LALBA Monoclonal Antibody

1. Studies indicate that alpha-lactalbumin has two domains, a large alpha-helical domain and a small beta-sheet domain connected by a calcium binding loop. PMID: 27238572
2. High molecular mass complexes are formed with alpha-lactalbumin and alphaB-crystallin, preventing the amorphous aggregation of alpha-lactalbumin. PMID: 23005341
3. analysis of macromolecular crowding on the structural stability of human alpha-lactalbumin PMID: 22735492
4. Data show that alpha-lactalbumin and CD14 form a complex in the gut which alters degradation of CD14, suggesting a mechanism by which this key LPS receptor may remain functional in the neonatal gut. PMID: 20717070
5. The complexes formed by partially folded alpha-lactalbumin with oleic acid display selective apoptotic activity against tumor cells. PMID: 19968717
6. comparison of the structural and stability properties of the isolated alpha-helical domain of lysozyme with that of alpha-lactalbumin PMID: 11718563
7. pH-dependent stability of the alpha-lactalbumin molten globule state. PMID: 12833543
8. Structural characterisation of the human alpha-lactalbumin molten globule at high temperature PMID: 12860137
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. lipids are tissue-specific cofactors in alpha-lactalbumin protein folding PMID: 14627740
11. NMR study of the conformation of HAMLET, the folding variant of human alpha-lactalbumin, complexed to oleic acid. PMID: 15075403
12. The electrostatic nature of the alpha-lactalbumin (LA)-histone interaction justifies use of alpha-LA as a basis for design of antitumor agents, acting through disorganization of chromatin structure due to interaction between alpha-LA and histone. PMID: 15134431
13. a folding variant of alpha-lactalbumin has a role in lactating mammary gland apoptosis PMID: 15141307
14. the non-cooperative denaturation of the molten globule, alpha-lactalbumin secondary structure elements are stabilized by non-specific, non-native interactions PMID: 15558602
15. Fold and topology of alpha-lactalbumin may be formed from degenerate groups of side chains. PMID: 15956205
16. Local interactions as well as hydrophobic interactions formed in the molten globule state play an important role in organizing the structure in the transition state and in guiding the subsequent folding of alpha-lactalbumin. PMID: 16121399
17. 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
18. alpha-lactalbumin molten globule has even more native-like character than suggested by studies conducted at higher temperature PMID: 18939797
19. recombinant human alpha-LA was purified from transgenic milk and displayed physicochemical properties similar to its natural counterpart with respect to molecular weight, structure, and regulatory activity for beta-1,4-galactosyltransferase PMID: 19038921
20. the structural preferences of the alpha-LA molten globule at pH 7 at the level of individual residues were investigated. PMID: 19766656
21. hydrogen exchange behavior of variants using mass spectrometry PMID: 11518539

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HGNC: 6480

OMIM: 149750

KEGG: hsa:3906

STRING: 9606.ENSP00000301046

UniGene: Hs.72938