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Your Position: Home > Other Recombinant Proteins > HSA > Human Serum Albumin /HSA Protein

Human HSA Protein

  • Synonym
    HSA,ALB,Serum Albumin
  • Source
    Human HSA, His Tag (HSA-H5220) is expressed from human 293 cells (HEK293). It contains AA Asp 25 - Leu 609 (Accession # NP_000468).
    Predicted N-terminus: Asp 25
  • Molecular Characterization
    HSA(Asp 25 - Leu 609) NP_000468

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

    The protein has a calculated MW of 67.3 kDa. The protein migrates as 66 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 PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

    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.

    No activity loss is observed after storage at:

    1. 4-8°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Human HSA, His Tag (Cat. No. HSA-H5220) SDS-PAGE gel

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

  • Background
    Human serum albumin (HSA) is also known as ALB,which is the main protein of plasma and has a good binding capacity for water,Ca2+,Na+,K+,fatty acids,hormones, bilirubin and drugs.The main function of HSA is the regulation of the colloidal osmotic pressure of blood. As Major zinc transporter in plasma, HSA typically binds about 80% of all plasma zinc.A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. Defects in serum albumin can cause familial dysalbuminemic hyperthyroxinemia which is a form of euthyroid hyperthyroxinemia that is due to increased affinity of serum albumin for T4.It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.
  • References
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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