Bovine α Lactalbumin,α-La ELISA Kit

Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.

1. This study shows, for the first time, that alpha-lactalbumin isolated in a rare 28kDa dimeric form induces cell death, while 14kDa monomeric alpha-lactalbumin is inactive. PMID: 28193539
2. Macromolecular crowding reduces the calcium binding affinity of holo-lactalbumin alpha resulting in the formation of apo-lactalbumin alpha (the calcium-depleted form of holo-LA) leading to aggregate formation. PMID: 25437004
3. Data suggest that stabilization of apo-alpha-lactalbumin by mono- and oligo-saccharides can be accounted for by simplified statistical-thermodynamic model considering volume exclusion deriving from steric repulsion between protein and saccharides. PMID: 26000826
4. These findings suggest that the SNP alpha-LA2516 in the alpha-LA gene likely does not have potential as a molecular marker for milk production traits in Chinese Holstein cows. PMID: 24065678
5. alphaLA forms a misfolded disulfide bond shuffled isomer, X-alphaLA which represents a different low energy fold for the protein; binding calcium plays an important role in both maintaining the native structure of alphaLA and providing a mechanism for distinguishing between folded and misfolded species. PMID: 22189830
6. Structural features of the alphaB-crystallin oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of alpha-lactalbumin at 37 degrees C and malate dehydrogenase when heated at 42 degrees C, were investigated. PMID: 21152271
7. the organization and dynamics of the functionally important tryptophan residues of BLA in native, molten globule and denatured states utilizing the wavelength-selective fluorescence approach were explored. PMID: 20346348
8. The complexes formed by partially folded alpha-lactalbumin with oleic acid display selective apoptotic activity against tumor cells. PMID: 19968717
9. a functional Ca(2+)-binding site is not required for conversion of alpha-lactalbumin to the active complex or to cause cell death PMID: 14627739
10. Negatively charged alpha-lactalbumin (LA) interaction with basic histone stabilizes apo-alpha-LA and destabilizes the Ca2+-bound protein due to compensation for excess negative charge of alpha-LA's Ca2+-binding loop by positively charged histone residues. PMID: 15134431
11. interaction of alphaB-cyrstallin with, and promoted unfolding of, reduced alpha-lactalbumin, but showed limited chaperone activity for other target proteins PMID: 15670152
12. Data indicate that deletion of the beta-subdomain in alpha-lactalbumin does not alter the ability of the protein to assemble into well-ordered fibrils, implying that this chain region is not essential for the amyloid formation. PMID: 15853802
13. Fold and topology of alpha-lactalbumin may be formed from degenerate groups of side chains. PMID: 15956205
14. residual long-range interactions may act as nucleation sites for protein folding, while this property of residual structure is replaced by the calcium-binding site between the domains in alpha-lactalbumin. PMID: 16731974
15. characterized the acid induced molten globule state (A-state) of alpha-LA both qualitatively and quantitatively. PMID: 16741984
16. Results describe the reaction mechanism and formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of the dye 2,2'-dipyridyl with non-native states of bovine and human alpha-lactalbumins in aqueous solution. PMID: 16851644
17. interaction between calcium-depleted alpha-lactalbumin and lysozyme leads to the formation of different supramolecular structures depending on the temperature PMID: 17260954
18. stopped-flow CD, fluorescence, and time-resolved NMR studies that the Ca(2+)-induced refolding of bovine alpha-lactalbumin (BLA) at constant denaturant concentration (4 M urea) exhibits triple-exponential kinetics. PMID: 18377934
19. Allelic frequencies and RFLP patterns of alpha-lactalbumin gene vary between two species of cattle. PMID: 18607792
20. Disulfide bond shuffling in bovine alpha-lactalbumin: MD simulation confirms experiment PMID: 18942855
21. Serotonin suppressed alpha-lactalbumin mRNA expression in lactogen-treated primary bovine mammary epithelial cell cultures. PMID: 19654143

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Secreted.

Glycosyl hydrolase 22 family

Mammary gland specific. Secreted in milk.

KEGG: bta:281894

STRING: 9913.ENSBTAP00000007701

UniGene: Bt.87412