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LALBA encodes alpha-lactalbumin, a principal protein of milk. Additionally we are shipping LALBA Antibodies (118) and LALBA Kits (44) and many more products for this protein.
Showing 10 out of 31 products:
a folding variant of alpha-lactalbumin has a role in lactating mammary gland apoptosis
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.
High molecular mass complexes are formed with alpha-lactalbumin and alphaB-crystallin (show CRYAB Proteins), preventing the amorphous aggregation of alpha-lactalbumin.
analysis of macromolecular crowding on the structural stability of human alpha-lactalbumin
Data show that alpha-lactalbumin and CD14 (show NDUFA2 Proteins) form a complex in the gut (show GUSB Proteins) which alters degradation of CD14 (show NDUFA2 Proteins), suggesting a mechanism by which this key LPS (show IRF6 Proteins) receptor may remain functional in the neonatal gut (show GUSB Proteins).
The complexes formed by partially folded alpha-lactalbumin with oleic acid display selective apoptotic activity against tumor cells.
comparison of the structural and stability properties of the isolated alpha-helical domain of lysozyme (show LYZ Proteins) with that of alpha-lactalbumin
pH-dependent stability of the alpha-lactalbumin molten globule state.
Structural characterisation of the human alpha-lactalbumin molten globule at high temperature
a functional Ca(2 (show CA2 Proteins)+)-binding site is not required for conversion of alpha-lactalbumin to the active complex or to cause cell death
lipids are tissue-specific cofactors in alpha-lactalbumin protein folding
This study shows, for the first time, that alpha-lactalbumin isolated in a rare 28kDa dimeric form induces cell death, while 14kDa (show NDUFA6 Proteins) monomeric alpha-lactalbumin is inactive.
Macromolecular crowding reduces the calcium binding affinity of holo-lactalbumin alpha resulting in the formation of apo (show C9orf3 Proteins)-lactalbumin alpha (the calcium-depleted form of holo-LA) leading to aggregate formation.
Data suggest that stabilization of apo (show C9orf3 Proteins)-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.
Structural features of the alphaB-crystallin (show CRYAB Proteins) oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of alpha-lactalbumin at 37 degrees C and malate dehydrogenase (show MDH Proteins) when heated at 42 degrees C, were investigated.
the organization and dynamics of the functionally important tryptophan residues of BLA (show LACTB Proteins) in native, molten globule and denatured states utilizing the wavelength-selective fluorescence approach were explored.
Negatively charged alpha-lactalbumin (LA) interaction with basic histone stabilizes apo (show C9orf3 Proteins)-alpha-LA and destabilizes the Ca2 (show CA2 Proteins)+-bound protein due to compensation for excess negative charge of alpha-LA's Ca2 (show CA2 Proteins)+-binding loop by positively charged histone residues.
interaction of alphaB-cyrstallin with, and promoted unfolding of, reduced alpha-lactalbumin, but showed limited chaperone activity for other target proteins
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.
This gene encodes alpha-lactalbumin, a principal protein of milk. Alpha-lactalbumin forms the regulatory subunit of the lactose synthase (LS) heterodimer and beta 1,4-galactosyltransferase (beta4Gal-T1) forms the catalytic component. Together, these proteins enable LS to produce lactose by transfering galactose moieties to glucose. As a monomer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity. A folding variant of alpha-lactalbumin, called HAMLET, likely induces apoptosis in tumor and immature cells.
Lactose synthase B protein
, lactalbumin, alpha-
, lactose synthase B protein
, lysozyme-like protein 7
, alpha lactalbumin
, alpha-lactalbumin A
, alpha-lactalbumin B
, lactalbumin, alpha