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Recombinant Human Matrix metalloproteinase-26 (MMP26)

ACP10280

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP10280 Target NameMMP26
Target SynonymsMMP26; Matrix metalloproteinase-26; MMP-26; EC 3.4.24.-; Endometase; Matrilysin-2FormLyophilized powder
Expression SystemCustom Production. Please inquire and provide the desire expression system.Expression Range90-261
Protein LengthFull Length of Mature ProteinPurity>85% (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 IDQ9NRE1
Background Information
  • Uniprot Id

    Q9NRE1

  • Target Species

    Human

  • Target Name

    MMP26

  • Target Full Name

    Matrix metalloproteinase-26

  • Target Function

    May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.

  • Target Subcellular Location

    Secreted, extracellular space, extracellular matrix.

  • Target Protein Families

    Peptidase M10A family

  • Target Tissue Specificity

    Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines.

  • Target Synonyms

    MMP26; Matrix metalloproteinase-26; MMP-26; EC 3.4.24.-; Endometase; Matrilysin-2

  • 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. The encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme may degrade collagen type IV, fibronectin, fibrinogen, and beta-casein, and activate matrix metalloproteinase-9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The encoded protein may promote cell invasion in multiple human cancers.

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