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MAB13405 | Anti-MMP-2 Proform Antibody, NT, clone CA-4001

100 µg  
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      Replacement Information

      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, M, R WB, IH(P), FUNC M Purified Monoclonal Antibody
      Catalogue NumberMAB13405
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-MMP-2 Proform Antibody, NT, clone CA-4001
      Alternate Names
      • Gelatinase A
      • 72 kDa Type IV Collagenase
      Product Information
      • POSITIVE CONTROL: HFL-1 cells. Conditioned, serum-free medium from (TPA-treated) human fetal lung cells. Placenta.
      PresentationPurified from ascites fluid by Protein G chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 15 mM sodium azide
      ApplicationAnti-MMP-2 Proform Antibody, N-terminus, clone CA-4001 detects level of MMP-2 Proform & has been published & validated for use in WB, IH(P).
      Key Applications
      • Western Blotting
      • Immunohistochemistry (Paraffin)
      • Affects Function
      Application NotesWestern Blot (0.5-1.0 μg/mL for 2 hours at room temperature, non-reduced conditions. However, chicken samples react best when fully reduced. Antibody dilution buffers should be simple for best results, PBS or TBS with 0.05% tween only. Immunogen used is highly conserved between species, thus immunoabsorption to pro-MMP2 in milk may impair reactivity.

      Immunohistochemistry on frozen and formalin-fixed, paraffin-embedded tissue sections: 2-10 μg/mL for 30 minutes at room temperature. {Seftor, et al 2001} and Gottsch ML et al 2002}. Antigen retrieval is optional in most cases. Antibody dilution solutions should not contain serum because of possible immunoabsorption of the antibody to proMMP2 present in the solution.

      Blocking: Inhibition of MMP-2 Activity (2-4 μg/mL).

      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenN-terminal peptide APSPIIKFPGDVAPKTDK of procollagenase IV, coupled to KLH.{Marqulies, et al 1992}
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityIt recognizes a protein of 72 kDa which is identified as pro (latent) form (active form is 62 kDa) of matrix metalloproteinase-2 and any fragment with N-terminal (proform) domain still attached. Antibody shows no cross-reaction with pro and active forms of MMP-9. MMP-2 is synthesized as 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids. MMPs have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). Cellular Localization: Cytoplasmic.
      Species Reactivity
      • Human
      • Mouse
      • Rat
      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
      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.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • 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 at 2-8°C in undiluted aliquots for up to 12 months after date of receipt.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2608478 2608478
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2616189 2616189
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2705121 2705121
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2739487 2739487
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2784239 2784239
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2802043 2802043
      MOUSE ANTI-HUMAN MMP-2 (PROFORM) -2804210 2804210

      References | 25 Available | See All References

      Reference overviewPub Med ID
      Cadherin-6B is proteolytically processed during epithelial-to-mesenchymal transitions of the cranial neural crest.
      Schiffmacher, AT; Padmanabhan, R; Jhingory, S; Taneyhill, LA
      Molecular biology of the cell 25 41-54 2014

      Show Abstract
      24196837 24196837
      Senescent cancer-associated fibroblasts secrete active MMP-2 that promotes keratinocyte dis-cohesion and invasion.
      Hassona, Y; Cirillo, N; Heesom, K; Parkinson, EK; Prime, SS
      British journal of cancer 111 1230-7 2014

      Show Abstract
      25117810 25117810
      Matrix metalloproteinase-2 cleavage of the β1 integrin ectodomain facilitates colon cancer cell motility.
      Kryczka, J; Stasiak, M; Dziki, L; Mik, M; Dziki, A; Cierniewski, C
      The Journal of biological chemistry 287 36556-66 2012

      Show Abstract
      22898815 22898815
      Involvement of S100A14 protein in cell invasion by affecting expression and function of matrix metalloproteinase (MMP)-2 via p53-dependent transcriptional regulation.
      Chen, H; Yuan, Y; Zhang, C; Luo, A; Ding, F; Ma, J; Yang, S; Tian, Y; Tong, T; Zhan, Q; Liu, Z
      The Journal of biological chemistry 287 17109-19 2012

      Show Abstract
      22451655 22451655
      Tissue inhibitor of metalloproteinase-2 regulates matrix metalloproteinase-2-mediated endothelial barrier dysfunction and breast cancer cell transmigration through lung microvascular endothelial cells.
      Shen Q, Lee ES, Pitts RL, Wu MH, Yuan SY
      Mol Cancer Res 8 939-51. Epub 2010 Jun 22. 2010

      Show Abstract
      20571065 20571065
      Chromosome 7 and 19 trisomy in cultured human neural progenitor cells.
      Sareen, D; McMillan, E; Ebert, AD; Shelley, BC; Johnson, JA; Meisner, LF; Svendsen, CN
      PloS one 4 e7630 2009

      Show Abstract Full Text Article
      19898616 19898616
      Integrin cleavage facilitates cell surface-associated proteolysis required for vascular smooth muscle cell invasion.
      Kai Kappert, Heike Meyborg, Bernadette Baumann, Vesna Furundzija, Jan Kaufmann, Kristof Graf, Dietger Stibenz, Eckart Fleck, Philipp Stawowy, Kai Kappert, Heike Meyborg, Bernadette Baumann, Vesna Furundzija, Jan Kaufmann, Kristof Graf, Dietger Stibenz, Eckart Fleck, Philipp Stawowy, Kai Kappert, Heike Meyborg, Bernadette Baumann, Vesna Furundzija, Jan Kaufmann, Kristof Graf, Dietger Stibenz, Eckart Fleck, Philipp Stawowy, Kai Kappert, Heike Meyborg, Bernadette Baumann, Vesna Furundzija, Jan Kaufmann, Kristof Graf, Dietger Stibenz, Eckart Fleck, Philipp Stawowy
      The international journal of biochemistry cell biology 41 1511-7 2009

      Show Abstract
      19166965 19166965
      MMP-14 and TIMP-2 overexpression protects against hydroquinone-induced oxidant injury in RPE: implications for extracellular matrix turnover.
      Alcazar, O; Cousins, SW; Marin-Castaño, ME
      Investigative ophthalmology & visual science 48 5662-70 2007

      Show Abstract
      18055817 18055817
      Vascular matrix metalloproteinase-9 mediates the inhibition of myogenic reactivity in small arteries isolated from rats after short-term administration of relaxin.
      Jeyabalan, A; Novak, J; Doty, KD; Matthews, J; Fisher, MC; Kerchner, LJ; Conrad, KP
      Endocrinology 148 189-97 2007

      Show Abstract
      17053025 17053025
      Hypoxia stimulates breast carcinoma cell invasion through MT1-MMP and MMP-2 activation.
      Muñoz-Nájar, UM; Neurath, KM; Vumbaca, F; Claffey, KP
      Oncogene 25 2379-92 2006

      Show Abstract
      16369494 16369494


      An Introduction to Antibodies and Their Applications

      Data Sheet

      Anti-MMP-2 Proform, N-terminus, clone CA-4001 - Data Sheet

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