Human CYB5R3 Protein, His Tag

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製品番号/仕様
価格
数量
CY3-H5143-100ug
$360.00
CY3-H5143-1mg
$2380.00
ETA of in-stock products:2 business days
総アイテム数 製品金額$ 0

製品詳細

  • Synonyms

    CYB5R3

  • Source

    Human CYB5R3 Protein, His Tag (CY3-H5143) is expressed from E. coli cells. It contains AA Lys 2 - Phe 278 (Accession # P00387-2).

    Predicted N-terminus: Met

    Request for sequence
  • Molecular Characterization

    CYB5R3 Structure

    Other Tags and Version Biotin & Other Labeled Version

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

    The protein has a calculated MW of 33.5 kDa. The protein migrates as 33-35 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

  • Endotoxin

    Less than 1.0 EU per μg by the LAL method / rFC method.

  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, 0.2 M Arginine, pH7.4 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.
  • ACRO Quality Management System

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

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データ表示

  • SDS-PAGE

    CYB5R3 SDS-PAGE

    Human CYB5R3 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 95% (With Star Ribbon Pre-stained Protein Marker).

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バックグランド

CYB5R3 (Cytochrome B5 Reductase 3) encodes cytochrome b5 reductase, which includes a membrane-bound form in somatic cells (anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in erythrocytes. The membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic reticulum and functions in desaturation and elongation of fatty acids, in cholesterol biosynthesis, and in drug metabolism. The erythrocyte form is located in a soluble fraction of circulating erythrocytes and is involved in methemoglobin reduction. The membrane-bound form has both membrane-binding and catalytic domains, while the soluble form has only the catalytic domain. Alternate splicing results in multiple transcript variants. Mutations in this gene cause methemoglobinemias.

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