Description

  • Product name

    Native human MMP2 protein (Active)
    See all MMP2 proteins and peptides
  • Biological activity

    ≥850mU/mg protein.

    One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.

    Activation: Requires activation by 2mM (final concentration) APMA or 1mM mersalic acid for 60-120 min. at 37°C. We do not recommend to use trypsin for activation! Do not dilute enzyme for activation!

    Specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-GlyIle-Ala-Gly-Gln-D-Arg (Dnp-peptide).

    Substrate concentration should be 0.5mg/ml containing 0.05mg/ml albumine. One unit MMP catalyzes the hydrolysis of 1µmol Dnp-peptide/min. at 37°C and pH 7.0.

    Alternatively the fluorogenic substrate (7-Methoxycoumarin-4-yl) acetyl-Pro-Leu-GlyLeu-N-β-Dnp-L-(α,β-diaminopropionyl)Ala-Arg-NH2 can be used.

    Hydrolysis of the Gly-Leu bond separates the highly fluorescent (7-Methoxycoumarin-4-yl)acetyl group from the 2,4-dinitrophenyl resulting in an increase of fluorogenic intensity.

    Km: 7.0x105M-1s-1


    Substrate should be kept as a 9.15mM stock solution in DMSO (10mg/ml). In the assay, the substrate concentration should be ~25µM. The assay can be performed in a 96-well microtiter plate (100/200µl per well) suitable for fluorogenic measurements (Ex 328 nm; Em 393 nm).

  • Purity

    > 90 % SDS-PAGE.
    No other MMP contaminants are detectable.
  • Expression system

    Native
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Native
    • Species

      Human
    • Sequence

      APSPIIKFPG DVAPKTDKEL AVQYLNTFYG CPKESCNLFV LKDTLKKMQK FFGLPQTGDL DQNTIETMRK PRCGNPDVAN YNFFPRKPKW DKNQITYRII GYTPDLDPET VDDAFARAFQ VWSDVTPLRF SRIHDGEADI MINFGRWEHG DGYPFDGKDG LLAHAFAPGT GVGGDSHFDD DELWTLGEGQ VVRVKYGNAD GEYCKFPFLF NGKEYNSCTD TGRSDGFLWC STTYNFEKDG KYGFCPHEAL FTMGGNAEGQ PCKFPFRFQG TSYDSCTTEG RTDGYRWCGT TEDYDRDKKY GFCPETAMST VGGNSEGAPC VFPFTFLGNK YESCTSAGRS DGKMWCATTA NYDDDRKWGF CPDQGYSLFL VAAHEFGHAM GLEHSQDPGA LMAPIYTYTK NFRLSQDDIK GIQELYGASP DIDLGTGPTP TLGPVTPEIC KQDIVFDGIA QIRGEIFFFK DRFIWRTVTP RDKPMGPLLV ATFWPELPEK IDAVYEAPQE EKAVFFAGNE YWIYSASTLE RGYPKPLTSL GLPPDVQRVD AAFNWSKNKK TYIFAGDKFW RYNEVKKKMD PGFPKLIADA WNAIPDNLDA VVDLQGGGHS YFFKGAYYLK LENQSLKSVK FGSIKSDWLG C
    • Predicted molecular weight

      72 kDa
    • Amino acids

      30 to 660
    • Additional sequence information

      Full length mature protein, without the signal peptide.

Specifications

Our Abpromise guarantee covers the use of ab168864 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

    Functional Studies

    SDS-PAGE

  • Form

    Liquid
  • Additional notes

    Inhibitors: Activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and by chelators of divalent cations like EDTA or o-phenanthroline.

     

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 7.00
    Preservative: 0.05% Sodium azide
    Constituents: 0.05% Brij, 0.06% Calcium chloride, 0.00001% Zinc chloride, 0.79% Tris HCl, 1.16% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • 72 kDa gelatinase
    • 72kD type IV collagenase
    • CLG 4
    • CLG 4A
    • CLG4
    • CLG4A
    • Collagenase Type 4 alpha
    • Collagenase type IV A
    • Gelatinase A
    • Gelatinase alpha
    • Gelatinase neutrophil
    • Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase
    • Matrix Metalloproteinase 2
    • Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
    • Matrix metalloproteinase II
    • Matrix metalloproteinase-2
    • MMP 2
    • MMP II
    • MMP-2
    • MMP2
    • MMP2_HUMAN
    • MONA
    • Neutrophil gelatinase
    • PEX
    • TBE 1
    • TBE-1
    see all
  • 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.
    PEX, the C-terminal non-catalytic fragment of MMP2, posseses 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.
  • Tissue specificity

    Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.
  • Involvement in disease

    Defects in MMP2 are the cause of Torg-Winchester syndrome (TWS) [MIM:259600]; also known as multicentric osteolysis nodulosis and arthropathy (MONA). TWS is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Torg-Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes.
  • Sequence similarities

    Belongs to the peptidase M10A family.
    Contains 3 fibronectin type-II domains.
    Contains 4 hemopexin-like domains.
  • Domain

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
  • 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.
  • Cellular localization

    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.
  • Information by UniProt

References

This product has been referenced in:

  • Schmitt R  et al. A potential key mechanism in ascending aortic aneurysm development: Detection of a linear relationship between MMP-14/TIMP-2 ratio and active MMP-2. PLoS One 14:e0212859 (2019). Read more (PubMed: 30794673) »
  • Wang Y  et al. Myosin Heavy Chain 10 (MYH10) Gene Silencing Reduces Cell Migration and Invasion in the Glioma Cell Lines U251, T98G, and SHG44 by Inhibiting the Wnt/ß-Catenin Pathway. Med Sci Monit 24:9110-9119 (2018). Read more (PubMed: 30552850) »
See all 3 Publications for this product

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