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Cynomolgus ADAM9 Protein, His Tag (active enzyme)

  • Synonym
    Disintegrin and metalloproteinase domain-containing protein 9 (EC:3.4.24.-) Cellular disintegrin-related protein,Meltrin-gamma,Metalloprotease,disintegrin,cysteine-rich protein 9,Myeloma cell metalloproteinase,ADAM9,KIAA0021, MCMP, MDC9, MLTNG
  • Source
    Cynomolgus ADAM9, His Tag(AD9-C52H7) is expressed from human 293 cells (HEK293). It contains AA Ala 206 - Asp 697 (Accession # A0A2K5X4X8-1).
    Predicted N-terminus: Ala 206
  • Molecular Characterization
    ADAM9 Structure

    This protein carries a polyhistidine tag at the C-terminus

    The protein has a calculated MW of 55.3 kDa. The protein migrates as 65-70 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 20 mM Tris, 500 mM NaCl, pH7.3 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
ADAM9 SDS-PAGE

Cynomolgus ADAM9, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

Bioactivity

Measured by its ability to cleave a fluorogenic peptide substrate Mca-PLAQAV-Dpa-RSSSR-NH2. The specific activity is >50 pmol/min/µg (QC tested).

  • Background
    ADAM9 (A disintegrin and a metalloprotease 9) is a membrane-anchored protein that participates in a variety of physiological functions, primarily through the disintegrin domain for adhesion and the metalloprotease domain for ectodomain shedding of a wide variety of cell surface proteins. ADAM9 influences the developmental process, inflammation, and degenerative diseases.Recently, increasing evidence has shown that ADAM9 plays an important role in tumor biology. Overexpression of ADAM9 has been found in several cancer types and is correlated with tumoraggressiveness and poor prognosis. In addition, through either proteolytic or non-proteolytic pathways, ADAM9 promotes tumor progression, therapeutic resistance, and metastasis of cancers.Therefore, comprehensively understanding the mechanism of ADAM9 is crucial for the development of therapeutic anti-cancer strategies. In this review, we summarize the current understanding of ADAM9 in biological function, pathophysiological diseases, and various cancers. Recent advances in therapeutic strategies using ADAM9-related pathways are presented as well.
  • Clinical and Translational Updates

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