Journal: Nature Communications

Article Title: Phosphorylation of PA28γ by CK2 kinase facilitates HNSCC tumor formation and progression

doi: 10.1038/s41467-025-67131-7

Figure Lengend Snippet: a WCLs derived from HSC-3 cells were immunoprecipitated with control IgG, anti-PA28γ, or anti-CK2β antibody, followed by IB analysis of co-IP products and WCLs. b Immunofluorescence analyses of the cellular localization of endogenous PA28γ and CK2β in HNSCC cells. DAPI (blue), nucleus; Scale bars, 10 μm. c Schematic representation of the evolutionarily conserved PA28γ-T23 site in different species. Residues around the T23 site have a common characteristic of CK2 kinase substrates, namely the predominance of acidic amino acid residues (E/D) between n-4 and n + 7. α1–4 denotes helix-α1–4. d IB analysis of IP products and WCLs derived from HEK293T cells transfected with the indicated plasmids. e In vitro kinase assays were performed with recombinant His-PA28γ WT and T23A proteins purified from E. coli system as substrates and purified CK2 proteins containing CK2α and CK2β as the source of kinase. IB analysis of the indicated proteins in vitro kinase assay samples. f, g IB analysis of WCLs derived from HEK293T cells transfected with the subunits of CK2 ( f ) and HNSCC cells treated with 100ngml –1 EGF before harvesting ( g ). h, i HNSCC cells silenced with siRNA negative control (siNC) or siCK2 ( h ) and HSC-3 cells silenced with siNC or CK2α/α‘/β siRNA ( i ) were stimulated without or with 100ngml –1 EGF for 30 min before harvesting for IB analysis. j HEK293T cells transfected with the indicated plasmids were treated with 100ngml –1 EGF. WCLs were immunoprecipitated with the indicated antibodies, followed by IB analysis of co-IP products and WCLs. k In vitro kinase assays were performed with recombinant His-PA28γ proteins purified from E. coli system as substrates and purified CK2 proteins containing CK2α and CK2β as the source of kinase. 2 μM or 20 μM CK2 inhibitor TBB was added as indicated. l IB analysis of IP products and WCLs derived from HEK293T cells transfected with the indicated plasmids and silenced with siNC or #1, #2 NIP30 siRNA. m IB analysis of WCLs derived from HEK293T cells transfected with the indicated plasmids and silenced with siNC or #1, #2 NIP30 siRNA. Source data are provided as a Source Data file.

Article Snippet: Anti-His (IB, 1:10000; IP, 1:300; 66005-1-Ig), anti-GST (IB, 1:10000; 66001-2-Ig), anti-NIP30 (IB, 1:1000; 16830-1-AP), anti-SRC3 (IB, 1:3000; 29587-1-AP), anti-SirT1 (IB, 1:3000; 13161-1-AP), anti-pan-keratin (pan-K) (IHC, 1:3000; 26411-1-AP), anti-Ki67 (IHC, 1:5000; 27309-1-AP) and anti-CK2β (IHC, 1:200; 20234-1-AP) antibodies were purchased from Proteintech.

Techniques: Derivative Assay, Immunoprecipitation, Control, Co-Immunoprecipitation Assay, Immunofluorescence, Transfection, In Vitro, Recombinant, Purification, Kinase Assay, Negative Control

Journal: Cancer & Metabolism

Article Title: Phosphoproteomics revealed cellular signals immediately responding to disruption of cancer amino acid homeostasis induced by inhibition of l -type amino acid transporter 1

