MMP-7 Antibody (Rabbit mAb) [G24L14]

Application: Reactivity: Mouse, Rat

Usage Information

Dilution
WB1:1000 IP1:100

Application
WB, IHC

Reactivity
Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
30 kDa 28 kDa, 20-22 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
MMP-7 Antibody (Rabbit mAb) [G24L14] detects endogenous levels of total MMP-7 protein.

Clone
G24L14

Synonym(s)
MAT; Matrilysin; matrilysin, uterine; Matrin; matrix metallopeptidase 7; matrix metalloproteinase 7; Matrix metalloproteinase-7; MMP-7; Mmp7; Pump-1 protease; Uterine metalloproteinase

Background
MMP-7, also known as matrilysin, is a secreted zinc-dependent endopeptidase of the matrix metalloproteinase family characterized as a “minimal-domain” MMP that lacks the large hemopexin-like C-terminal domain yet efficiently cleaves a broad spectrum of extracellular matrix and non-matrix substrates, positioning it as a compact but versatile regulator of tissue remodeling and tumor biology. The protein is synthesized as a latent proenzyme containing an N‑terminal signal peptide, a prodomain that maintains catalytic zinc in an inactive configuration through the “cysteine switch,” and a catalytic domain with the conserved HEXGHXXGXXHS motif and binding sites for zinc and calcium ions; proteolytic removal of the prodomain generates active MMP-7, which can then degrade matrix components such as proteoglycans, fibronectin, laminin and elastin, facilitating basement membrane and stromal remodeling. MMP-7 extends its impact beyond ECM degradation by processing a range of non-ECM proteins that modulate growth, survival and invasion: it cleaves insulin-like growth factor binding proteins to increase IGF bioavailability and enhance proliferation, converts membrane-bound heparin-binding EGF precursor (proHB‑EGF) into mature HB‑EGF that stimulates EGFR signaling, and sheds cell-surface Fas ligand and TNF‑α precursors to soluble forms that influence apoptosis of neighboring cells within the tumor microenvironment. MMP-7 also cleaves E‑cadherin, generating soluble E‑cadherin fragments that weaken cell–cell adhesion and promote invasion, and participates in ectodomain shedding of other adhesion and signaling molecules, thereby coordinating structural and signaling changes that support tumor progression. In angiogenesis, recombinant MMP-7 directly accelerates proliferation of human umbilical vein endothelial cells in a dose-dependent manner on type I and IV collagen, and upregulates endothelial secretion of MMP‑1 and MMP‑2 without altering VEGF production, indicating that MMP-7 can act as a pro-angiogenic factor by amplifying the local protease milieu that drives basement membrane dissolution, endothelial migration and neovessel formation. Expression analyses across cancers show that MMP-7 is frequently overexpressed in epithelial tumors, including colorectal, gastric, lung, and prostate cancers, and its levels correlate with advanced stage, lymph node metastasis, and poor prognosis, leading to recognition of MMP-7 as an oncogenic effector that mediates proliferation, differentiation, metastasis and invasion via multiple mechanisms. In colorectal cancer, MMP-7 is secreted from cancer-induced neovessels and acts as a metastatic factor, while in lung adenocarcinoma, it is upregulated by COX‑2 and promotes proliferation and invasion of tumor cells, linking inflammatory COX‑2 signaling to protease-dependent invasive behavior. Beyond oncology, MMP-7 is implicated in kidney disease as a regulator of tubular and interstitial remodeling, and urinary MMP-7 is emerging as a sensitive biomarker of kidney injury, reflecting its role in ECM turnover and fibrosis. The minimal-domain metalloprotease structure, activation via prodomain removal, ability to cleave both ECM and key non-ECM regulators (IGFBPs, HB‑EGF, FasL, TNF‑α, E‑cadherin), and demonstrated roles in angiogenesis, tumor invasion, metastasis and organ injury make MMP-7 a mechanistically rich target for evaluating protease-driven remodeling in cancer, fibrosis, immune pathologies, and for exploring MMP-7 as a diagnostic and therapeutic node in disease-associated microenvironments.

Background

MMP-7, also known as matrilysin, is a secreted zinc-dependent endopeptidase of the matrix metalloproteinase family characterized as a “minimal-domain” MMP that lacks the large hemopexin-like C-terminal domain yet efficiently cleaves a broad spectrum of extracellular matrix and non-matrix substrates, positioning it as a compact but versatile regulator of tissue remodeling and tumor biology. The protein is synthesized as a latent proenzyme containing an N‑terminal signal peptide, a prodomain that maintains catalytic zinc in an inactive configuration through the “cysteine switch,” and a catalytic domain with the conserved HEXGHXXGXXHS motif and binding sites for zinc and calcium ions; proteolytic removal of the prodomain generates active MMP-7, which can then degrade matrix components such as proteoglycans, fibronectin, laminin and elastin, facilitating basement membrane and stromal remodeling. MMP-7 extends its impact beyond ECM degradation by processing a range of non-ECM proteins that modulate growth, survival and invasion: it cleaves insulin-like growth factor binding proteins to increase IGF bioavailability and enhance proliferation, converts membrane-bound heparin-binding EGF precursor (proHB‑EGF) into mature HB‑EGF that stimulates EGFR signaling, and sheds cell-surface Fas ligand and TNF‑α precursors to soluble forms that influence apoptosis of neighboring cells within the tumor microenvironment. MMP-7 also cleaves E‑cadherin, generating soluble E‑cadherin fragments that weaken cell–cell adhesion and promote invasion, and participates in ectodomain shedding of other adhesion and signaling molecules, thereby coordinating structural and signaling changes that support tumor progression. In angiogenesis, recombinant MMP-7 directly accelerates proliferation of human umbilical vein endothelial cells in a dose-dependent manner on type I and IV collagen, and upregulates endothelial secretion of MMP‑1 and MMP‑2 without altering VEGF production, indicating that MMP-7 can act as a pro-angiogenic factor by amplifying the local protease milieu that drives basement membrane dissolution, endothelial migration and neovessel formation. Expression analyses across cancers show that MMP-7 is frequently overexpressed in epithelial tumors, including colorectal, gastric, lung, and prostate cancers, and its levels correlate with advanced stage, lymph node metastasis, and poor prognosis, leading to recognition of MMP-7 as an oncogenic effector that mediates proliferation, differentiation, metastasis and invasion via multiple mechanisms. In colorectal cancer, MMP-7 is secreted from cancer-induced neovessels and acts as a metastatic factor, while in lung adenocarcinoma, it is upregulated by COX‑2 and promotes proliferation and invasion of tumor cells, linking inflammatory COX‑2 signaling to protease-dependent invasive behavior. Beyond oncology, MMP-7 is implicated in kidney disease as a regulator of tubular and interstitial remodeling, and urinary MMP-7 is emerging as a sensitive biomarker of kidney injury, reflecting its role in ECM turnover and fibrosis. The minimal-domain metalloprotease structure, activation via prodomain removal, ability to cleave both ECM and key non-ECM regulators (IGFBPs, HB‑EGF, FasL, TNF‑α, E‑cadherin), and demonstrated roles in angiogenesis, tumor invasion, metastasis and organ injury make MMP-7 a mechanistically rich target for evaluating protease-driven remodeling in cancer, fibrosis, immune pathologies, and for exploring MMP-7 as a diagnostic and therapeutic node in disease-associated microenvironments.

References
https://pubmed.ncbi.nlm.nih.gov/33713636/ https://pubmed.ncbi.nlm.nih.gov/16380641/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%