Albumin from Bovine Serum
What is BSA and what is the molecular weight of BSA?
Albumins bind, sequester and stabilize a range of important molecules and proteins. Bovine serum albumin (BSA) is a small (~66 kDa) globular albumin protein that has been utilized in many well-cited applications. Our BSA products have been used and published in peer-reviewed articles for many applications, including cell culture, IHC, ELISA and many more. We offer a wide variety of BSA products for your research and manufacturing needs
Bovine serum albumin by purification method and application
The table below shows common applications and peer-reviewed articles that use our most popular BSA products. The list is not intended to be comprehensive and product numbers not listed may be suitable and specifically tested for various uses. Select the BSA best suited for your needs by reviewing what other researchers just like you are using.
Purification Methods and Application References for Bovine Serum Albumin | ||
---|---|---|
Product | Purification Method | Application References |
A2153 | Cold-Ethanol Fractionation | Cell/Tissue Culture: 50,51,52 ELISA Blocking: 74 IHC/ICC/IF: 109, 110 Immunoblotting: 124, 125 Standard/Calibrator: 145 |
A3156 | Cold-Ethanol Fractionation | Cell/Tissue Culture: T |
A4378 | Cold-Ethanol Fractionation | IHC/ICC/IF: 97 |
A4503 | Cold-Ethanol Fractionation | Cell/Tissue Culture: 26,27,28 ELISA Blocking: 65 IHC/ICC/IF: 98 Immunoblotting: 132, 133, 134 |
A6003 | Cold-Ethanol Fractionation | Cell/Tissue Culture: 46, 47 Standard/Calibrator: 139, 140 Stabilization/Diluent: 10, 155 |
A8806 | Cold-Ethanol Fractionation | Binding, Transport, & Carrier: 4, 5, 6, 7 Cell/Tissue Culture: 48 IHC/ICC/IF: 107 Stabilization/Diluent: 156 |
A9418 | Cold-Ethanol Fractionation | Cell/Tissue Culture: T |
A0281 | Heat-Shock Fractionation | Cell/Tissue Culture: 43, 44, 45 |
A1470 | Heat-Shock Fractionation | Binding, Transport, & Carrier: 1 Cell/Tissue Culture: 1, 16, 17, 18 Immunoblotting: 115 |
A1595 | Heat-Shock Fractionation | Cell/Tissue Culture: 53, 54, 55 |
A2058 | Heat-Shock Fractionation | Immunoblotting: 123 Standard/Calibrator: 141, 142, 143 |
A3059 | Heat-Shock Fractionation | Cell/Tissue Culture: 30, 56 Immunoblotting: 118, 119 Standard/Calibrator: 137 Stabilization/Diluent: 56, 152 |
A3294 | Heat-Shock Fractionation | ChIP/ Sequencing/ Hybridization: 62 IHC/ICC/IF: 108 Standard/Calibrator: 144 |
A3311 | Heat-Shock Fractionation | Cell/Tissue Culture: T |
A3803 | Heat-Shock Fractionation | Binding, Transport, & Carrier: 2, 3 Cell/Tissue Culture: 36 ELISA Blocking: 68 IHC/ICC/IF: 99 Standard/Calibrator: 138 |
A3858 | Heat-Shock Fractionation | ELISA Blocking: 5 |
A3912 | Heat-Shock Fractionation | Cell/Tissue Culture: 37 IHC/ICC/IF: 100 Immunoblotting: 120 |
A4161 | Heat-Shock Fractionation | Cell/Tissue Culture: 23, 24, 25 |
A4612 | Heat-Shock Fractionation | Cell/Tissue Culture: 49 |
A4919 | Heat-Shock Fractionation | Cell/Tissue Culture: 13, 14 IHC/ICC/IF: 84 |
A7030 | Heat-Shock Fractionation | Cell/Tissue Culture: 39, 40, 41, 42 ELISA Blocking: 69, 70, 71, 72, 73 IHC/ICC/IF: 106 Immunoblotting: 122 Stabilization/Diluent: 154 |
A7888 | Heat-Shock Fractionation | Cell/Tissue Culture: 31, 32, 33, 34 ELISA Blocking: 67 |
A7906 | Heat-Shock Fractionation | Cell/Tissue Culture: 29 ChIP/ Sequencing/ Hybridization: 58, 59, 60 ELISA Blocking: 66 Immunoblotting: 116, 117 Standard/Calibrator: 135, 136 Stabilization/Diluent: 149, 150, 151 |
A7979 | Heat-Shock Fractionation | Cell/Tissue Culture: T |
A8022 | Heat-Shock Fractionation | ELISA Blocking: 63 IHC/ICC/IF: 88, 89, 90, 91, 92 Immunoblotting: 92, 112, 113, 114 Stabilization/Diluent: 147 |
A8412 | Heat-Shock Fractionation | Cell/Tissue Culture: T |
A8577 | Heat-Shock Fractionation | Stabilization/Diluent: 153 |
A9085 | Heat-Shock Fractionation | Cell/Tissue Culture: 15 IHC/ICC/IF: 85, 86, 87 Immunoblotting: 86, 87, 126 |
A9430 | Heat-Shock Fractionation | Cell/Tissue Culture: 19 |
A9543 | Heat-Shock Fractionation | Cell/Tissue Culture: 35 |
A9576 | Heat-Shock Fractionation | Cell/Tissue Culture: T |
A9647 | Heat-Shock Fractionation | IHC/ICC/IF: 76, 77, 78, 79, 80, 81, 82, 83 Immunoblotting: 111 Standard/Calibrator: 127, 128, 129, 130, 131 Stabilization/Diluent: 146 |
