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L7269

Sigma-Aldrich

α-Lactalbumin from human milk

≥95% (SDS-PAGE), lyophilized powder

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About This Item

Numer CAS:
Numer MDL:
Kod UNSPSC:
12352202
NACRES:
NA.61

pochodzenie biologiczne

human milk

Poziom jakości

Próba

≥95% (SDS-PAGE)

Formularz

lyophilized powder

masa cząsteczkowa

14,070 Da by calculation

stężenie

>75 % protein (UV)

metody

cell migration: suitable

rozpuszczalność

H2O: soluble 10 mg/mL(lit.)

numer dostępu UniProt

temp. przechowywania

−20°C

informacje o genach

human ... LALBA(3906)

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Opis ogólny

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.

Zastosowanie

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

Działania biochem./fizjol.

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.
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).
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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