doi: 10.1186/s40170-022-00295-8

Figure Lengend Snippet: Changes in the phosphorylation of substrates of suggested key kinases and their regulatory proteins by LAT1 inhibition. Protein extracted from cells treated with 30 μM JPH203 and control cells was analyzed by Western blot. (A and B) The decrease in phosphorylation associated with JPH203 treatment for indicated time: Thr-389 of p70 S6K ( A ) and Ser-1469 of TOP2A ( B ). The data are presented as a ratio of the signal intensity of phosphorylated protein to total protein ± SD ( n = 3). * p value < 0.05. ns = not significant (one sample t test) ( C ) Decreased phosphorylation of part of CK2 substrates by LAT1 inhibition with JPH203 for 24 h. Phosphorylation on the consensus CK2 substrate motif was detected by a specific antibody. D Decreased phosphorylation of Ser-209 of CK2β, a regulatory subunit of CK2, in cells treated with JPH203 for 24 h. E CK2 activity of BTC cells treated with JPH203. The extracted protein of BTC cells treated with 30 μM JPH203 for 24 h was subject to CK2 activity assay by ELISA using p53 N-terminal peptide and p53-pS46 antibody conjugated with horseradish peroxidase. F The decrease of CK2α co-immunoprecipitated with NOLC1. Protein extracted from KKU-055 and KKU-213 cells treated with JPH203 for 24 h was subject to immunoprecipitation using anti-NOLC1 antibody

Article Snippet: In Western blotting, the following antibodies were used at the indicated dilutions: p70 S6K–pT389 (1:1000, #9234), p70 S6K (1:1000, #9202), phospho–CK2 substrate (1:1000, #8738) from Cell Signaling Technology (Danvers, MA, USA); CK2β (1:500, 22418-1-AP), NOLC1 (1:1000, 11815-1-AP), and β-actin (1:5000, 66009-1-Ig) from Proteintech Group (Chicago, IL, USA); TOP2A-pS1469 (1:1000, PA5-64536) from Affinity Biosciences (Cincinnati, OH, USA); CK2β–pS209 (1:1000, 44-1090G) from Invitrogen (Waltham, MA, USA); TOP2A (1:200, sc-365916), CK2α (1:1000, sc-373894) from Santa Cruz Biotechnology (Dallas, TX, USA); goat anti-mouse IgG-HRP (1:5000, 115-035-062), goat anti-rabbit IgG-HRP (1:5000, 111-035-003) from Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

Techniques: Phospho-proteomics, Inhibition, Control, Western Blot, Activity Assay, Enzyme-linked Immunosorbent Assay, Immunoprecipitation

Journal: Cancer & Metabolism

Article Title: Phosphoproteomics revealed cellular signals immediately responding to disruption of cancer amino acid homeostasis induced by inhibition of l -type amino acid transporter 1

doi: 10.1186/s40170-022-00295-8

Figure Lengend Snippet: Evaluation of the combined treatment of JPH203 and CX-4945. A Effect of the combination of JPH203 with CX-4945 on cell proliferation. BTC cell lines were treated with JPH203 or CX-4945 alone, or in combination. After 3 days of treatment, cell growth was assessed by WST assay. The absorbance at 450 nm of each sample was expressed as % of the control without JPH203 treatment. B Wound healing assay using KKU-100 treated with 30 μM JPH203 or 5μM CX-4945 alone, or in combination. C The number of migrating cells of KKU-055 and KKU-100 treated with 30 μM JPH203 or 5 μM CX-4945 alone, or in combination. The significance of the difference between the treatment with each inhibitor alone and the combination was determined by one-way ANOVA followed by Tukey’s multiple comparison test. Data represent means ± SD ( n = 4 for WST assay, n = 3 for wound healing assay). *Tukey post-hoc p value < 0.05. D Decreased phosphorylation of part of CK2 substrates by LAT1 inhibition with 30 μM JPH203 and 1 μM CX-4945, or in combination for 24 h. Phosphorylation on the consensus CK2 substrate motif was detected by a specific antibody

