L5385

α-Lactalbumin from bovine milk

Type I, ≥85% (PAGE), lyophilized powder

• Sinónimos: Bos d 4, Lactose synthase B protein, alpha-lactalbumin
• Número CAS: 9051-29-0
• UNSPSC Code: 12352202
• NACRES: NA.61
• MDL number: MFCD00162025
• Biological source: bovine milk
• Assay: ≥85% (PAGE)
• Form: lyophilized powder
• Technique(s): cell culture | mammalian: suitable, electrophoresis: suitable
• Impurities: calcium, tested
• Concentration: ≥85 % protein

Propiedades

• biological source: bovine milk
• Quality Segment: 300
• type: Type I
• assay: ≥85% (PAGE)
• form: lyophilized powder
• concentration: ≥85 % protein
• technique(s): cell culture | mammalian: suitable, electrophoresis: suitable
• impurities: calcium, tested
• solubility: H₂O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow
• UniProt accession no.: P00711
• storage temp.: −20°C
• Gene Information: cow ... LALBA(281894)

Descripción

General description

α-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.

Application

α-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

α-Lactalbumin is the cheif protein in human milk. It consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. α-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native α-lactalbumin from the reduced, denatured form. α-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 Α° resolution, demonstrating four α-helices and a triple stranded antiparallel β-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.

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.

Analysis Note

Calcium saturated. May have traces of ammonium sulfate and sodium phosphate

Información de seguridad

• Clase de almacenamiento: 11 - Combustible Solids
• wgk: WGK 3
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, type N95 (US)