Home>>Biochemical Assay Reagents>>Bovine Serum Albumin (BSA)

Bovine Serum Albumin (BSA) Sale

(Synonyms: 牛血清白蛋白) 目录号 : GC35542

牛血清白蛋白 (BSA) (BSA) 是一种含有 583 个残基的蛋白质,由三个同源的 all-&#945 组成;域,以心形结构组织。

Bovine Serum Albumin (BSA) Chemical Structure

Cas No.:9048-46-8

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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment:

Samples are prepared in 96-well microplates and all wells without samples are filled with 200 μL PBS to minimize evaporation. To each well is loaded 100 μL SH-SY5Y growth medium with or without 10.000 SH-SY5Y neuroblastoma cells. The assay is started by adding 25 μL buffer, with or without 5 mg/mL sonicated Bovine Serum Albumin previously incubated for 0, 2 or 96 h at 70°C (giving a final BSA concentration of 1 mg/mL). All sample combinations are loaded in triplets, and for each of the six Bovine Serum Albumin combinations a corresponding triplet is loaded without cells, to be used as blank. One triplet is also loaded without both cells and BSA and one only without Bovine Serum Albumin[1].

References:

[1]. Holm NK, et al. Aggregation and fibrillation of bovine serum albumin. Biochim Biophys Acta. 2007 Sep;1774(9):1128-38.

产品描述

Bovine Serum Albumin (BSA) is a 583-residue protein consisting of three homologous all-α domains, organized in a heart-shaped structure. BSA is a globular protein that is used in numerous biochemical applications.

Bovine serum albumin (BSA) is a 583-residue protein consisting of three homologous all-α domains, organized in a heart-shaped structure. Bovine serum albumin constitutes ca. 60% of all plasma protein and binds and transports a large number of physiological and non-physiological ligands. Bovine serum albumin contains 17 disulfide bonds and one unpaired cysteine (Cys34), which facilitates dimerization and also influences higher-order association, since the rate of aggregation is slowed down if Cys34 is covalently bound to another compound. MTT assay for fibril cytotoxicity shows Bovine Serum Albumin is beneficial for cell growth irrespective of its aggregated state. Lack of cytotoxicity is confirmed by membrane permeabilization assays. In the subsequent 40 h, an increase in the viability of the treated cells of 300-400% is observed, indicating that the cells incubated with Bovine Serum Albumin achieve a higher viability than the untreated cells[1].

References:
[1]. Holm NK, et al. Aggregation and fibrillation of bovine serum albumin. Biochim Biophys Acta. 2007 Sep;1774(9):1128-38.

Chemical Properties

Cas No. 9048-46-8 SDF
别名 牛血清白蛋白
Canonical SMILES S=B[*]
分子式 分子量 66.43kDa
溶解度 Water : 100 mg/mL 储存条件 Store at -20°C, protect from light
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储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
为了提高溶解度,请将管子加热至37℃,然后在超声波浴中震荡一段时间。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 15.0534 mL 75.2672 mL 150.5344 mL
5 mM 3.0107 mL 15.0534 mL 30.1069 mL
10 mM 1.5053 mL 7.5267 mL 15.0534 mL
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Research Update

Interaction among Bovine Serum Albumin (BSA) molecules in the presence of anions: a small-angle neutron scattering study

J Biol Phys 2022 Jun;48(2):237-251.PMID:PMC9054964DOI:10.1007/s10867-022-09608-w.

Protein-protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (pI ≈ 4.8), is studied in the presence of anions (Cl-, Br-, I-, F-, SO42-) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the pI of BSA, it nearly follows the series.

Recent developments in the detection of bovine serum albumin

Int J Biol Macromol 2019 Oct 1;138:602-617.PMID:31319084DOI:10.1016/j.ijbiomac.2019.07.096.

