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MAB3308 | Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11

100 µg  
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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      B, Eq, H, M, Po, R, Rb ELISA, IH(P), WB M Purified Monoclonal Antibody
      Catalogue NumberMAB3308
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11
      Alternate Names
      • Gelatinase A
      • 72 kDa Type IV Collagenase
      Background InformationThe 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. 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.
      Product Information
      • Lung, nerve, and various soft tissue tumors
      PresentationLiquid in 0.1 M sodium phosphate buffer, pH 7.0 containing 2% protease free bovine Serum albumin.
      ApplicationThis Anti-MMP-2 Antibody, a.a. 468-483 hMMP2, clone 42-5D11 is validated for use in ELISA, IH(P), WB for the detection of MMP-2.
      Key Applications
      • ELISA
      • Immunohistochemistry (Paraffin)
      • Western Blotting
      Application NotesImmunoblotting 1-5 μg/mL

      Immunohistochemistry on frozen and paraffin-embedded tissues using PLP fixation: 1-5 μg/mL (has not been tested in traditional formalin fixed tissues)

      Biological Information
      ImmunogenSynthetic oligopeptide corresponding to amino acid residue 468-483 (VTPRDKPMGPLLVATF) of human matrix metalloproteinase 2 (human MMP-2, gelatinase A).
      Epitopea.a. 468-483 hMMP2
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificitySpecifically reacts with precursor and active forms of human MMP-2. Does not cross react with human MMP-1, -3, -9, or -13. Also reacts with rat, mouse, and bovine MMP2, other species not tested.
      Species Reactivity
      • Bovine
      • Horse
      • Human
      • Mouse
      • Pig
      • Rat
      • Rabbit
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryProteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome.
      Gene Symbol
      • MMP2
      • TBE-1
      • CLG4A
      • CLG4
      • MMP-II
      • MONA
      • MMP-2
      • EC
      Purification MethodProtein A Purfied
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P08253 # In addition to gelatin and collagens, it cleaves KiSS1 at a Gly- -Leu bond.
      COFACTOR: Binds 4 calcium ions per subunit. & Binds 2 zinc ions per subunit.
      SIZE: 660 amino acids; 73882 Da
      SUBUNIT: Ligand for integrin alpha-V/beta-3.
      TISSUE SPECIFICITY: Produced by normal skin fibroblasts.
      DOMAIN: SwissProt: P08253 The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
      PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT- MMP3).
      DISEASE: SwissProt: P08253 # Defects in MMP2 are the cause of multicentric osteolysis nodulosis and arthropathy (MONA) [MIM:605156]. Inherited osteolyses or 'vanishing bone' syndromes are rare disorders of unknown etiology characterized by destruction and resorption of affected bones. MONA is an autosomal recessive osteolysis with multicentric involvement characterized by carpal and tarsal resorption, crippling arthritic changes, marked osteoporosis, palmar and plantar subcutaneous nodules and distinctive facies. & Defects in MMP2 are the cause of Winchester syndrome [MIM:277950]. Winchester syndrome is an autosomal recessive osteolysis syndrome. Winchester syndrome is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes. The clinical and molecular findings suggest that Winchester syndrome and MONA are allelic disorders that form a continuous clinical spectrum.
      SIMILARITY: Belongs to the peptidase M10A family. & Contains 3 fibronectin type-II domains. & Contains 4 hemopexin-like domains.
      Molecular Weight72 kDa
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Availability by Geography
      • This product is not available for sale in Japan.
      Usage Statement
      • Manufactured by Daiichi Fine Chemical Co., Ltd
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-HUMAN MMP-2 - 2491118 2491118
      MOUSE ANTI-HUMAN MMP-2 -2521482 2521482
      MOUSE ANTI-HUMAN MMP-2 -2576360 2576360
      MOUSE ANTI-HUMAN MMP-2 -2665059 2665059
      MOUSE ANTI-HUMAN MMP-2 -2689149 2689149
      MOUSE ANTI-HUMAN MMP-2 -2709166 2709166
      MOUSE ANTI-HUMAN MMP-2 -2746555 2746555

      References | 45 Available | See All References

      Reference overviewPub Med ID
      Folate deficiency decreases apoptosis of endometrium decidual cells in pregnant mice via the mitochondrial pathway.
      Liao, XG; Li, YL; Gao, RF; Geng, YQ; Chen, XM; Liu, XQ; Ding, YB; Mu, XY; Wang, YX; He, JL
      Nutrients 7 1916-32 2015

      Show Abstract
      25781218 25781218
      Inhibition of SHP2 in basal-like and triple-negative breast cells induces basal-to-luminal transition, hormone dependency, and sensitivity to anti-hormone treatment.
      Zhao, H; Agazie, YM
      BMC cancer 15 109 2015

      Show Abstract
      25885600 25885600
      Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model.
      Akkad, H; Corpeno, R; Larsson, L
      PloS one 9 e92622 2014

      Show Abstract
      24705179 24705179
      Endothelial nitric oxide synthase and superoxide mediate hemodynamic initiation of intracranial aneurysms.
      Liaw, N; Fox, JM; Siddiqui, AH; Meng, H; Kolega, J
      PloS one 9 e101721 2014

      Show Abstract
      24992254 24992254
      Histological, histochemical, and protein changes after induced malocclusion by occlusion alteration of Wistar rats.
      Guerra, Cde S; Carla Lara Pereira, Y; Issa, JP; Luiz, KG; Guimarães, EA; Gerlach, RF; Iyomasa, MM
      BioMed research international 2014 563463 2014

      Show Abstract
      25028660 25028660
      Differential effects of caveolin-1 and -2 knockdown on aqueous outflow and altered extracellular matrix turnover in caveolin-silenced trabecular meshwork cells.
      Aga, M; Bradley, JM; Wanchu, R; Yang, YF; Acott, TS; Keller, KE
      Investigative ophthalmology & visual science 55 5497-509 2014

      Show Abstract
      25103269 25103269
      Role of Cox-2 in vascular inflammation: an experimental model of metabolic syndrome.
      Renna, NF; Diez, ER; Lembo, C; Miatello, RM
      Mediators of inflammation 2013 513251 2013

      Show Abstract
      23476105 23476105
      Expression of MMP-2 and MMP-9 in the rat trigeminal ganglion during the development of temporomandibular joint inflammation.
      Nascimento, GC; Rizzi, E; Gerlach, RF; Leite-Panissi, CR
      Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas / Sociedade Brasileira de Biofisica ... [et al.] 46 956-967 2013

      Show Abstract
      24270905 24270905
      Expression of soluble and functional full-length human matrix metalloproteinase-2 in Escherichia coli.
      Gonçalves, AN; Meschiari, CA; Stetler-Stevenson, WG; Nonato, MC; Alves, CP; Espreafico, EM; Gerlach, RF
      Journal of biotechnology 157 20-4 2012

      Show Abstract
      22001844 22001844
      MMP2 and acrosin are major proteinases associated with the inner acrosomal membrane and may cooperate in sperm penetration of the zona pellucida during fertilization.
      Ferrer, M; Rodriguez, H; Zara, L; Yu, Y; Xu, W; Oko, R
      Cell and tissue research 349 881-95 2012

      Show Abstract
      22729485 22729485

      Data Sheet

      Anti-MMP-2, a.a. 468-483 hMMP2, clone 42-5D11 - Data Sheet

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