Article Snippet: In Western blotting, the following antibodies were used at the indicated dilutions: p70 S6K–pT389 (1:1000, #9234), p70 S6K (1:1000, #9202), phospho–CK2 substrate (1:1000, #8738) from Cell Signaling Technology (Danvers, MA, USA); CK2β (1:500, 22418-1-AP), NOLC1 (1:1000, 11815-1-AP), and β-actin (1:5000, 66009-1-Ig) from Proteintech Group (Chicago, IL, USA); TOP2A-pS1469 (1:1000, PA5-64536) from Affinity Biosciences (Cincinnati, OH, USA); CK2β–pS209 (1:1000, 44-1090G) from Invitrogen (Waltham, MA, USA); TOP2A (1:200, sc-365916), CK2α (1:1000, sc-373894) from Santa Cruz Biotechnology (Dallas, TX, USA); goat anti-mouse IgG-HRP (1:5000, 115-035-062), goat anti-rabbit IgG-HRP (1:5000, 111-035-003) from Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

Techniques: WST Assay, Control, Wound Healing Assay, Comparison, Phospho-proteomics, Inhibition

Journal: Advanced Science

Article Title: Proline‐Selective Electrochemiluminescence Detecting a Single Amino Acid Variation Between A1 and A2 β‐Casein Containing Milks

doi: 10.1002/advs.202411956

Figure Lengend Snippet: a) Milk can contain either or both variants of β‐casein. The Pro‐to‐His substitution for the A1 variant facilitates proteolysis and formation of a β‐casomorphin‐7 (BCM‐7) bioactive peptide. b) Putative electrochemiluminescence (ECL) mechanisms that show the electrical and optical signals are linked although the linkage across these two modalities is amino‐acid‐dependent. c) Device used to simultaneously measure electrical and optical signals.

Article Snippet: To measure the amount of A1‐ and A2‐ β‐casein, a bovine A1 β‐casein and a A2 β‐casein sandwich ELISA assays (Biosensis, Australia) were used.

Techniques: Variant Assay, Electrochemiluminescence

Journal: Advanced Science

Article Title: Proline‐Selective Electrochemiluminescence Detecting a Single Amino Acid Variation Between A1 and A2 β‐Casein Containing Milks

doi: 10.1002/advs.202411956

Figure Lengend Snippet: Proline has a unique ECL response compared to other amino acids. a) Time series plots of input ( E ) and outputs (electrical, Q = ∫ i d t ; and optical, ECL ) for 5‐cycle cyclic voltammogram (CV). Lys and His have different response‐patterns and quantitative features ( Q Tot (Total Charge) and AUC Tot (Total Area Under Curve)). b) Phase plane analysis shows: Lys has a small electrical response (comparable to the Ru(bpy) 3 2+ control); His has a strong electrical (i.e., oxidative) response; and Pro has an intermediate electrical response but a very strong optical response (ECL). c) Our relative ECL responses for 15 amino acids compares with previous measurements [ ^22a ] using Spearman's correlation coefficients (r). A gray overlay indicates 95% confidence band for the best‐fit linear regression line (dotted line). d) Cluster analysis shows that Pro forms its own group (silhouette coefficient = 0.57). e) Electrical and optical responses vary linearly with amino acid concentration in an amino acid‐dependent manner. f) Cross‐modal analysis for His and Pro that differ between A1 and A2 β ‐casein variants (the dotted lines represent the fitted linear regression lines). All data are shown as the mean or the mean with the error bar presenting ± standard deviation (N = 4).

Article Snippet: To measure the amount of A1‐ and A2‐ β‐casein, a bovine A1 β‐casein and a A2 β‐casein sandwich ELISA assays (Biosensis, Australia) were used.

