L7269
α-Lactalbumin from human milk
≥95% (SDS-PAGE), lyophilized powder
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About This Item
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biological source
human milk
assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
14,070 Da by calculation
solubility
H2O: soluble 10 mg/mL(lit.)
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... LALBA(3906)
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General description
α-Lactalbumin (α-LA) is a small, acidic, 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.
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
- 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.
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).
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Los clientes también vieron
Breast Milk Fractions Solubilize Fe(III) and Enhance Iron Flux across Caco-2 Cells
Robert E. S.
The Journal of Nutrition, 449?455-449?455 (2003)
HAMLET effect on cell death and mitochondrial respiration in colorectal cancer cell lines with KRAS/BRAF mutations.
??ilinskas, et al.
Journal of Cancer Research and Clinical Oncology (2023)
The surface exposed amino acid residues of monomeric proteins determine the partitioning in aqueous two-phase systems
Kristina B, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 253-268 (2002)
Applications for ?-lactalbumin in human nutrition
Donald K L, et al.
Nutrition Research Reviews, 76(6), 444?460-444?460 (2018)
Junai Gan et al.
Molecular nutrition & food research, 63(18), e1900259-e1900259 (2019-07-05)
The use of human milk products is increasing for high-risk infants. Human milk contains endogenous enzymes that comprise a dynamic proteolytic system, yet biological properties of these enzymes and their activities in response to variations including pH within infants are
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