L7269

α-Lactalbumin from human milk

≥95% (SDS-PAGE), lyophilized powder

• Número CAS: 9051-29-0
• UNSPSC Code: 12352202
• NACRES: NA.61
• MDL number: MFCD00130492
• Biological source: human milk
• Assay: ≥95% (SDS-PAGE)
• Form: lyophilized powder
• Technique(s): cell migration: suitable
• Concentration: >75 % protein (UV)

Propiedades

• biological source: human milk
• Quality Segment: 200
• assay: ≥95% (SDS-PAGE)
• form: lyophilized powder
• mol wt: 14,070 Da by calculation
• concentration: >75 % protein (UV)
• technique(s): cell migration: suitable
• solubility: H₂O: soluble 10 mg/mL(lit.)
• UniProt accession no.: P00709
• storage temp.: −20°C
• Gene Information: human ... LALBA(3906)

Descripción

General description

α-Lactalbumin (α-LA) is a small, acidic,[1] whey protein that constitutes about 22% of the total proteins in human milk. It is produced by the epithelial cells of the mammary gland. α-LA is made up of two domains, a large α-helical domain, and a small β-sheet domain.[1]

Application

α-Lactalbumin (α-LA) has been used as a standard

• to study the partitioning behavior of different monomeric proteins with exposure to amino acids on the protein surface[2]
• to study the interaction between α-LA and cathepsin D
• to study the ability of breast milk fractions to enhance the transepithelial flux of extrinsic iron in colon carcinoma cell line

Biochem/physiol Actions

α-Lactalbumin (α-LA) forms a complex with lactose synthase within the mammary gland and plays a role in milk production and regulates milk volume. It acts as an essential source for bioactive peptides and essential amino acids such as lysine, tryptophan, branched-chain amino acids, and sulfur-containing amino acids that play a role in an infant′s nutrition. In addition, α-LA has a wide range of applications including a supplement to foster gastrointestinal health and modulate sleep and depression. α-LA also shows therapeutic effects against sarcopenia, seizures, mood disorders, and cancer. It has a Ca²⁺ binding site that binds with Na⁺, K⁺, Mg²⁺, and Mn²⁺ and many Zn²⁺ binding sites.[1]

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. Complexes of α-lactalbumin with oleic acid show drastically different activities than α-lactalbumin alone, being strongly cytotoxic to tumor cells. The complex is referred to as HAMLET (human alpha-lactalbumin made lethal to tumor cells).

Información de seguridad

• Clase de almacenamiento: 11 - Combustible Solids
• wgk: WGK 3
• flash_point_f: Not applicable
• flash_point_c: Not applicable