Techniques: Control, Concentration Assay, Standard Deviation

Journal: Advanced Science

Article Title: Proline‐Selective Electrochemiluminescence Detecting a Single Amino Acid Variation Between A1 and A2 β‐Casein Containing Milks

doi: 10.1002/advs.202411956

Figure Lengend Snippet: ELISA test kits and ECL can distinguish the protein standards for the A1 and A2 β‐casein variants. a) Schematic of ELISA and ECL measurements. b) As expected, ELISA kit designed to detect the A1‐variant shows low response to the A2‐variant. c) As expected, ELISA kit designed to detect the A2‐variant shows low response to the A1‐variant. All ELISA data are shown as the mean with the error bar representing ± standard deviation (N = 4). d) Time series input‐output plots and phase plane plots for the A1‐ and A2‐β‐casein standards. e) The electrical response metric ( Q Tot ) cannot distinguish the A1‐ and A2‐β‐caseins. f) The optical response metric ( AUC Tot ) can distinguish the A1‐ and A2‐β‐caseins. All ECL data are shown as the mean with the error bar representing ± standard deviation (N = 3). All p values in bar graphs were calculated with the Kruskal–Wallis test and the statistical significance is defined as: * = p < 0.05, ns (not siginificant) = p > 0.05.

Article Snippet: To measure the amount of A1‐ and A2‐ β‐casein, a bovine A1 β‐casein and a A2 β‐casein sandwich ELISA assays (Biosensis, Australia) were used.

Techniques: Enzyme-linked Immunosorbent Assay, Variant Assay, Standard Deviation

Journal: Advanced Science

Article Title: Proline‐Selective Electrochemiluminescence Detecting a Single Amino Acid Variation Between A1 and A2 β‐Casein Containing Milks

doi: 10.1002/advs.202411956

Figure Lengend Snippet: Validation of the ECL method by comparison with immunoanalysis. a) Immunoassays with A1‐specific and A2‐specific ELISAs show that the A2 milk has only the A2 β‐casein variant while regular milk has a mixture of A1 and A2 variants. Each bar is shown as the mean with the error presenting standard deviation (N = 3 for each milk). b) The correlations between the ELISA and ECL method indicate that the optical metric ( AUC Tot ) and cross‐modal metric ( AUC Tot / Q Tot ) distinguish regular and A2 milks based on their levels of their β‐casein variants (the electrical metric, Q Tot , by itself cannot discriminate regular and A2 milks). Spearman's correlation coefficients (r) are indicated. All gray overlays indicate 95% confidence bands for the best‐fit linear regression line (dotted line).

Article Snippet: To measure the amount of A1‐ and A2‐ β‐casein, a bovine A1 β‐casein and a A2 β‐casein sandwich ELISA assays (Biosensis, Australia) were used.

Techniques: Biomarker Discovery, Comparison, Variant Assay, Standard Deviation, Enzyme-linked Immunosorbent Assay

Journal: Advanced Science

Article Title: Proline‐Selective Electrochemiluminescence Detecting a Single Amino Acid Variation Between A1 and A2 β‐Casein Containing Milks

doi: 10.1002/advs.202411956

Figure Lengend Snippet: Comparison of the ECL method with conventional methods. a) The selectivity of the ECL is compared to gold standard immunoassays: data and Cluster analysis show that both the ELISA and ECL methods can distinguish A2 from regular milks (Silhouette coefficient = 0.87 (immunoassay); 0.6 (ECL)). b) The generic nature of the ECL method is illustrated by the cross‐modal metric ( AUC Tot / Q Tot ): this metric decreases as the analysis becomes more challenging (from distinguishing amino acids, to distinguishing proline‐rich peptides and proteins, and samples in complex backgrounds) yet the ECL method can discern the A2 and regular milks. p values were calculated with the Kruskal–Wallis test.

Article Snippet: To measure the amount of A1‐ and A2‐ β‐casein, a bovine A1 β‐casein and a A2 β‐casein sandwich ELISA assays (Biosensis, Australia) were used.

