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Recombinant Human Matrix metalloproteinase-20 (MMP20)

The plasmid vector incorporates the gene encoding the Human MMP20 protein (108-483aa), generating recombinant plasmid, which is then introduced into baculovirus cells. Selection of positive baculovirus cells is based on their capacity to withstand a particular antibiotic. Subsequently, the baculovirus cells containing the recombinant plasmid are cultivated under conditions that facilitate the expression of the Human MMP20 gene. The protein carries a N-terminal 10xHis tag and C-terminal Myc tag. Following expression, affinity purification is employed to isolate and purify the recombinant Human MMP20 protein from the cell lysate. Denaturing SDS-PAGE is used to resolve the resulting recombinant protein, enabling an estimation of its purity, exceeding 85%.

ACP05039

The plasmid vector incorporates the gene encoding the Human MMP20 protein (108-483aa), generating recombinant plasmid, which is then introduced into baculovirus cells. Selection of positive baculovirus cells is based on their capacity to withstand a particular antibiotic. Subsequently, the baculovirus cells containing the recombinant plasmid are cultivated under conditions that facilitate the expression of the Human MMP20 gene. The protein carries a N-terminal 10xHis tag and C-terminal Myc tag. Following expression, affinity purification is employed to isolate and purify the recombinant Human MMP20 protein from the cell lysate. Denaturing SDS-PAGE is used to resolve the resulting recombinant protein, enabling an estimation of its purity, exceeding 85%.

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Specifications


Cat.No ACP05039 Target NameMMP20
Target SynonymsAI2A2; Enamel metalloproteinase; Enamelysin; Matrix metalloproteinase 20; Matrix metalloproteinase-20; MMP 20; MMP-20; MMP20; MMP20_HUMANFormLiquid or Lyophilized powder
Expression SystemBaculovirusExpression Range108-483aa
Mol Weight46.4Protein LengthFull Length of Mature Protein
PurityGreater than 85% as determined by SDS-PAGE.Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDO60882
Background Information
  • Uniprot Id

    O60882

  • Target Species

    Human

  • Target Name

    MMP20

  • Target Full Name

    Matrix metalloproteinase-20

  • Target Function

    Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.

  • Target Involvement

    Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2)

  • Target Subcellular Location

    Secreted, extracellular space, extracellular matrix.

  • Target Protein Families

    Peptidase M10A family

  • Target Tissue Specificity

    Expressed specifically in the enamel organ.

  • Target Research Area

    Others

  • Target Synonyms

    AI2A2; Enamel metalloproteinase; Enamelysin; Matrix metalloproteinase 20; Matrix metalloproteinase-20; MMP 20; MMP-20; MMP20; MMP20_HUMAN

  • Target 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 MMP's 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.

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