B2064 | Heat-Shock Fractionation | Cell/Tissue Culture: 38 IHC/ICC/IF: 101, 102, 103, 104 Immunoblotting: 103 |
B2518 | Heat-Shock Fractionation | IHC/ICC/IF: 105 Immunoblotting: 121 |
B4287 | Heat-Shock Fractionation | Cell/Tissue Culture: 20, 21, 22 T ELISA Blocking: 64 IHC/ICC/IF: 93, 94, 95, 96 Stabilization/Diluent: 148 |
B6917 | Heat-Shock Fractionation | ChIP/ Sequencing/ Hybridization: 57 |
BSA Structure
BSA is a single polypeptide chain consisting of about 583 amino acid residues and no carbohydrates. At pH 5-7 it contains 17 intrachain disulfide bridges and 1 sulfhydryl group.
What does bovine serum albumin do?
Albumins are a group of acidic proteins which occur plentifully in the body fluids and tissues of mammals and in some plant seeds. Unlike globulins, albumins have comparatively low molecular weights, are soluble in water, are easily crystallized, and contain an excess of acidic amino acids. Serum and plasma albumin are carbohydrate-free and comprises 55-62% of the protein present.
Albumin binds water, Ca2+, Na+, and K+. Due to a hydrophobic cleft, albumin binds fatty acids, bilirubin, hormones, and drugs. The main biological function of albumin is to regulate the colloidal osmotic pressure of blood. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. Albumin is used to solubilize lipids and is also used as a blocking agent in western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present (e.g., electrophoresis).
Bovine serum albumin physical properties
pI in Water at 25 °C: | Fatty Acid Depleted - 5.3, Endogenous Material - 4.7; 4.9 |
pH of 1% Solution: | 5.2-7 |
Optical Rotation: | [α] 259 : -61°; [α] 264 : -63° |
Stokes Radius (r s ): | 3.48 nm |
Sedimentation constant, S 20,W X 10 13 | 4.5 (monomer), 6.7 (dimer) |
Diffusion constant, D 20,W X 10 7 | 5.9 |
Partial specific volume, V 20 | 0.733 |
Intrinsic viscosity, η | 0.0413 |
Frictional ratio, f/f 0 | 1.30 |
Overall dimensions, Å | 40 X 140 |
Refractive index increment1 (578 nm) X 10 -3 | 1.90 |
Optical absorbance, A279 nm (1 gram/liter) | 0.667 |
Mean residue rotation1 [ m' ] 233 | 8443 |
Mean residue ellipticity | 21.1 [θ] 209 nm ; 20.1 [θ] 222 nm |
Estimated α-helix, % | 54 |
Estimated β-form % | 18 |
Bovine serum albumin solubility
Albumins are readily soluble in water and can only be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of BSA is very good (especially if the solutions are stored as frozen aliquots). In fact, albumins are frequently used as stabilizers for other solubilized proteins (e.g., labile enzymes). However, albumin is readily coagulated by heat. When heated to 50 °C or above, albumin quite rapidly forms hydrophobic aggregates which do not revert to monomers upon cooling. At somewhat lower temperatures aggregation is also expected to occur, but at relatively slower rates.
How is bovine serum albumin made?
Albumin is relatively simple to isolate and purify. One of the first methods of isolation involved extensive dialysis of serum against water and removed most globulins. A second procedure took advantage of the good solubility of albumin at low to moderate ammonium sulfate concentrations, and effected precipitation by lowering the pH. Electrophoretic isolation was also employed, as was affinity chromatography. However, none of these methods were applicable to large scale production.
Initial isolation is accomplished by heat treatment or by alcohol precipitation. Most commercial preparations are now prepared by alcohol precipitation, a method developed by E. J. Cohn and his associates in the 1940's ("Fraction V" yields albumin with a purity of about 96%), or by Heat Treatment. The additional removal of impurities can be accomplished by crystallization, preparative electrophoresis, ion exchange chromatography, affinity chromatography (e.g., ConA-agarose removes glycoproteins), heat treatment (removes globulins), low pH treatment, charcoal treatment, organic solvent precipitation (i.e., isooctane), and low temperature treatment. Charcoal treatment and organic solvent precipitation remove fatty acids.
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