JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB280347

Recombinant human MMP2 protein (Active)

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant human MMP2 protein (Active) is a Human Full Length protein in the 110 to 660 aa range with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for Functional studies. The predicted molecular weight of ab280347 protein is 63 kDa.

- Save time and ensure accurate results - use our recombinant MMP-2 protein as a control
- Optimal protein bioactivity, stability and reproducibility
- Available in different sizes to fit your experimental needs

View Alternative Names

CLG4A, MMP2, 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, TBE-1, MMP-2

4 Images
Functional Studies - Recombinant human MMP2 protein (Active) (AB280347)
  • FuncS

Supplier Data

Functional Studies - Recombinant human MMP2 protein (Active) (AB280347)

Biological activity of ab280347. Passed with a specific activity above >1,100 pmol/min/μg.

Cell based assay testing is performed on the first lot of protein only and is provided as a reference for protein activity; subsequent lots of protein must pass all biophysical quality control parameters that meet the same parameters as the first lot.

Lot : GR3379499-4

Mass Spectrometry - Recombinant human MMP2 protein (Active) (AB280347)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant human MMP2 protein (Active) (AB280347)

Mass determination by ESI-TOF.

Predicted MW is 62116.46 Da. (+/- 10 Da by ESI-TOF). Observed MW is 26116.57 Da. Additional masses are due to residual O-glycans.

HPLC - Recombinant human MMP2 protein (Active) (AB280347)
  • HPLC

Supplier Data

HPLC - Recombinant human MMP2 protein (Active) (AB280347)

HPLC analysis of ab280347.

SDS-PAGE - Recombinant human MMP2 protein (Active) (AB280347)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human MMP2 protein (Active) (AB280347)

SDS-Page anaylsis of ab280347.

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

<0.005 EU/µg

Expression system

HEK 293 cells

Tags

Tag free

Applications

FuncS

applications

Biologically active

Yes

Biological activity

Fully active determined by its ability to cleave human MMP2 fluorogenic peptide substrate (MCa-PLGL-Dpa-AR-NH2.

Accession

P08253

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Ensure the validity of your result using our recombinant human MMP2 protein ab280347 as a control.

The ab280347 MMP2 protein is sourced from HEK293 cells and can be used as a positive control in SDS-PAGE, mass spectrometry and HPLC.

Check out our protein gel staining guide for SDS-PAGE here

Premium Bioactive Protein range

The ab280347 MMP2 protein is part of the premium bioactive protein range which are ideal for preclinical cell culture and functional studies. These recombinant proteins are of the highest activity, purity, and consistency, meeting rigorous biophysical characterization.

More premium bioactive proteins can be found here

Sequence info

[{"sequence":"YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC","proteinLength":"Full Length","predictedMolecularWeight":"63 kDa","actualMolecularWeight":null,"aminoAcidEnd":660,"aminoAcidStart":110,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P08253","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The MMP-2 protein also known as matrix metalloproteinase-2 or gelatinase A is an enzyme involved in the breakdown of extracellular matrix components. It plays a critical role in tissue remodeling and cell migration. Comprised of a molecular weight of approximately 72 kDa this metalloproteinase is secreted as an inactive proenzyme that requires activation. MMP2 is expressed in various tissues including the brain heart and blood vessels where it contributes to normal physiological processes and pathological conditions.
Biological function summary

Matrix metalloproteinase-2 is mainly involved in the degradation of type IV and V collagens gelatin and fibronectin. As part of the metalloproteinase family it works alongside other MMPs to maintain tissue homeostasis and repair. MMP-2 forms part of a complex network that ensures the timely degradation of matrix components balancing synthesis and breakdown. It remains regulated by tissue inhibitors of metalloproteinases (TIMPs) preventing excessive degradation that could lead to tissue damage.

Pathways

MMP-2 plays a significant role within the extracellular matrix (ECM) remodeling and angiogenesis pathways. It interacts with various proteins including integrins and TIMP-2 to modulate cellular behaviors such as migration and invasion. MMP-2 contributes to processes like wound healing and embryonic development through its involvement in ECM degradation and new tissue formation.

Matrix metalloproteinase-2 is linked to cancer progression and cardiovascular diseases. In cancer abnormal MMP-2 activity facilitates tumor invasion and metastasis by breaking down matrix barriers. Increased MMP-2 expression associates with poor prognosis in cancers like breast and prostate. In cardiovascular diseases such as atherosclerosis it contributes to plaque destabilization and vascular remodeling. The imbalance in MMP-2 activity and its regulation by proteins like TIMP-1 are involved in the pathology of these disorders.

Specifications

Form

Liquid

Additional notes

>=95% Purity by HPLC

General info

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.. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.. Isoform 2. Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.

Sequence similarities

Belongs to the peptidase M10A family.

Post-translational modifications

Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.. The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.

Subcellular localisation

Nucleus

Product protocols

Target data

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.. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.. Isoform 2. Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
See full target information MMP2

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com