alpha-Lactalbumin from bovine milk, Type I, >=85% (PAGE), lyophilized powder
Application
?-Lactalbumin from bovine milk has been used as a supplement of basal medium for various cell cultures. It has also been used as a marker for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Biochem/physiol Actions
?-Lactalbumin is the cheif protein in human milk. It consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. ?-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native ?-lactalbumin from the reduced, denatured form. ?-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. The mature protein consists of 123 amino acid residues (14 kD), and it has a three-dimensional structure with 1.7 ?° resolution, demonstrating four ?-helices and a triple stranded antiparallel ?-sheet.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase. Site-directed mutagenesis of Asp87 or Asp88 to Ala completely abolishes the strong calcium binding affinity and reduces the stimulation of lactose synthase to ﹤3.5% of the maximal rate.
General description
?-Lactalbumin is a small, globular, whey protein that has been found in all milk studied to date. It is a metalloprotein of approximately 14 kDa produced in the mammary glands.
Packaging
25, 100, 500 mg in poly bottle
1 g in poly bottle
Quality
Calcium saturated. May have traces of ammonium sulfate and sodium phosphate
| Quality Level | 200 |
|---|---|
| Manufacturer | SIGMA-ALDRICH |
| Technique(s) | electrophoresis: suitable, cell culture - mammalian: suitable |
| Storage Temp. | −20°C |
| Solubility | H2O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow |
| Form | lyophilized powder |
| Assay | ≥85% (PAGE) |
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