A part of MilliporeSigma

MAB13426 | Anti-MMP-13 Antibody, clone LIPCO IID1

100 µg  
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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      M, R WB M Purified Monoclonal Antibody
      Catalogue NumberMAB13426
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-MMP-13 Antibody, clone LIPCO IID1
      Alternate Names
      • Collagenase-3
      Product Information
      • POSITIVE CONTROL: Conditioned, serum-free medium from (PMA-treated) rat fibrosarcoma cells or rat keratinocyte CCL-4.
      ApplicationAnti-MMP-13 Antibody, clone LIPCO IID1 is an antibody against MMP-13 for use in WB.
      Key Applications
      • Western Blotting
      Application NotesWestern Blotting (Lyons, 1991; Lyons, 1993): 1:200-1:400 at room temperature for 2 hours.


      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenRat MMP-13 from BC-1 cells.
      Clone LIPCO IID1
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityIt recognizes proteins of ~60 kDa and ~48 kDa which are identified as pro (latent) and activate forms of matrix metalloproteinase-13 (MMP-13; also known as Collagenase-3). Antibody shows no cross-reactivity with the pro and active forms of other MMPs. Human collagenase-3 (MMP13) is a recently identified member of the matrix metalloproteinase (MMP) family that is expressed in breast carcinomas and in articular cartilage from arthritic patients. The MMP-13 gene has been isolated and characterized. This gene is composed of 10 exons and 9 introns and spans over 12.5 kb. The overall organization of the collagenase-3 gene is similar to that of other MMP genes clustered at chromosome 11q22, including fibroblast collagenase (MMP-1), matrilysin (MMP-7), and macrophage metalloelastase (MMP-12), but is more distantly related to genes coding for stromelysin-3 (MMP-11), gelatinase-A (MMP-2), and gelatinase-B (MMP-9), which map outside of this gene cluster.

      Cellular Localization:

      Species Reactivity
      • 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. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
      Gene Symbol
      • MMP13
      • MMP-13
      • CLG3
      • EC 3.4.24.-
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P45452 # Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process.
      COFACTOR: Binds 4 calcium ions per subunit. & Binds 2 zinc ions per subunit.
      SIZE: 471 amino acids; 53820 Da
      TISSUE SPECIFICITY: Seems to be specific to breast carcinomas.
      DOMAIN: SwissProt: P45452 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.
      DISEASE: SwissProt: P45452 # Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2) [MIM:602111]; also known as spondyloepimetaphyseal dysplasia type Missouri. SEMDs are a heterogeneous group of skeletal disorders characterized by defective growth and modeling of the spine and long bones. The SEMDs are distinguished from the spondylometaphyseal dysplasias and the spondyloepiphyseal dysplasias by the combined involvement of the epiphyses and metaphyses. The 3 disorders have malformations of the vertebrae in common.
      SIMILARITY: Belongs to the peptidase M10A family. & 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.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-RAT MMP-13 (COLLAGENASE-3) -2602773 2602773
      MOUSE ANTI-RAT MMP-13 (COLLAGENASE-3) -2698441 2698441
      MOUSE ANTI-RAT MMP-13 (COLLAGENASE-3) -2726139 2726139
      MOUSE ANTI-RAT MMP-13 (COLLAGENASE-3) -2749226 2749226


      Reference overviewPub Med ID
      SUMO1 regulates endothelial function by modulating the overall signals in favor of angiogenesis and homeostatic responses.
      Yang, Ping, et al.
      Am J Transl Res, 5: 427-40 (2013) 2013

      Show Abstract
      23724166 23724166
      Protective effects of allopurinol against acute liver damage and cirrhosis induced by carbon tetrachloride: modulation of NF-κB, cytokine production and oxidative stress.
      Liseth R Aldaba-Muruato,Mario G Moreno,Mineko Shibayama,Víctor Tsutsumi,Pablo Muriel
      Biochimica et biophysica acta 1820 2012

      Show Abstract
      22056511 22056511
      Microarray and proteomic analysis of breast cancer cell and osteoblast co-cultures: role of osteoblast matrix metalloproteinase (MMP)-13 in bone metastasis.
      Morrison, C; Mancini, S; Cipollone, J; Kappelhoff, R; Roskelley, C; Overall, C
      The Journal of biological chemistry 286 34271-85 2011

      Show Abstract
      21784845 21784845
      Noninvasive assessment of UV-induced skin damage: comparison of optical measurements to histology and MMP expression.
      Papazoglou E, Sunkari C, Neidrauer M, Klement JF, Uitto J
      Photochem Photobiol 86 138-45. Epub 2009 Nov 10. 2010

      Show Abstract
      19906094 19906094
      Discoidin domain receptor 2 is associated with the increased expression of matrix metalloproteinase-13 in synovial fibroblasts of rheumatoid arthritis.
      Jin Su,Jiangtian Yu,Tingting Ren,Wei Zhang,Yuanqiang Zhang,Xinping Liu,Tiezheng Sun,Houshan Lu,Keiji Miyazawa,Libo Yao
      Molecular and cellular biochemistry 330 2009

      Show Abstract
      19415460 19415460
      A matrix metalloproteinase-9 activation cascade by hepatic stellate cells in trans-differentiation in the three-dimensional extracellular matrix.
      Han, YP; Yan, C; Zhou, L; Qin, L; Tsukamoto, H
      The Journal of biological chemistry 282 12928-39 2007

      Show Abstract
      17322299 17322299
      Conditional activation of RET/PTC3 and BRAFV600E in thyroid cells is associated with gene expression profiles that predict a preferential role of BRAF in extracellular matrix remodeling.
      Cleo Mesa, Mana Mirza, Norisato Mitsutake, Maureen Sartor, Mario Medvedovic, Craig Tomlinson, Jeffrey A Knauf, Georg F Weber, James A Fagin
      Cancer research 66 6521-9 2006

      Show Abstract
      16818623 16818623
      Essential role of matrix metalloproteinases in interleukin-1-induced myofibroblastic activation of hepatic stellate cell in collagen.
      Han, YP; Zhou, L; Wang, J; Xiong, S; Garner, WL; French, SW; Tsukamoto, H
      The Journal of biological chemistry 279 4820-8 2004

      Show Abstract
      14617627 14617627

      Data Sheet


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      Life Science Research > Antibodies and Assays > Primary Antibodies