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L7269

Sigma-Aldrich

α-Lactalbumin from human milk

≥95% (SDS-PAGE), lyophilized powder

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

human milk

Quality Level

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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
Antonio Carroccio et al.
Clinical gastroenterology and hepatology : the official clinical practice journal of the American Gastroenterological Association, 8(3), 254-260 (2009-11-26)
A percentage of patients with symptoms of irritable bowel syndrome (IBS) suffer from food hypersensitivity (FH) and improve on a food-elimination diet. No assays have satisfactory levels of sensitivity for identifying patients with FH. We evaluated the efficacy of an
Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme.
K Brew et al.
The Journal of biological chemistry, 242(16), 3747-3749 (1967-08-25)
E A Permyakov et al.
FEBS letters, 473(3), 269-274 (2000-05-20)
Small milk protein alpha-lactalbumin (alpha-LA), a component of lactose synthase, is a simple model Ca(2+) binding protein, which does not belong to the EF-hand proteins, and a classical example of molten globule state. It has a strong Ca(2+) binding site

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