Recombinant Bovine Kappa-Casein (CSN3) Protein (His&Myc)

Name: Recombinant Bovine Kappa-Casein (CSN3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06570P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Bovine Kappa-Casein (CSN3) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02668
Target Symbol	CSN3
Species	Bos taurus (Bovine)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	QEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV
Expression Range	22-190aa
Protein Length	Full Length of Mature Protein
Mol. Weight	26.4 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.; Casoxins A, B and C have opioid antagonist activity. Casoxin C causes biphasic ileal contractions through the binding to the complement C3a receptors.; Casoplatelin inhibits platelet aggregation.
Subcellular Location	Secreted.
Protein Families	Kappa-casein family
Database References	KEGG: bta:281728 STRING: 9913.ENSBTAP00000028685 UniGene: PMID: 28850632 It was concluded that GH or IGF-I can independently promote the expression of CSN3 in bovine mammary epithelial cells in vitro. PMID: 26173981 Statistical analysis established that the CSN3 gene has no statistically significant influence on daily milk, fat and protein yield and SCC PMID: 22614274 Effects of beta-kappa-casein (CSN2-CSN3) haplotypes and BLG genotypes on yields were weak or trivial. PMID: 20655450 the propensity of the disulfide-linked multimers to form fibrils is inversely related to their size, with monomeric kappa-casein being the most aggregation prone PMID: 20441567 molecular dynamics simulation of bovine chymosin complexed with the P9-P70 residues of bovine kappa-casein PMID: 20155951 Phe-Leu-Pro-Tyr-Pro-Tyr (FLPYPY), corresponding to peptidic sequence 76-81 of bovine kappa-casein, exhibits neurite outgrowth-stimulating activity over 10(-9) M PMID: 15618646 The recombinant Caseinomacropeptide (hCMP)has been produced as a secretory product in yeast and was estimated to be 7.0kDa by SDS-PAGE, and showed a lower glycosylation than the natural bovine CMP. PMID: 15866733 Findings suggest that alphaS- and beta-casein are potent inhibitors of kappa-casein fibril formation and may prevent large-scale fibril formation in vivo. PMID: 16363816 kappa-casein gene (CSN3) promoter regions of cattle of different breeds revealed that 2 distinct haplotypes (A and B) exist at this locus with A allele dominant in all groups and B allele more representative of promoters from other ruminants PMID: 17699026 The effect of lactoferrin on beta-casein and kappa-casein mRNA expression in mammospheres while silencing of LTF increased casein mRNA expression. PMID: 18226297 In heterozygotes, beta-casein A and beta-lactoglobulin A were found at higher concentrations in milk compared with the variant encoded by the alternative allele whereas kappa-casein A and B variants were found at similar concentrations in AB heterozygotes PMID: 18363977 These findings suggest a model of aggregation during which the S-carboxymethylated kappa-casein monomer is in rapid equilibrium with a micellar aggregate that subsequently undergoes a conformational rearrangement into a more organized species. PMID: 18616951 The frequencies of the B allele of kappa-casein among breeds ranged from 0.01 to 0.30; the Sindhi breed had the highest frequency for the B allele (0.30), while the frequencies of this allele in other breeds ranged from 0.01 to 0.18. PMID: 18752189 Six single nucleotide polymorphisms were identified and haplotype inference revealed 12 haplotypes, of which 8 were newly discovered PMID: 18765626

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.