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Cardiovascular Blood Serum Proteins

Native Human Serum Albumin protein (Rhodamine) (ab8031)

Key features and details

  • Expression system: Native
  • Suitable for: Flow Cyt, Immunomicroscopy

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Description

  • Product name

    Native Human Serum Albumin protein (Rhodamine)
    See all Human Serum Albumin proteins and peptides
  • Expression system

    Native
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Native
    • Species

      Human
    • Predicted molecular weight

      69 kDa
  • Conjugation

    Rhodamine. Ex: 550nm, Em: 570nm
  • Description

    Native Human Human Serum Albumin protein (Rhodamine)

Preparation and Storage

  • Alternative names

    • alb
    • ALBU_HUMAN
    • Albumin
    • Albumin (32 AA)
    • Albumin (AA 34)
    • Analbuminemia
    • Bisalbuminemia
    • Cell growth inhibiting protein 42
    • DKFZp779N1935
    • Dysalbuminemic hyperthyroxinemia
    • Growth inhibiting protein 20
    • HSA
    • Hyperthyroxinemia dysalbuminemic
    • PRO0883
    • PRO0903
    • PRO1341
    • Serum albumin
    see all
  • Function

    Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.
  • Tissue specificity

    Plasma.
  • Involvement in disease

    Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.
  • Sequence similarities

    Belongs to the ALB/AFP/VDB family.
    Contains 3 albumin domains.
  • Post-translational
    modifications

    Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.
    Glycated in diabetic patients.
    Phosphorylation sites are present in the extracelllular medium.
    Acetylated on Lys-223 by acetylsalicylic acid.
  • Cellular localization

    Secreted.
  • Target information above from: UniProt accession P02768 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Images

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