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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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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
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
Petter Storm et al.
PloS one, 8(3), e58578-e58578 (2013-03-19)
Ion channels and ion fluxes control many aspects of tissue homeostasis. During oncogenic transformation, critical ion channel functions may be perturbed but conserved tumor specific ion fluxes remain to be defined. Here we used the tumoricidal protein-lipid complex HAMLET as
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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