Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) Protein

Details for Product No. ABIN2666506, Supplier: Log in to see
Protein Name
  • 2-MMP
  • CG1794
  • DM2-MMP
  • Dm2-MMP
  • Dmel\\CG1794
  • MMP2
  • anon-WO0118547.84
  • dm-2MMP
  • dmmp2
  • l(2)02353
  • mmp2
  • wu:fa99h12
  • wu:fk89d01
  • fgmmp-2
  • Mmp-2
  • LOC100135793
  • Clg4a
  • GelA
  • MMP-2
  • CLG4
  • CLG4A
  • MMP-II
  • MONA
  • TBE-1
  • matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
  • Matrix metalloproteinase 2
  • matrix metalloproteinase 2
  • matrix metalloproteinase-2
  • matrix metallopeptidase 2
  • MMP2
  • Mmp2
  • mmp2
  • mmp-2
  • Mmp-2
  • LOC100135793
Protein Characteristics
C-Term, AA 34-662
5
4
4
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
Origin
Mouse (Murine)
34
5
3
Source
HEK-293
18
4
4
4
2
2
2
2
1
1
1
Protein Type
Recombinant
Biological Activity
Active
Application
Immunofluorescence (IF), Western Blotting (WB)
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Purity > 95 % , as determined by Coomassie stained SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level

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

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
Research Area Extracellular Matrix
Pathways Activation of Innate immune Response
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.
Supplier Images
ELISA image for Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein (ABIN2666506) Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein
ELISA image for Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein (ABIN2666506) Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein (Image 2)
SDS-PAGE (SDS) image for Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein (ABIN2666506) Matrix Metalloproteinase 2 (MMP2) (C-Term), (AA 34-662) (Active) protein (Image 3)
Background publications Qian, Wang, Zhan, Peng, Wei, Shi, Song: "The role of matrix metalloproteinase 2 on the survival of patients with non-small cell lung cancer: a systematic review with meta-analysis." in: Cancer investigation, Vol. 28, Issue 6, pp. 661-9, 2010 (PubMed).

Hoikkala, Pääkkö, Soini, Mäkitaro, Kinnula, Turpeenniemi-Hujanen: "Tissue MMP-2 and MMP-9 [corrected] are better prognostic factors than serum MMP-2/TIMP-2--complex or TIMP-1 [corrected] in stage [corrected] I-III lung carcinoma." in: Cancer letters, Vol. 236, Issue 1, pp. 125-32, 2006 (PubMed).

Yamamura, Nakanishi, Hiroi, Kumaki, Sato, Aida, Kawai: "Expression of membrane-type-1-matrix metalloproteinase and metalloproteinase-2 in nonsmall cell lung carcinomas." in: Lung cancer (Amsterdam, Netherlands), Vol. 35, Issue 3, pp. 249-55, 2002 (PubMed).

Passlick, Sienel, Seen-Hibler, Wöckel, Thetter, Mutschler, Pantel: "Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 6, Issue 10, pp. 3944-8, 2001 (PubMed).

Martignetti, Aqeel, Sewairi, Boumah, Kambouris, Mayouf, Sheth, Eid, Dowling, Harris, Glucksman, Bahabri, Meyer, Desnick: "Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome." in: Nature genetics, Vol. 28, Issue 3, pp. 261-5, 2001 (PubMed).

Nagase, Woessner: "Matrix metalloproteinases." in: The Journal of biological chemistry, Vol. 274, Issue 31, pp. 21491-4, 1999 (PubMed).

Itoh, Ikeda, Gomi, Nakao, Suzuki, Itohara: "Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice." in: The Journal of biological chemistry, Vol. 272, Issue 36, pp. 22389-92, 1997 (PubMed).

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