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Sigma-Aldrich

Albumin, Human Serum, Fraction V, High Purity

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Synonym(s):
Albumin, Human Serum, Fraction V, High Purity
CAS Number:
MDL number:

Assay

≥95% (cellulose acetate electrophoresis)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

pI 

4.7

solubility

aqueous buffer: 5 mg/mL
water: 5 mg/mL

shipped in

ambient

storage temp.

−20°C

InChI

1S/C3F8/c4-1(5,2(6,7)8)3(9,10)11

InChI key

QYSGYZVSCZSLHT-UHFFFAOYSA-N

General description

Human serum albumin (HSA) is an unglycosylated, soluble, and globular monomeric protein. It is abundantly found in the plasma, with a multidomain comprising three homologous domains, called I, II, and III. Three of these domains have subdomains A and B with common structural motifs. The HSA gene is localized on the human chromosome 4q13.3.

Application

Albumin, human serum, fraction V, high purity has been used to determine the binding affinity of nanobody α human serum albumin (HSA) to HSA and injected to detect the signals of tandem binding of human interleukin (IL-21R), IL-21-αHSA, and HSA. It has also been used to study the effects of fetuin-A phosphorylation on calciprotein particles (CPP) uptake.

Biochem/physiol Actions

Human serum albumin (HSA) plays a major role as a carrier protein for fatty acids, thyroid hormones, and steroids. It is involved in stabilizing extracellular fluid volume. HSA is used to treat hemodialysis, acute liver failure, chronic liver disease. It serves as an excipient for vaccines and therapeutic protein drugs. HSA is implicated in biological applications, including ligand trapping, nano delivery of drugs, and fusion proteins.

Warning

Toxicity: Standard Handling (A)

Preparation Note

Prepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Alternatively, this product may be stored in the refrigerator (4°C) prior to reconstitution. Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Tanaya Chatterjee et al.
PloS one, 7(5), e37468-e37468 (2012-06-01)
Virstatin is a small molecule that inhibits Vibrio cholerae virulence regulation, the causative agent for cholera. Here we report the interaction of virstatin with human serum albumin (HSA) using various biophysical methods. The drug binding was monitored using different isomeric
G O Evans et al.
Laboratory animals, 20(1), 27-31 (1986-01-01)
Widely differing results were obtained for urinary protein determinations in male rats using 2 test strips and a quantitative Coomassie Blue sodium dodecyl sulphate method. A comparison of the sensitivity of the protein methods with respect to rat albumin and
Hongchuan Liu et al.
International immunopharmacology, 101(Pt A), 108307-108307 (2021-11-05)
Interleukin-21 (IL-21) has exhibited anti-tumor activity in preclinical and clinical studies; however, its modest efficacy and short half-time has limited its therapeutic utility as a monotherapy. Therefore, we engineered a fusion protein (IL-21-αHSA) in which a nanobody targeting human serum
L S Schlesinger et al.
The Journal of experimental medicine, 174(5), 1031-1038 (1991-11-01)
Previous studies from this laboratory have demonstrated that Mycobacterium leprae, an obligate intracellular bacterial parasite, enters human mononuclear phagocytes via complement receptors on these host cells and bacterium-bound C3. The present study investigates the role of M. leprae surface molecules
L S Schlesinger et al.
Infection and immunity, 62(1), 280-289 (1994-01-01)
We have previously determined that complement receptors on human mononuclear phagocytes and complement component C3 in nonimmune serum mediate phagocytosis of the intracellular bacterial pathogen Mycobacterium leprae, the agent of leprosy. We have also determined that C3 fixes selectively to

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