Techniques: Comparison, Enzyme-linked Immunosorbent Assay

Journal: Journal of Animal Science

Article Title: Klebsiella pneumoniae causes mammary gland damage via FNIP1-mediated mitochondrial dysfunction

doi: 10.1093/jas/skaf384

Figure Lengend Snippet: K. pneumoniae inhibited milk fat and protein synthesis in BMECs. (A–C) mRNA levels of TNF-α , IL-1β , and IL-6 were detected by RT-qPCR method in BMECs (mean ± SEM, n = 3). (D) DEGs heat maps. (E) Enrichment analysis of differentially expressed genes KEGG. (F) The protein levels of SREBP1 and β-casein were detected in BMECs. (G, H) Relative protein abundance of SREBP1 and β-casein were normalized to β-actin (mean ± SEM, n = 3). (I, J) mRNA levels of SREBP1 and β-casein were detected by RT-qPCR method in BMECs (mean ± SEM, n = 3). (K) Typical images of BODIPY 493/503 staining in BMECs. * P < 0.05; ** P < 0.01.

Article Snippet: The following primary antibodies were used: SREBP1 (14088-1-AP, Proteintech, Hubei, China), β-casein (HY-P81091, MCE, Shanghai, China), OPA1 (DF8587, Affinity, Jiangsu, China), MFN1 (13798-1-AP, Proteintech, Hubei, China), cytochrome c oxidase I (COX I) (DF8920, Affinity, Jiangsu, China), DRP1 (12957-1-AP, Proteintech, Hubei, China), FIS1 (10956-1-AP, Proteintech, Hubei, China), FNIP1 (28380-1-AP, Proteintech, Hubei, China), β-actin (AF7018, Affinity, Jiangsu, China).

Techniques: Quantitative RT-PCR, Quantitative Proteomics, Staining

Journal: Journal of Animal Science

Article Title: Klebsiella pneumoniae causes mammary gland damage via FNIP1-mediated mitochondrial dysfunction

doi: 10.1093/jas/skaf384

Figure Lengend Snippet: K. pneumoniae caused mitochondrial dysfunction in mammary gland and dyssynthesis of milk fat and protein. (A) Representative images of H&E staining. (B) The severity of mastitis was assessed by differences in histological score ( n = 6 cows per group) between the control and K. pneumoniae infection groups. (C–G) mRNA levels of TNF-α , IL-1β , IL-6, SREBP1 , and β-casein were detected by RT-qPCR method in mammary gland tissues (mean ± SEM, n = 6). (H) The protein levels of SREBP1, β-casein OPA1, MFN1, COX I, DRP1, and FIS1 were detected in mammary gland tissues. (I–O) Relative protein abundance of OPA1, MFN1, COX I, DRP1, FIS1, SREBP1, and β-casein were normalized to β-actin (mean ± SEM, n = 3). (P) Relative ATP levels (mean ± SEM, n = 6). * P < 0.05; ** P < 0.01.

Article Snippet: The following primary antibodies were used: SREBP1 (14088-1-AP, Proteintech, Hubei, China), β-casein (HY-P81091, MCE, Shanghai, China), OPA1 (DF8587, Affinity, Jiangsu, China), MFN1 (13798-1-AP, Proteintech, Hubei, China), cytochrome c oxidase I (COX I) (DF8920, Affinity, Jiangsu, China), DRP1 (12957-1-AP, Proteintech, Hubei, China), FIS1 (10956-1-AP, Proteintech, Hubei, China), FNIP1 (28380-1-AP, Proteintech, Hubei, China), β-actin (AF7018, Affinity, Jiangsu, China).

Techniques: Staining, Control, Infection, Quantitative RT-PCR, Quantitative Proteomics

Journal: Journal of Animal Science

Article Title: Klebsiella pneumoniae causes mammary gland damage via FNIP1-mediated mitochondrial dysfunction

