Recombinant Bovine Alpha-lactalbumin(LALBA)

Code CSB-YP012724BO
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Source Yeast
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Code CSB-EP012724BO
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Source E.coli
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Code CSB-EP012724BO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP012724BO
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Source Baculovirus
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Code CSB-MP012724BO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names LALBA
Uniprot No. P00711
Alternative Names LALBA; ALACTA; Alpha-lactalbumin; Lactose synthase B protein; allergen Bos d 4
Species Bos taurus (Bovine)
Expression Region 20-142
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

(From Uniprot)
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.
Gene References into Functions
  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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Subcellular Location Secreted.
Protein Families Glycosyl hydrolase 22 family
Tissue Specificity Mammary gland specific. Secreted in milk.
Database Links

KEGG: bta:281894

STRING: 9913.ENSBTAP00000007701

UniGene: Bt.87412


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