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expression is induced by pseudophosphorylated prolactin in mammary gland [RGD, Feb 2006].. Additionally we are shipping CSN2 Antibodies (63) and CSN2 Kits (28) and many more products for this protein.
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Human CSN2 Protein expressed in Escherichia coli (E. coli) - ABIN668028
Greenberg, Groves, Dower: Human beta-casein. Amino acid sequence and identification of phosphorylation sites. in The Journal of biological chemistry 1984
Show all 2 references for ABIN668028
Exogenous 5-HT (show DDC Proteins) decreased beta-casein expression in MCF-12A human mammary epithelial cells and was responsible for inhibiting phosphorylation of STAT5 (show STAT5A Proteins), resulting in a decline in lactational function.
The acidic fragment of human Abeta (show APP Proteins) (Abeta1-11) and a phosphorylated fragment of beta-Casein induced tau fibrillization in vitro.
New functions of lactoferrin (show LTF Proteins) and beta-casein in mammalian milk as cysteine protease (show CTSB Proteins) inhibitors. They might play a role in antiseptic and antiinfectious functions due to cysteine protease (show CTSB Proteins) inhibition of bacteria and viruses.
The RCM (show Unc5c Proteins)-kappa does form concentration-dependent micelles. Also, beta-CN phosphorylation level influences micelle formation. Complexes were low-temperature reversible and RCM (show Unc5c Proteins)-kappa fibrils were seen.
a negative cross talk between PR and Stat5a (show STAT5A Proteins)/GR may contribute to the physiological role of progesterone to repress lactogenic hormone induction of the beta-casein gene
Data suggest that the resulting knock-in cells and blastocysts could be used for the production of transgenic cattle that express human fibroblast growth factor 2 (show FGF2 Proteins) (hFGF2) within the bovine beta-casein gene locus.
Translation attenuation via 3' terminal codon usage in bovine mRNA is responsible for the difference in alpha-S2- and beta-casein profile in milk.
This suggests a superiority of allele A2 (0.7072) which does not produce BCM (show TNFRSF17 Proteins)-7, and thus is safe for human consumption. The expected homozygosity for gene CSN2 is in the population stated a slight increase in homozygosity
chaperone-like activity of bovine beta-casein (beta-CN) against thermal denaturation and aggregation processes of bovine carbonic anhydrase
The obtained results lead to the following conclusion: the highest amount of beta-casomorphin-7 released from the hydrolyzed and processed milk is related to the beta-casein A1 allele, irrespective of a lactation period.
These results demonstrate the enhanced chaperone activity of modified beta-casein and its protective effects on lysozyme (show LYZ Proteins) refolding.
Effects of beta-kappa-casein (show CSN3 Proteins) (CSN2-CSN3 (show CSN3 Proteins)) haplotypes and BLG genotypes on yields were weak or trivial.
New functions of lactoferrin (show LTF Proteins) and beta-casein in mammalian milk as cysteine protease (show CTSW Proteins) inhibitors. They might play a role in antiseptic and antiinfectious functions due to cysteine protease (show CTSW Proteins) inhibition of bacteria and viruses.
bovine beta-casein heat and alkaline denaturation analysis
Data show that the tail peptide beta-casein-(f193-209) is important in maintaining the hydrophobic core of beta-casein.
octamer-binding transcription factor-1 (show POU2F1 Proteins) may serve as a master regulator that facilitates the DNA binding of both signal transducer and activator of transcription 5 (show STAT5A Proteins) and glucocorticoid receptor (show NR3C1 Proteins) in hormone-induced beta-casein expression
It was found that both IGF-1 (show IGF1 Proteins) and IGF-2 activate the expression of milk protein beta-casein in the presence of prolactin (show PRL Proteins) and hydrocortisone. It was found that beta-casein expression is accompanied by cyclin D1 (show CCND1 Proteins) coexpression.
mammary cells express beta-casein in response to prolactin (show PRL Proteins) in a pathway that involves gap junction intracellular communication and OCT-1 (show POU2F1 Proteins) and is independent of STAT5 (show STAT5A Proteins) nuclear translocation
Progesterone receptor (show PGR Proteins) directly inhibits beta-casein gene transcription in mammary epithelial cells through promoting promoter and enhancer repressive chromatin modifications
Our data thus suggest that the degradation of beta-casein occurs via the microautophagic pathway.
In vitro expression of recombinant basement membrane-mediated beta-casein gene can be controlled pharmacologically by histone deacetylase (show HDAC1 Proteins) inhibitors or by overexpression of a histone acetylase enzyme.
Elevated levels of beta-casein gene expression were found in transgenic mice with stat5 (show STAT5A Proteins) during late pregnancy and lactation.
the first intron of the murine beta-casein gene contains a functional promoter, and beta-casein has intronic enhancer elements
Liver-enriched inhibitory protein plays critical role in mediating TNF (show TNF Proteins)-induced down-regulation of the beta-casein gene.
The ubiquitous Oct-1 (show POU2F1 Proteins) transcription factor may be involved in hormonally regulated, tissue-specific beta-casein gene expression.
CSN2 polymorphisms are potential markers for milk production in goats.
the nucleotide C at position 1311 negatively affects the promoter activity of the CSN2 gene; the SNP g.1311T>C associated with the absence of beta-casein in milk
findings demonstrate that the proximal -300 bp of CSN2 promoter containing the STAT5a (show STAT5A Proteins) binding site (-102 to -82) is the response element for lactogenic hormone stimulation; also intron 1 may be required for tissue or developmental stage-specific expression in mammary gland
Data show that the presence of beta-casein (CSN2) transcripts was detected in all samples, including cells originating from non-lactating goat.
Results describe the primary structure of a low-molecular weight multiphosphorylated variant of beta-casein in equine milk.
The effects of prolactin receptor (show PRLR Proteins) and beta-casein genotype on the nutritive value of sow milk are reported.
The authors describe five novel missense single nucleotide polymorphisms in the CSN2 and CSN3 (show CSN3 Proteins) genes that have large differences in allele frequencies among commercial pig breeds.
Transcription of porcine CSN2 is regulated by lactogenic signals via the STAT5 (show STAT5A Proteins) site (-102bp to -84bp) and intron 1.
expression is induced by pseudophosphorylated prolactin in mammary gland
, beta casein B
, milk protein
, beta casein
, pre-beta-casein (AA -15 to 213)