| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | 72 kDa type IV collagenase;3.4.24.24;72 kDa gelatinase;Gelatinase A;Matrix metalloproteinase-2;MMP-2;TBE-1;PEX;MMP2;CLG4A; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human MMP2 recombinant protein (Position: E412-N573). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-MMP2 Antibody Picoband® is an antibody reagent for detection of MMP2 (72 kDa type IV collagenase). Researchers commonly use anti-MMP2 antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, Flow, ELISA).
Boster Bio Anti-MMP2 Antibody Picoband® catalog # A00286-3. Tested in ELISA, WB applications. This antibody reacts with Human. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Target: MMP2 — 72 kDa type IV collagenase (72 kDa type IV collagenase). Alternative names: 72 kDa type IV collagenase;3.4.24.24;72 kDa gelatinase;Gelatinase A;Matrix metalloproteinase-2;MMP-2;TBE-1;PEX;MMP2;CLG4A;
- Antibody format: Polyclonal; Rabbit IgG
- Species context: Host: Rabbit, Reactivity: Human
- Purification: Immunogen affinity purified.
- Immunogen: E.coli-derived human MMP2 recombinant protein (Position: E412-N573).
- Molecular weight context: observed 70 kDa, calculated 73882 MW (reported)
- Provided application(s): WB, IHC, Flow, ELISA
These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.
Biological background
Function: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.
Cellular localization: Isoform 1: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.
Tissue details: Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. .
Background: Matrix metalloproteinase-2 (MMP2) is a Type IV collagenase, 72-kD, which is also known as gelatinase and is a member of a group of secreted zinc metalloproteases. The MMP2 gene is 17 kb long with 13 exons varying in size from 110 to 901 bp and 12 introns ranging from 175 to 4,350 bp, located within a region of human chromosome 16q13. In addition, the extra exons encode the amino acids of the fibronectin-like domain which has so far been found in only the 72- and 92-kDa type IV collagenase. MMP2, which has a critical role in the binding of progelatinase A and TIMP4 via the C-terminal hemopexin-like domain (C domain), is functionally associated on the surface of angiogenic blood vessels. Not only is a likely effector of endometrial menstrual breakdown, MMP2 is also effector and regulator of the inflammatory response. Moreover, MMP2 could be helpful in diagnosing Takayasu arteritis.
Cross reactivity: No cross-reactivity with other proteins.
Research relevance and current trends
- Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
- Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
- Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.
Common research applications
- Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
- Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
- Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.
Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.
Notes for experimental interpretation
- Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
- Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
- Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.
For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.