STAT3 plays an important role in vascular remodeling, but there are no studies on its protein function and structure. In this study, the physical and chemical properties, hydrophilicity / hydrophobicity, transmembrane domain, phosphorylation site, glycosylation site, subcellular localization, signal peptide distribution and secondary and tertiary structure of STAT3 protein were predicted online by bioinformatics tools. The results showed that the number of amino acids of STAT3 was 771aa, the theoretical isoelectric point was 5.94, the instability index was 49.21, and the average coefficient of hydrophilicity was-0.389. It was found to be a hydrophilic protein with no transmembrane domain, 45 phosphorylation sites and 4 glycosylation sites. The protein is expressed in the nucleus, there is no signal peptide distribution in the whole sequence, and the protein structure is complex. The secondary structure is mainly composed of α-helix, Extended strand, β-turn and Random coil, accounting for 50.58%, 11.80%, 2.46% and 35.15%, respectively. The tertiary structure is mainly composed of α-helix and Random coil. In summary, this study suggests that the amino acid sequence 75-190aa of STAT3 can be used to express antigens and prepare antibodies, and the sequence 737-754aa of STAT3 can be used to prepare peptide antigens This study provides a basis for further exploring the function of STAT3 protein, and lays a foundation for expression and purification of STAT3 protein, preparation of STAT3 antibody and screening of drug targets. This then provides powerful conditions for pathological detection of pulmonary vascular remodeling and gene drug therapy of ascites syndrome in broilers.
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Author Name: Li Q, Wu P, Wu X, Zou Z, Li G, Latigo V, Lin Li, Guo X, Hu G and Liu P
URL: View PDF
Keywords: STAT3 gene, broiler, ascites syndrome, bioinformatics analysis
ISSN: 2708-7182
EISSN: 2708-7190
EOI/DOI: https://doi.org/10.47278/journ
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