126658
Albumin, Human Serum, Fraction V, High Purity
Synonym(s):
Albumin, Human Serum, Fraction V, High Purity
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About This Item
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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
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
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L S Schlesinger et al.
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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
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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
Edward R Smith et al.
PloS one, 8(4), e60904-e60904 (2013-04-12)
The formation of fetuin-A-containing calciprotein particles (CPP) may facilitate the clearance of calcium phosphate nanocrystals from the extracellular fluid. These crystals may otherwise seed extra-osseous mineralization. Fetuin-A is a partially phosphorylated glycoprotein that plays a critical role in stabilizing these
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