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MMP2 antibody (Matrix Metalloproteinase 2)

Details for Product anti-MMP2 Antibody No. ABIN371655, Supplier: Login to see
Antigen
  • 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
Reactivity
Human
309
115
105
11
8
6
6
5
2
1
1
1
1
1
1
1
1
Host
Mouse
220
101
6
2
2
1
Clonality (Clone)
Monoclonal ()
Conjugate
This MMP2 antibody is un-conjugated
17
12
8
3
3
3
3
3
3
3
3
3
3
3
3
2
2
2
1
1
Application
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
242
118
82
74
51
44
33
33
11
8
5
5
2
1
1
1
1
Supplier
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Immunogen Recombinant MMP-2.
Clone SB13a
Isotype IgG1
Specificity This antibody is specific for Human MMP-2. Does not cross react to Human MMP-1, MMP-3 or MMP-9.
Characteristics Synonyms: MMP2, CLG4A, 72 kDa gelatinase, Matrix metalloproteinase-2, Gelatinase A, TBE-1, 72 kDatype IV collagenase
Purification Purified
Alternative Name MMP-2 (MMP2 Antibody Abstract)
Background The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis. MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.Synonyms: 72 kDa gelatinase, 72 kDa type IV collagenase, CLG4A, Gelatinase A, MMP2, Matrix metalloproteinase-2, TBE-1
Gene ID 4313
UniProt P08253
Research Area Extracellular Matrix
Pathways
Application Notes ELISA: 1/3,000-1/8,000. Immunohistochemistry (Frozen/Paraffin): < / = 2 μg/mL.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 0.5 mg/mL
Buffer 100 mM Borate buffered saline, pH 8.2. No preservatives or amine-containing buffer salts added.
Storage 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing.
Shelf life: one year from despatch.
Expiry Date 12 months
Background publications Faisal Khan, Laurie, McCaffrey et al.: "Exposure of cryptic domains in the alpha 1-chain of laminin-1 by elastase stimulates macrophages urokinase and matrix metalloproteinase-9 expression." in: The Journal of biological chemistry, Vol. 277, Issue 16, pp. 13778-86, 2002 (PubMed).

Giannelli, Falk-Marzillier, Schiraldi et al.: "Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5." in: Science (New York, N.Y.), Vol. 277, Issue 5323, pp. 225-8, 1997 (PubMed).

Chandler, Coates, Gearing et al.: "Matrix metalloproteinases degrade myelin basic protein." in: Neuroscience letters, Vol. 201, Issue 3, pp. 223-6, 1996 (PubMed).

Knäuper, Will, López-Otin et al.: "Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme." in: The Journal of biological chemistry, Vol. 271, Issue 29, pp. 17124-31, 1996 (PubMed).

Aimes, Quigley: "Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments." in: The Journal of biological chemistry, Vol. 270, Issue 11, pp. 5872-6, 1995 (PubMed).

Sires, Dublet, Aubert-Foucher et al.: "Degradation of the COL1 domain of type XIV collagen by 92-kDa gelatinase." in: The Journal of biological chemistry, Vol. 270, Issue 3, pp. 1062-7, 1995 (PubMed).

Fridman, Toth, Peña et al.: "Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2)." in: Cancer research, Vol. 55, Issue 12, pp. 2548-55, 1995 (PubMed).

Steffensen, Wallon, Overall: "Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen." in: The Journal of biological chemistry, Vol. 270, Issue 19, pp. 11555-66, 1995 (PubMed).

Collier, Wilhelm, Eisen et al.: "H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen." in: The Journal of biological chemistry, Vol. 263, Issue 14, pp. 6579-87, 1988 (PubMed).

Seltzer, Eisen, Bauer et al.: "Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin." in: The Journal of biological chemistry, Vol. 264, Issue 7, pp. 3822-6, 1989 (PubMed).

Senior, Griffin, Fliszar et al.: "Human 92- and 72-kilodalton type IV collagenases are elastases." in: The Journal of biological chemistry, Vol. 266, Issue 12, pp. 7870-5, 1991 (PubMed).