L7252
Lactalbumin
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About This Item
Biological source:
bovine
Form:
powder
Technique(s):
cell culture | insect: suitable
biological source
bovine
form
powder
technique(s)
cell culture | insect: suitable
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
bovine ... LALBA(281894)
Application
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.
Biochem/physiol Actions
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.
General description
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
Yoshiko Moriyama et al.
Langmuir : the ACS journal of surfaces and colloids, 28(47), 16268-16273 (2012-11-01)
The thermal stability of two homologous proteins, lysozyme and α-lactalbumin, was examined by circular dichroism. The present study clearly showed two different aspects between the homologous proteins: (1) the original helices of lysozyme and α-lactalbumin were unchanged at heat treatments
Jinbing Xie et al.
Advanced healthcare materials, 2(6), 795-799 (2013-01-09)
Upon controlled UV illumination, disulfide bonds in bovine α-lactalbumin (BLA) are selectively broken, leading to self-assembly of the BLA and doxorubicin (DOX) molecules into nanoparticles via hydrophobic interactions and intermolecular disulfide bonds. Such protein-drug nanoparticles have synergistic anticancer activity in
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)
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