doi: 10.1093/jas/skaf384

Figure Lengend Snippet: Mdivi-1 recovered K. pneumoniae -induced mitochondrial damage and dyssynthesis of milk fat and protein in BMECs. (A) BMECs were treated with K. pneumoniae and/or 10 μM Mdivi-1 to analyze the protein levels of OPA1, MFN1, COX I, DRP1, and FIS1. (B–F) Relative protein abundance of OPA1, MFN1, COX I, DRP1, and FIS1 were normalized to β-actin (mean ± SEM, n = 3). (G) Relative ATP levels (mean ± SEM, n = 3). (H) BMECs were treated with K. pneumoniae and/or 10 μM Mdivi-1 to analyze the protein levels of SREBP1 and β-casein. (I, J) Relative protein abundance of SREBP1 and β-casein were normalized to β-actin (mean ± SEM, n = 3). (K, L) BMECs were treated with K. pneumoniae and/or 10 μM Mdivi-1 to analyze mRNA levels of SREBP1 and β-casein (mean ± SEM, n = 3). (M) Typical images of BODIPY 493/503 staining in BMECs. (N–P) BMECs were treated with K. pneumoniae and/or 10 μM Mdivi-1 to analyze mRNA levels of TNF-α , IL-1β , and IL-6 (mean ± SEM, n = 3). (Q) Detection of the content of LDH (mean ± SEM, n = 3). * P < 0.05; ** P < 0.01.

Article Snippet: The following primary antibodies were used: SREBP1 (14088-1-AP, Proteintech, Hubei, China), β-casein (HY-P81091, MCE, Shanghai, China), OPA1 (DF8587, Affinity, Jiangsu, China), MFN1 (13798-1-AP, Proteintech, Hubei, China), cytochrome c oxidase I (COX I) (DF8920, Affinity, Jiangsu, China), DRP1 (12957-1-AP, Proteintech, Hubei, China), FIS1 (10956-1-AP, Proteintech, Hubei, China), FNIP1 (28380-1-AP, Proteintech, Hubei, China), β-actin (AF7018, Affinity, Jiangsu, China).

Techniques: Quantitative Proteomics, Staining

Journal: Journal of Animal Science

Article Title: Klebsiella pneumoniae causes mammary gland damage via FNIP1-mediated mitochondrial dysfunction

doi: 10.1093/jas/skaf384

Figure Lengend Snippet: FNIP1 silencing alleviated K. pneumoniae -induced milk fat and protein dyssynthesis. (A) After FNIP1 silence, BMECs were infected with K. pneumoniae for 6 h to analyze the protein levels of SREBP1 and β-casein. (B, C) Relative protein abundance of SREBP1 and β-casein were normalized to β-actin (mean ± SEM, n = 3). (D, E) After FNIP1 silence, mRNA levels of SREBP1 and β-casein were detected by RT-qPCR method in BMECs (mean ± SEM, n = 3). (F) Typical images of BODIPY 493/503 staining in BMECs. (G–I) After FNIP1 silence, mRNA levels of TNF-α , IL-1β , and IL-6 were detected by RT-qPCR method in BMECs (mean ± SEM, n = 3). * P < 0.05; ** P < 0.01.

Article Snippet: The following primary antibodies were used: SREBP1 (14088-1-AP, Proteintech, Hubei, China), β-casein (HY-P81091, MCE, Shanghai, China), OPA1 (DF8587, Affinity, Jiangsu, China), MFN1 (13798-1-AP, Proteintech, Hubei, China), cytochrome c oxidase I (COX I) (DF8920, Affinity, Jiangsu, China), DRP1 (12957-1-AP, Proteintech, Hubei, China), FIS1 (10956-1-AP, Proteintech, Hubei, China), FNIP1 (28380-1-AP, Proteintech, Hubei, China), β-actin (AF7018, Affinity, Jiangsu, China).

Techniques: Infection, Quantitative Proteomics, Quantitative RT-PCR, Staining

Journal: Molecular cell

Article Title: Multiplexed kinase interactome profiling quantifies cellular network activity and plasticity