Albumin is a globular protein which plays a pivotal role in maintaining plasma pressure and the nutritional balance. Different compounds are transported by binding to albumin in the blood. Also, human health is closely related to the serum albumin concentration in blood plasma or other biological fluids. Due to the high structural similarity with human serum albumin (HSA), Bovine Serum Albumin (BSA) has been widely investigated as a model protein in different fields. Importantly, albumin detection has recently gained huge interest, as this protein serves as an important indicator of cow health, and its milk and meat quality. Also, it is also known as an allergenic and a carrier protein. As a result, it is highly essential to determine bovine albumin in various industries, such as medicine, pharmaceutical, clinical and food. Therefore, the development of new, efficient, fast and straightforward methods for selective detection of BSA is critical. This review seeks to highlight different characteristics of BSA and its importance. Then, by focusing on recent developments made in the last two decades in BSA biosensing and determination methods, the use of different biomaterials/nanomaterials is discussed.

Residual Bovine Serum Albumin (BSA) quantitation in vaccines using automated Capillary Western technology

Anal Biochem 2014 Sep 15;461:49-56.PMID:24841366DOI:10.1016/j.ab.2014.05.004.

Bovine Serum Albumin (BSA) is a major component of fetal bovine serum (FBS), which is commonly used as a culture medium during vaccine production. Because BSA can cause allergic reactions in humans the World Health Organization (WHO) has set a guidance of 50 ng or less residual BSA per vaccine dose. Vaccine manufacturers are expected to develop sensitive assays to detect residual BSA. Generally, sandwich enzyme-linked immunosorbent assays (ELISA) are used in the industry to detect these low levels of BSA. We report the development of a new improved method for residual BSA detection using the SimpleWestern technology to analyze residual BSA in an attenuated virus vaccine. The method is based on automated Capillary Western and has linearity of two logs, >80% spike recovery (accuracy), intermediate precision of CV <15%, and LOQ of 5.2 ng/ml. The final method was applied to analyze BSA in four lots of bulk vaccine products and was used to monitor BSA clearance during vaccine process purification.

Bovine Serum Albumin Catalysed Hydrogen and Deuterium Evolution at Mercury Electrodes

Chempluschem 2020 Jul;85(7):1596-1601.PMID:33210475DOI:10.1002/cplu.202000348.

The hydrogen evolution reaction (HER), catalysed by proteins at mercury electrodes and reflected in chronopotentiometric stripping peak H, provides a label-free and reagentless analytical technique that is sensitive to protein structure. Here we show how the kinetic isotope effect affected the HER catalysed by the protein Bovine Serum Albumin (BSA). We found that the deuteron bond, which is stronger than that of a proton, contributed to less effective transport of deuterons mediated by BSA at the Hg|D2 O interface, and enhanced structural stability of the surface-attached native BSA in D2 O solution. A structural transition was also observed in the surface-attached urea-denatured BSA, and is probably due to the destabilisation of some secondary structural remnants retained by the 17 SS-bonds. Because the catalytically active groups involved in proton or deuteron transfer in native proteins are often exposed towards solutions and their protons exchange almost instantly, no signs of H/D exchange were observed in native BSA using peak H under the given conditions.

Electroanalysis of Ibuprofen and Its Interaction with Bovine Serum Albumin

Molecules 2022 Dec 21;28(1):49.PMID:36615246DOI:10.3390/molecules28010049.

The current work presents a sensitive, selective, cost-effective, and environmentally benign protocol for the detection of ibuprofen (IBP) by an electrochemical probe made of a glassy carbon electrode modified with Ag-ZnO and MWCNTs. Under optimized conditions, the designed sensing platform was found to sense IBP up to a 28 nM limit of detection. The interaction of IBP with Bovine Serum Albumin (BSA) was investigated by differential pulse voltammetry. IBP-BSA binding parameters such as the binding constant and the stoichiometry of complexation were calculated. The results revealed that IBP and BSA form a single strong complex with a binding constant value of 8.7 × 1013. To the best of our knowledge, this is the first example that reports not only IBP detection but also its BSA complexation.