MMP-3 Antibody [K11K15] | Primary Antibodies

Application: Reactivity: Human, Rat

Lane 1: U-87 MG, Lane 2: U-118 MG, Lane 3: 3T3, Lane 4: PC-12

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, 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
60 kDa

Positive Control	U-87 MG cells; U-118 MG cells; LN18 cells; PC-12 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
MMP-3 Antibody [K11K15] detects endogenous levels of total MMP-3 protein.

Clone
K11K15

Synonym(s)
Stromelysin-1; SL-1; Matrix metalloproteinase-3 (MMP-3); Transin-1; MMP3; STMY1

Background
Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1, is a zinc-dependent endopeptidase of the MMP family that degrades extracellular matrix components and is crucial for tissue remodeling during embryonic development, wound healing, and pathological processes such as cancer invasion and arthritis. MMP-3 has a modular structure featuring an N-terminal prodomain (~80 amino acids) that maintains latency via a cysteine switch with the catalytic zinc, a central catalytic domain with the conserved HExGHxxGxxH motif where three histidines coordinate Zn²⁺ for proteolysis, a hinge region, and a C-terminal hemopexin-like domain that facilitates substrate specificity. The hemopexin-like domain enables recognition of Phe residues in Gly-X-Phe motifs of triple-helical collagens through cooperative Cat-Hpx interactions, allowing efficient collagenolysis and a broad substrate repertoire including aggrecan, fibronectin, and laminin. MMP-3 is activated by proteolytic removal of the prodomain, often by furin or other MMPs, which unleashes its role in processes such as inflammation (by processing cytokines like IL-1β, chemokines, and growth factors), tumor progression (by cleaving E-cadherin to promote epithelial-mesenchymal transition and metastasis), and cardiovascular disease (through atherosclerotic plaque instability). Dysregulation of MMP-3 is linked to joint destruction in arthritis and cancer progression via upregulated transcription from AP-1/NF-κB sites.

Background

Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1, is a zinc-dependent endopeptidase of the MMP family that degrades extracellular matrix components and is crucial for tissue remodeling during embryonic development, wound healing, and pathological processes such as cancer invasion and arthritis. MMP-3 has a modular structure featuring an N-terminal prodomain (~80 amino acids) that maintains latency via a cysteine switch with the catalytic zinc, a central catalytic domain with the conserved HExGHxxGxxH motif where three histidines coordinate Zn²⁺ for proteolysis, a hinge region, and a C-terminal hemopexin-like domain that facilitates substrate specificity. The hemopexin-like domain enables recognition of Phe residues in Gly-X-Phe motifs of triple-helical collagens through cooperative Cat-Hpx interactions, allowing efficient collagenolysis and a broad substrate repertoire including aggrecan, fibronectin, and laminin. MMP-3 is activated by proteolytic removal of the prodomain, often by furin or other MMPs, which unleashes its role in processes such as inflammation (by processing cytokines like IL-1β, chemokines, and growth factors), tumor progression (by cleaving E-cadherin to promote epithelial-mesenchymal transition and metastasis), and cardiovascular disease (through atherosclerotic plaque instability). Dysregulation of MMP-3 is linked to joint destruction in arthritis and cancer progression via upregulated transcription from AP-1/NF-κB sites.

References
https://pubmed.ncbi.nlm.nih.gov/31827179/ https://pubmed.ncbi.nlm.nih.gov/34276395/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

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%