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Details for Product No. ABIN371655

Matrix Metalloproteinase 2 (MMP2) antibody

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Antigen
Synonyms
CLG4, MONA, CLG4A, TBE-1, MMP-II, GelA, Clg4a, MMP-2, 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, L ... show more
Reactivity
»Alternatives Human
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Conjugate
»Alternatives Un-conjugated
Application
»Alternatives Immunohistochemistry (Frozen Sections) (IHC (fro)), ELISA, Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Pubmed 11 references available
Catalog no. ABIN371655
Quantity 0.1 mg
Price
297.00 $   Plus shipping costs $45.00
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Availability Will be delivered in 6 to 8 Business Days
Immunogen Recombinant MMP-2.
Clone SB13a
Isotype IgG1
Characteristics Synonyms: MMP2, CLG4A, 72 kDa gelatinase, Matrix metalloproteinase-2, Gelatinase A, TBE-1, 72 kDatype IV collagenase
Purification Purified
Alternative Name MMP-2
Background The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted andmembrane-bound zinc endopeptidases. Collectively, these enzymes can degrade all thecomponents of the extracellular matrix, including fibrillar and non-fibrillar collagens,fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, apropeptide, and a catalytic domain containing the highly conserved zinc-binding sitecharacterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hingeregion, and a C terminal hemopexin-like domain allow categorization of MMPs into thecollagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs aresynthesized 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 matrixbreakdown. MMPs are considered to play an important role in wound healing, apoptosis,bone elongation, embryo development, uterine involution, angiogenesis and tissueremodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas,lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and incancer cell invasion and metastasis. MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves typeIV collagen, the major structural component of basement membranes. The metastaticpotential of tumor cells has been found to correlate with the activity of this enzyme.
UniProt P08253
Research Area Extracellular Matrix
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
Format Liquid
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 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).

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).

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).

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).

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).

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).

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).

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).

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

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).

Alternatives for antigen "Matrix Metalloproteinase 2 (MMP2)", type "Antibodies"
Hosts (146), (101), (5), (2), (1)
Reactivities (233), (104), (94), (43), (38), (25), (13), (1), (1), (1), (1), (1)
Applications (197), (101), (99), (59), (39), (34), (30), (27), (21), (17), (10), (6), (2), (1), (1), (1), (1), (1)
Conjugates (19), (12), (6), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (1), (1)
Epitopes (13), (11), (8), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
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