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MMP2 Protein (AA 34-662, C-Term)

This Recombinant MMP2 protein is produced in HEK-293 Cells.
Catalog No. ABIN2666505

Quick Overview for MMP2 Protein (AA 34-662, C-Term) (ABIN2666505)

Target

See all MMP2 Proteins
MMP2 (Matrix Metalloproteinase 2 (MMP2))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 22
  • 5
  • 5
  • 2
  • 2
  • 2
  • 1
Mouse

Source

  • 26
  • 7
  • 1
  • 1
  • 1
  • 1
  • 1
HEK-293 Cells

Application

Western Blotting (WB), Immunofluorescence (IF)

Purity

> 95 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    C-Term, AA 34-662

    Sterility

    0.22 μm filtered

    Endotoxin Level

    Less than 0.1 EU per μg of protein as determined by the LAL method.

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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Biological activity: Mouse MMP-2 cleaves the peptide substrate Mca-PLGL-Dpa-AR-NH2 with an activity above 1400 pmol/min/μg.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    For maximum results, quick spin vial prior to opening.

    Buffer

    0.22 μm filtered protein solution is in TCN (25 mM TRIS, 5 mM CaCl2, 150 mM NaCl, pH 7.5).

    Handling Advice

    Avoid repeated freeze/thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Unopened vial can be stored at -70°C for six months.
  • Target

    MMP2 (Matrix Metalloproteinase 2 (MMP2))

    Alternative Name

    MMP-2

    Background

    MMP-2, also known as gelatinase A, is a member of matrix metalloproteinase family proteins (MMPs). MMPs are structurally related, zinc-containing enzymes that degrade the extracellular matrix (ECM) and connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling as well as in disease processes such as arthritis and metastasis. MMP-2 consists of a prodomain, which is cleaved upon activation, a catalytic domain containing the zinc binding site, a fibronectin-like domain (that plays a role in the substrate targeting), and a carboxyl terminal (hemopexin-like repeats) domain. Activation of MMP-2 requires proteolytic processing: a complex of membrane type 1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase 2 recruits pro-MMP-2 from the extracellular milieu to the cell surface. Next, the MMP-2 is activated by active MT1-MMP and subsequently undergoes auto-catalytic cleavage. Substrates of MMP-2 include type IV collagen, aggrecan, link protein, decorin, fibronectin, and type X and XI collagens, all of which are components of the articular cartilaginous matrix. Importantly, MMP-2 secretion is elevated in several types of human cancers and its elevated expression has been associated with poor prognosis. Mutations in the MMP2 gene are associated with Torg-Winchester syndrome, multicentric osteolysis, arthritis syndrome, and possibly keloids. MMP-2 deficient mice exhibit slightly delayed growth, reduced neovascularization, retarded tumor progression, an exaggerated asthma response to allergens, and impaired branching morphogenesis of the mammary gland.

    Molecular Weight

    This 663 amino acid recombinant protein has a predicted molecular mass of approximately 74.5 kDa. The protein migrates at about 72 kDa in DTT-reducing conditions and about 71 kDa in non-reducing conditions by SDS-PAGE.The predicted N-terminal amino acid i

    Pathways

    Activation of Innate immune Response
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