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biological source
bovine
Quality Level
form
powder
technique(s)
cell culture | insect: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LALBA(281894)
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.
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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
Infection of mosquitoes with Plasmodium spp. in monkeys
Collins WE, et al.
Methods IN Malaria Research, 144-144 (2008)
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
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