Home Shop MMP-2 (catalytic domain) (human), (recombinant)

MMP-2 (catalytic domain) (human), (recombinant)

BML-SE237

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Represents a naturally occurring active form of MMP-2 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.

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Product Details

Activity	Preincubation of MMP-2 catalytic domain at 5nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 30nM for 1 hour completely inhibits enzymatic activity.
Alternative Name	Matrix metalloproteinase 2, Gelatinase A, 72 kDa Type IV collagenase
Application Notes	Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Formulation	Liquid. In 50mM TRIS-HCl, pH 7.5, containing 300mM NaCl, 5mM CaCl₂, 20µM ZnCl₂, 0.05% Brij-35 and 20% glycerol.
Gene/Protein Identifier	NM_004530 (RefSeq)
MW	~40kDa
Purity	≥90% (SDS-PAGE)
Purity Detail	Purified by multi-step chromatography.
Source	Produced in yeast. Active recombinant matrix metalloproteinase-2 (MMP-2, gelatinase A, 72kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Tyr¹¹⁰-Asp⁴⁵², which comprises the catalytic/fibronectin domain of human MMP-2, with a C-terminal purification tag.
Specific Activity	≥200 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate.
UniProt ID	P08253

Handling & Storage

Use/Stability	The enzyme is stable on ice for at least several hours. However, it is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. After initial defrost, aliquot product into individual tubes and refreeze at -70°C. Avoid repeated freeze/defrost cycles.NOTE: When stored under the above conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.
Long Term Storage	-80°C
Shipping	Dry Ice

Regulatory Status	RUO – Research Use Only

Apolipoprotein-A1 transports and regulates MMP2 in the blood: Sarker, H., Panigrahi, R., et al.; Nat. Commun. 16, 3752 (2025), Abstract
Directed evolution of metalloproteinase inhibitor TIMP-1 for selective inhibition of MMP-9 exploits catalytic and fibronectin domain interactions: Shoari, A., Coban, M. A., et al.; J. Biol. Chem. 301, 110258 (2025), Abstract
Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9: S.C. Park, et al.; Matrix Biol. 123, 59 (2023), Abstract
Developing Metal-Binding Isosteres of 8-Hydroxyquinoline as Metalloenzyme Inhibitor Scaffolds: H. Seo, et al.; Inorg. Chem. 61, 7631 (2022), Abstract
MMP2 and TLRs modulate immune responses in the tumor microenvironment: L.R. Muniz-Bongers, et al.; JCI Insight 6, 144913 (2021), Abstract
Overhydroxylation of lysine of collagen increases uterine fibroids proliferation: roles of lysyl hydroxylases, lysyl oxidases, and matrix metalloproteinases: M. Kamel, et al.; Biomed. Res. Int. 2017, 5316845 (2017), Abstract — Full Text
Structural and functional insights into the interaction of sulfated glycosaminoglycans with tissue inhibitor of metalloproteinase-3 – A possible regulatory role on extracellular matrix homeostasis: S. Rother, et al.; Acta Biomater. 45, 143 (2016), Abstract
Development and validation of novel enzyme activity methods to assess inhibition of matrix metalloproteinases (MMPs) in human serum by antibodies against enzyme therapeutics: T.J. Edkins, et al.; J. Pharm. Biomed. Anal. 70, 408 (2012), Abstract
Kinetics and thermodynamics of irreversible inhibition of matrix metalloproteinase 2 by a Co(III) Schiff base complex: A.S. Harney, et al.; J. Biol. Inorg. Chem. 17, 853 (2012), Abstract — Full Text
Targeted imaging of the spatial and temporal variation of matrix metalloproteinase activity in a porcine model of postinfarct remodeling: relationship to myocardial dysfunction: Z. Sahul, et al.; Circ. Cardiovasc. Imaging 4, 381 (2011), Abstract — Full Text

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Alternative Name	Galardin, Ilomastat, N-[(2R)-2-(Hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan methylamide
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MMP-2 (catalytic domain) (human), (recombinant)

BML-SE237

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

Manuals And Inserts

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