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Official Full Name matrix metallopeptidase 20
Background Proteins 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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene degrades amelogenin, the major protein component of dental enamel matrix, and thus thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. This gene is part of a cluster of MMP genes located on chromosome 11q22.3. [provided by RefSeq, Aug 2011]
Synonyms MMP20; matrix metallopeptidase 20; AI2A2; MMP-20; matrix metalloproteinase-20; enamel metalloproteinase; matrix metalloproteinase 20 (enamelysin);
    • Species :
    • Human
    • Mouse
    • Rhesus Macaque
    • Source :
    • E.coli
    • HEK293
    • Mammalian Cell
    • Tag :
    • His
    • T7
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human MMP20-162H Recombinant Human MMP20, Catalytic Domain E.coli N/A
    Human MMP20-4276HCL Recombinant Human MMP20 293 Cell Lysate HEK293 N/A
    Human MMP20-541H Recombinant Human MMP20 Protein, His-tagged E.coli His
    Mouse Mmp20-1881M Recombinant Mouse Mmp20 protein, His & T7-tagged E.coli His/T7
    Mouse MMP20-9917M Recombinant Mouse MMP20 Protein Mammalian Cell His
    Rhesus Macaque MMP20-2791R Recombinant Rhesus monkey MMP20 Protein, His-tagged Mammalian Cell His

    mmp20 involved in several pathways and played different roles in them. We selected most pathways mmp20 participated on our site, such as Assembly of collagen fibrils and other multimeric structures, Collagen degradation, Collagen formation, which may be useful for your reference. Also, other proteins which involved in the same pathway with mmp20 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Assembly of collagen fibrils and other multimeric structures COL8A2; COL5A2; ABHD1; LOXL4; TLL2; DST; COL3A1; LOXL1; CTSB; COL8A1
    Collagen degradation MMP11; ADAM9; MMP13; CTSB; CTSLL; EMID2; COL15A1B; MMP19; CTSK; ADAM10
    Collagen formation P3H2; COL4A6; COL4A3; COL13A1; BMP1B; COL17A1; TLL1; CTSB; PCOLCE2; ABHD1
    Degradation of the extracellular matrix CTSL1; MMP19; MMP10; BMP1; MMP12; BSG; TLL1; KLK7; CTRB1; CTSLL
    Extracellular matrix organization COL13A1; P3H2; MGC174857; COL15A1B; KLK7; EFEMP2; COL4A5; CTSG; ADAMTS3; COL4A4
    Matrix Metalloproteinases MMP8; MMP11; MMP23B; BSG; MMP17; TIMP4; MMP20; MMP10; MMP12; MMP25

    mmp20 has several biochemical functions, for example, calcium ion binding, metalloendopeptidase activity, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by mmp20 itself. We selected most functions mmp20 had, and list some proteins which have the same functions with mmp20. You can find most of the proteins on our site.

    Function Related Protein
    calcium ion binding KCNIP3; CAPN2B; ZFP652; CDH19; CD97; ANXA2A; ITSN1; ANXA1C; CDH17; VSNL1A
    metalloendopeptidase activity PHEX; MMP25; MMP19; AFG3L2; ADAMTS15; HE1A; ADAM10; ADAMDEC1; MEP1A; ADAM7
    protein binding NGFR; OLR1; RABEP1; ACTR3; TGIF2LY; DDB1; MYF5; PLEKHB2; PHF7; MYH7
    zinc ion binding OTUD7B; CSRP2; RNF220A; MLLT10; LDB3; VAT1L; ZCCHC17; RNF169; NRAP; RNF170

    mmp20 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with mmp20 here. Most of them are supplied by our site. Hope this information will be useful for your research of mmp20.

    Satchell, PG; Anderton, X; et al. Conservation and variation in enamel protein distribution during vertebrate tooth development. JOURNAL OF EXPERIMENTAL ZOOLOGY 294:91-106(2002).

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