AlbumiNZ™ Low Endo BSA
Product Description
Bovine albumin is a single polypeptide chain consisting of approximately 583 to 595 amino acid residues and no carbohydrates. It contains 17 intrachain disulfide bridges and 1 sulfhydryl group
Application Notes
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 and to a lesser degree to provide cellular nutrition. Bovine albumin contains 16% nitrogen and is often used as a standard in protein calibration studies. Albumin is used to solubilize lipids, stabilize protein solutions, and is also used as a blocking agent in Western blots or ELISA applications.
Usage Statement
Research Use Only (RUO). Ready for CE IVD labeling of clinical applications.
Key Applications
Stem cell research || Cell Culture applications || Immunoassay
| SKU | 02199896-CF |
| Application Notes | 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 and to a lesser degree to provide cellular nutrition. Bovine albumin contains 16% nitrogen and is often used as a standard in protein calibration studies. Albumin is used to solubilize lipids, stabilize protein solutions, and is also used as a blocking agent in Western blots or ELISA applications. |
| Biochemical Physiological Actions | Albumin loses its helical structure rapidly in 2-4 M urea and 4 M guanidinium chloride. The unfolding is reversible, even, to some extent, after concomitant reduction of all disulfide bonds . Reduced albumin can reform into structures capable of binding antibodies and other ligands . Formation of SS bonds is rapid but the return of native structure is slow and some wrong disulfide pairings may persist . After oxidation of the cystine bridges, however, native structure is irreversibly lost. |
| Concentration | Total Protein: ≥95% |
| EC Number | 232-936-2 |
| Foreign Activity | Mycoplasma, Virus not detected |
| Grade | Low Endotoxin Grade |
| Applications | Stem cell research || Cell Culture applications || Immunoassay |
| Moisture Content | ≤5% |
| Molecular Weight | 66KDa |
| Pack Size | No |
| pH | 6.5 - 7.5 (4% aq soln) |
| Physical Appearance | Off-white to Light Yellowish to Brown Powder |
| Presentation | Off-white to Light Yellowish to Brown Powder |
| Product Families Description | 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. |
| Purity | ≥97% Total Protein |
| Research Areas | Embryonic Stem Cells||Hematopoietic Stem Cells||Neural Stem Cells||Pluripotent Stem Cells |
| 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. Dissolves completely in 20 min at 20-25 °C (20%). |
| Storage and Handling | Store at +4 °C. |
| Usage Statement | Research Use Only (RUO). Ready for CE IVD labeling of clinical applications. |