Bovine Serum Albumin (BSA)
(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-α 组成；域，以心形结构组织。
Cas No.:9048-46-8
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
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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]. |
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References: [1]. Holm NK, et al. Aggregation and fibrillation of bovine serum albumin. Biochim Biophys Acta. 2007 Sep;1774(9):1128-38. |
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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.
| 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 |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 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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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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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 |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
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.