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MMP11 Protein (AA 32-488) (Fc Tag)

MMP11 Origine: Humain Hôte: HEK-293 Cells Recombinant The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
N° du produit ABIN6964295
  • Antigène Voir toutes MMP11 Protéines
    MMP11 (Matrix Metallopeptidase 11 (Stromelysin 3) (MMP11))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 32-488
    Origine
    • 3
    • 3
    • 2
    • 1
    Humain
    Source
    • 6
    • 2
    • 1
    HEK-293 Cells
    Purification/Conjugué
    Cette MMP11 protéine est marqué à la Fc Tag.
    Fonction
    Recombinant human MMP11 protein with C-terminal human Fc tag
    Specificité
    MMP11 (Arg32-Leu488) hFc (Glu99-Ala330)
    Attributs du produit
    Extracellular Domain Protein
    Purification
    Purified from cell culture supernatant by affinity chromatography
    Pureté
    The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization.
    Stock
    -20 °C,-80 °C
    Stockage commentaire
    Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.
    Date de péremption
    12 months
  • Antigène
    MMP11 (Matrix Metallopeptidase 11 (Stromelysin 3) (MMP11))
    Autre désignation
    MMP11 (MMP11 Produits)
    Synonymes
    SL-3 Protein, ST3 Protein, STMY3 Protein, Stmy3 Protein, MMP-11 Protein, matrix metallopeptidase 11 Protein, matrix metallopeptidase 11 L homeolog Protein, stromelysin-3 Protein, MMP11 Protein, Mmp11 Protein, mmp11.L Protein, LOC103694874 Protein
    Sujet
    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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [provided by RefSeq, Jul 2008]
    Poids moléculaire
    predicted molecular mass of 76.5 kDa after removal of the signal peptide.The apparent molecular mass of MMP11-hFc is 70-100 kDa due to glycosylation.
    UniProt
    P24347
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