Human ADAM28 Protein, His Tag

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Cat. No. / Size
Price
Qty
AD8-H52H3-50ug
$450.00
AD8-H52H3-500ug
$1700.00
ETA of in-stock products:2 business days

Product Details

  • Synonyms

    ADAM28​

  • Source

    Human ADAM28 Protein, His Tag (AD8-H52H3) is expressed from human 293 cells (HEK293). It contains AA Val 199 - Phe 665 (Accession # Q9UKQ2).

    Predicted N-terminus: Val 199

    Request for sequence
  • Molecular Characterization

    ADAM28​ Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 54.1 kDa. The protein migrates as 63-70 kDa and 90 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Supplied as 0.2 μm filtered solution in 20 mM MES, 150 mM NaCl, pH6.5 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • SDS-PAGE

    ADAM28​ SDS-PAGE

    Human ADAM28 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

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Background

ADAM28 is a member of the ADAM (A Disintegrin And Metalloprotease) family, which are transmembrane or secreted proteins with diverse functions, including shedding of cell surface proteins, cell adhesion, and proteolysis of extracellular matrix components. ADAM28 possesses both disintegrin and metalloprotease domains, allowing it to mediate cell-cell or cell-matrix interactions and cleave various substrates.

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