non-ECM Targets | L-selectin, pro-TNF-α, α1-antitrypsin |
| Cytokines/Growth Factors | IL-1β, IGF-BP-3, SDF-1 |
Production in HEK Cells
HEK293 cells are a primary source for recombinant MMP-1 due to efficient protein folding and post-translational modifications.
Expression and Purification
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Protein Form: Pro-MMP-1 (Met1-Asn469) fused with a polyhistidine tag at the C-terminus .
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Formulation: Supplied as a lyophilized powder (ENZ-1085) or liquid (ENZ-099) in buffers containing MES, NaCl, glycerol, and Brij35 .
Activation Protocol
Recombinant MMP-1 requires activation to achieve catalytic activity:
Product Specs
Product Science Overview
Matrix Metalloproteinase-1 (MMP-1), also known as interstitial collagenase or fibroblast collagenase, is a member of the matrix metalloproteinase (MMP) family. These enzymes are involved in the breakdown of extracellular matrix (ECM) components, playing crucial roles in various physiological and pathological processes, including tissue remodeling, embryonic development, and disease progression such as arthritis and cancer metastasis .
MMP-1 is a zinc-dependent endopeptidase that primarily degrades interstitial collagens, including types I, II, and III . It can also degrade a broad range of other substrates such as types VII, VIII, and X collagens, casein, gelatin, myelin basic protein, L-selectin, pro-TNF, IL-1β, IGFBP-3, IGFBP-5, pro-MMP-2, and pro-MMP-9 . The enzyme is secreted as an inactive pro-protein and is activated upon cleavage by extracellular proteinases .
MMP-1 is expressed by various cell types, including fibroblasts, keratinocytes, endothelial cells, monocytes, and macrophages . Its expression is tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications. Factors such as cytokines, growth factors, and mechanical stress can influence MMP-1 expression .
Human recombinant MMP-1 is often produced in HEK 293 cells, a human embryonic kidney cell line, to ensure proper post-translational modifications and biological activity . The recombinant enzyme is typically purified to high levels of purity (>95% as determined by SDS-PAGE) and is available in various forms, including lyophilized powder and buffered aqueous solutions .