doi: 10.1016/j.molcel.2023.01.015

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: The mixture was then subjected to the same digestion protocol and downstream handling as described above “Kinase affinity enrichment, KI competition, and on-bead digestion”. . Co-immunoprecipitation/MS (Co-IP/MS) analyses of AAK1 and CK2 PPI networks 200 μl of the corresponding cell lysate in modified RIPA buffer V1 (5 mg/mL protein) containing protease and phosphatase inhibitors (see ‘ Kinase affinity enrichment , KI competition and on-bead digestion’) were incubated with antibodies against AAK1, RALBP1, or REPS1 (FOCUS cell lysate, see ‘ Immunoblot analysis and antibodies ’), CK2α or CK2β (U2-OS cell lysate, Novus Biologicals, CK2α Ab: polyclonal, # NB100–378, CK2β Ab: polyclonal, #NBP1–06515) or GFP (control, clone D5.1, CST, Cat # 2956) at the manufacturer’s recommended concentrations, respectively, and agitated overnight on a tube rotator at 4°C.

Techniques: Virus, Recombinant, Mass Spectrometry, Protease Inhibitor, Western Blot, cDNA Synthesis, shRNA, Plasmid Preparation, Software, Phospho-proteomics, Real-time Polymerase Chain Reaction

Journal: International Journal of Molecular Sciences

Article Title: β-Casein A1 and A2 Genetic Variants and β-Casomorphin-7 in Raw Milk and Processed Milk Products

doi: 10.3390/ijms26178612

Figure Lengend Snippet: Proposed mechanism of β-casomorphin-7 (BCM-7) release from β-casein A1 variant during gastrointestinal digestion. Variant A2 does not generate BCM-7.

Article Snippet: After a brief homogenization, raw milk or dairy products were tested for the presence of A1 and A2 beta-casein variants using the Bovine A1 (or A2) Beta-Casein ELISA Kit (Biosensis Pty Ltd., Thebarton, Australia).

Techniques: Variant Assay

Journal: International Journal of Molecular Sciences

Article Title: β-Casein A1 and A2 Genetic Variants and β-Casomorphin-7 in Raw Milk and Processed Milk Products

doi: 10.3390/ijms26178612

Figure Lengend Snippet: Workflow of experiments leading to measure the content of β-casein variants A1 and A2 as well as BCM-7 in the raw milk and popular processed dairy products. By A–G letters, 7 dairy plants are abbreviated.

Article Snippet: After a brief homogenization, raw milk or dairy products were tested for the presence of A1 and A2 beta-casein variants using the Bovine A1 (or A2) Beta-Casein ELISA Kit (Biosensis Pty Ltd., Thebarton, Australia).

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: β-Casein A1 and A2 Genetic Variants and β-Casomorphin-7 in Raw Milk and Processed Milk Products

doi: 10.3390/ijms26178612

Figure Lengend Snippet: Relative content of β-casein A1 and A2 variants in raw milk and processed dairy products (pasteurized milk, UHT milk, and milk powder). Bars represent mean ± SD. Different superscript letters indicate significant differences ( p < 0.01) among product types. Note: in UHT milk, difference between the content of A1 and A2 variants did not reach statistical significance ( p > 0.05) due to high variability among samples. Different capital letters A and B indicate statistical significance between means at level p < 0.01.

Article Snippet: After a brief homogenization, raw milk or dairy products were tested for the presence of A1 and A2 beta-casein variants using the Bovine A1 (or A2) Beta-Casein ELISA Kit (Biosensis Pty Ltd., Thebarton, Australia).

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: β-Casein A1 and A2 Genetic Variants and β-Casomorphin-7 in Raw Milk and Processed Milk Products

doi: 10.3390/ijms26178612

Figure Lengend Snippet: Mean values and standard deviation (± SD) of β-casein variant A1 (left) and variant A2 (right) contents in raw milk obtained from cows with identified CSN2 genotype. Statistically significant differences ( p < 0.01) are indicated with different superscript letters. Different capital letters A and B indicate statistical significance between means at level p < 0.01.

Article Snippet: After a brief homogenization, raw milk or dairy products were tested for the presence of A1 and A2 beta-casein variants using the Bovine A1 (or A2) Beta-Casein ELISA Kit (Biosensis Pty Ltd., Thebarton, Australia).

Techniques: Standard Deviation, Variant Assay