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L7252

Sigma-Aldrich

Lactalbumin

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About This Item

Número CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61

fonte biológica

bovine

forma

powder

técnica(s)

cell culture | insect: suitable

nº de adesão UniProt

temperatura de armazenamento

2-8°C

Informações sobre genes

bovine ... LALBA(281894)

Descrição geral

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.

Aplicação

α-Lactalbumin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.
Lactalbumin has also been used in rearing anopheline mosquitoes.

Ações bioquímicas/fisiológicas

α-Lactalbumin 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 kDa), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four a-helices and a triple stranded antiparallel β-sheet.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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A Coscia et al.
Journal of biological regulators and homeostatic agents, 26(3 Suppl), 39-42 (2013-03-01)
Cow's milk proteins (CMPs) are among the best characterized food allergens. Cow's milk contains more than twenty five different proteins, but only whey proteins alpha-lactalbumin, beta-lactoglobulin, bovine serum albumin (BSA), and lactoferrin, as well as the four caseins, have been
Infection of mosquitoes with Plasmodium spp. in monkeys
Collins WE, et al.
Methods IN Malaria Research, 144-144 (2008)
Takashi Nakamura et al.
The Journal of biological chemistry, 288(20), 14408-14416 (2013-04-13)
Although HAMLET (human α-lactalbumin made lethal to tumor cells), a complex formed by human α-lactalbumin and oleic acid, has a unique apoptotic activity for the selective killing of tumor cells, the molecular mechanisms of expression of the HAMLET activity are
Y-B Zhang et al.
Cell death & disease, 4, e550-e550 (2013-03-23)
HAMLET is a complex of oleic acids and decalcified α-lactalbumin that was discovered to selectively kill tumor cells both in vitro and in vivo. Autophagy is an important cellular process involved in drug-induced cell death of glioma cells. We treated
C S James Ho et al.
PloS one, 7(12), e53051-e53051 (2013-01-10)
HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) is the first member in a new family of protein-lipid complexes with broad tumoricidal activity. Elucidating the molecular structure and the domains crucial for HAMLET formation is fundamental for understanding its tumoricidal

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