AlbumiNZ™ Low IgG BSA is chromatographically purified from New Zealand-sourced bovine plasma in an ISO quality system assuring complete traceability and consistent high quality. This albumin has very low endotoxin and low IgG to simplify downstream purification, is tested for the absence of viruses according to 9CFR and has the highest possible biosafety level. The albumin supports growth of stem cells and increases protein production from hybridoma cells.
Application Notes
AlbumiNZ™ Low IgG BSA supports growth of stem cells and increases protein production from hybridoma cells. Albumin is also used to solubilize lipids, and 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 such as electrophoresis. This grade finds applications in the manufacture of monoclonal antibodies.
Usage Statement
Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
Key Applications
Monoclonal antibody manufacture | Cell Culture | Binding and transport studies
| SKU | 02199897-CF |
| Alternate Names | BSA; Bovine albumin; Albumin from bovine serum; Bovine Plasma Albumin; Bovine Serum Albumin |
| Application Notes | AlbumiNZ™ Low IgG BSA supports growth of stem cells and increases protein production from hybridoma cells. Albumin is also used to solubilize lipids, and 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 such as electrophoresis. This grade finds applications in the manufacture of monoclonal antibodies. |
| Background_information | Albumins are a group of acidic proteins which occur in the body fluids and tissues of mammals and in some plant seeds. Serum and plasma albumin is carbohydrate-free and comprises 55-62% of the protein present. However, only about 40% of the total albumin in the body is in the circulating plasma at one time with the remainder being in extracellular spaces with which there is, in general, equilibration about every 24 hours. Bovine albumin is a single polypeptide chain consisting of approximately 583 to 595 amino acid residues and no carbohydrates. At pH 5-7, it contains 17 intrachain disulfide bridges and 1 sulfhydryl group. E.J. Cohn and associates developed one of the first commercial precipitation procedures using an alcohol precipitation. 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. Albumin binds water, Ca<sup>2+</sup>, Na<sup>+</sup> and K<sup>+</sup>. 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 and to a lesser degree to provide cellular nutrition. Human and bovine albumins contain 16% nitrogen. |
| Base Catalog Number | 199897 |
| Biochemical Physiological Actions | Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies. |
| CAS # | 9048-46-8 |
| Concentration | Total Protein: ≥95% |
| EC Number | 232-936-2 |
| Format | Lyophilized powder |
| Grade | Cell Culture Grade, ImmunoAssay (EIA) Grade |
| Host | Bovine |
| Molecular Weight | 66KDa |
| Personal Protective Equipment | Eyeshields, Gloves, Respirator filter |
| pH | 6.5 - 7.5 (4% aq soln) |
| Preparation Method | Prepared by salt fractionation, ion exchange, and gel filtration chromatography. |
| Protein or Enzyme Type | Albumin |
| Purity | ≥97% Total Protein |
| 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 albumin is very good (especially if the solutions are stored aliquoted and frozen). 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. |
| Usage Statement | Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department. |
![MP COA [199897] lot ID: 2156](https://www.mpbio.com/static/version1715349838/frontend/Mpbio/default/en_US/images/document.png "MP COA [199897] lot ID: 2156")
