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  • 产品名称：HumanSerumAlbumin(HSA)(AA25-609)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
HumanSerumAlbumin(HSA)(AA25-609)(Active)protein(Histag)
详情介绍：
Characteristics 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.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
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.
Molecular Weight 67.3 kDa
NCBI Accession NP_000468
UniProt P02768
Restrictions For Research Use only
Format Lyophilized
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.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Human Serum Albumin (HSA) (AA 25-609) (Active) protein (His tag) (ABIN2181228) Human HSA, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained over...
Background publications Minchiotti, Campagnoli, Rossi, Cosulich, Monti, Pucci, Kragh-Hansen, Granel, Disdier, Weiller, Galliano: "A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges." in: European journal of biochemistry / FEBS, Vol. 268, Issue 2, pp. 344-52, 2001 (PubMed).

Minchiotti, Galliano, Stoppini, Ferri, Crespeau, Rochu, Porta: "Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions." in: Biochimica et biophysica acta, Vol. 1119, Issue 3, pp. 232-8, 1992 (PubMed).

Carter, He, Munson, Twigg, Gernert, Broom, Miller: "Three-dimensional structure of human serum albumin." in: Science (New York, N.Y.), Vol. 244, Issue 4909, pp. 1195-8, 1989 (PubMed).