Anti-GFPT1 (Aa 525-681) Polyclonal Antibody (DPABH-12096) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

Total Page：16

File Type：pdf, Size：1020Kb

Anti-GFPT1 (aa 525-681) polyclonal antibody (DPABH-12096) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Immunogen Recombinant fragment corresponding to Human GFPT1 aa 525-681 (C terminal). (BC045641).Sequence: DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGE LKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKED TETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNL AKSVTV Isotype IgG Source/Host Rabbit Species Reactivity Human Purification Immunogen affinity purified Conjugate Unconjugated Applications WB, IHC-P Format Liquid Size 100 μg Buffer pH: 7.20; Constituents: 99% PBS, 1% BSA Preservative 0.02% Sodium Azide Storage Shipped at 4°C. Store at 4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. GENE INFORMATION Gene Name GFPT1 glutamine--fructose-6-phosphate transaminase 1 [ Homo sapiens ] Official Symbol GFPT1 Synonyms GFPT1; glutamine--fructose-6-phosphate transaminase 1; GFPT, glutamine fructose 6 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved phosphate transaminase 1; glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1; GFA; GFAT; GFAT1; hexosephosphate aminotransferase 1; D-fructose-6-phosphate amidotransferase 1; glutamine:fructose 6 phosphate amidotransferase 1; GFPT; GFAT 1; GFAT1m; Entrez Gene ID 2673 Protein Refseq NP_001231639 UniProt ID Q06210 Chromosome Location 2p13 Pathway Activation of Chaperone Genes by XBP1(S); Activation of Chaperones by IRE1alpha; Alanine, aspartate and glutamate metabolism; Amino sugar and nucleotide sugar metabolism; Asparagine N-linked glycosylation; Function glutamine-fructose-6-phosphate transaminase (isomerizing) activity; sugar binding; transferase activity; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.

Copy Link

Recommended publications

Causes and Evaluation of Mildly Elevated Liver Transaminase Levels ROBERT C
Causes and Evaluation of Mildly Elevated Liver Transaminase Levels ROBERT C. OH, LTC, MC, USA, and THOMAS R. HUSTEAD, LTC, MC, USA Tripler Army Medical Center Family Medicine Residency Program, Honolulu, Hawaii Mild elevations in levels of the liver enzymes alanine transaminase and aspartate transaminase are commonly dis- covered in asymptomatic patients in primary care. Evidence to guide the diagnostic workup is limited. If the history and physical examination do not suggest a cause, a stepwise evaluation should be initiated based on the prevalence of diseases that cause mild elevations in transaminase levels. The most common cause is nonalcoholic fatty liver disease, which can affect up to 30 percent of the population. Other common causes include alcoholic liver disease, medication- associated liver injury, viral hepatitis (hepatitis B and C), and hemochromatosis. Less common causes include α1-antitrypsin deficiency, autoimmune hepatitis, and Wilson disease. Extrahepatic conditions (e.g., thyroid disorders, celiac disease, hemolysis, muscle disorders) can also cause elevated liver transaminase levels. Initial testing should include a fasting lipid profile; measurement of glucose, serum iron, and ferritin; total iron-binding capacity; and hepa- titis B surface antigen and hepatitis C virus antibody testing. If test results are normal, a trial of lifestyle modification with observation or further testing for less common causes is appropriate. Additional testing may include ultrasonog- raphy; measurement of α1-antitrypsin and ceruloplasmin; serum protein electrophoresis; and antinuclear antibody, smooth muscle antibody, and liver/kidney microsomal antibody type 1 testing. Referral for further evaluation and possible liver biopsy is recommended if transaminase levels remain elevated for six months or more.
[Show full text]
High-Throughput Discovery of Novel Developmental Phenotypes
High-throughput discovery of novel developmental phenotypes The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Dickinson, M. E., A. M. Flenniken, X. Ji, L. Teboul, M. D. Wong, J. K. White, T. F. Meehan, et al. 2016. “High-throughput discovery of novel developmental phenotypes.” Nature 537 (7621): 508-514. doi:10.1038/nature19356. http://dx.doi.org/10.1038/nature19356. Published Version doi:10.1038/nature19356 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:32071918 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Nature. Manuscript Author Author manuscript; Manuscript Author available in PMC 2017 March 14. Published in final edited form as: Nature. 2016 September 22; 537(7621): 508–514. doi:10.1038/nature19356. High-throughput discovery of novel developmental phenotypes A full list of authors and affiliations appears at the end of the article. Abstract Approximately one third of all mammalian genes are essential for life. Phenotypes resulting from mouse knockouts of these genes have provided tremendous insight into gene function and congenital disorders. As part of the International Mouse Phenotyping Consortium effort to generate and phenotypically characterize 5000 knockout mouse lines, we have identified 410 Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms #Corresponding author: [email protected].
[Show full text]
Gamma Glutamyl Transferase (GGT) NCD 190.32
Medicare National Coverage Determination (NCD) Policy TRANSFERASE GAMMA GLUTAMYL Summary: Gamma Glutamyl Transferase (GGT) NCD 190.32 The terms of Medicare National Coverage Determinations (NCDs) are binding on all fee-for-service (Part A/B) Medicare Administrative Contractors (MACs) and Medicare Advantage (MA) plans. NCDs are not binding, however, on Medicaid and other governmental payers, nor are they binding on commercial payers in their non-MA lines of business. Item/Service Description* Gamma Glutamyl Transferase (GGT) is an intracellular enzyme that appears in blood following leakage from cells. Renal tubules, liver, and pancreas contain high amounts, although the measurement of GGT in serum is almost always used for assessment of hepatobiliary function. Unlike other enzymes which are found in heart, skeletal muscle, and intestinal mucosa as well as liver, the appearance of an elevated level of GGT in serum is almost always the result of liver disease or injury. It is specifically useful to differentiate elevated alkaline phosphatase levels when the source of the alkaline phosphatase increase (bone, liver, or placenta) is unclear. The combination of high alkaline phosphatase and a normal GGT does not, however, rule out liver disease completely. As well as being a very specific marker of hepatobiliary function, GGT is also a very sensitive marker for hepatocellular damage. Abnormal concentrations typically appear before elevations of other liver enzymes or bilirubin are evident. Obstruction of the biliary tract, viral infection (e.g., hepatitis, mononucleosis), metastatic cancer, exposure to hepatotoxins (e.g., organic solvents, drugs, alcohol), and use of drugs that induce microsomal enzymes in the liver (e.g., cimetidine, barbiturates, phenytoin, and carbamazepine) all can cause a moderate to marked increase in GGT serum concentration.
[Show full text]
Como As Enzimas Agem?
O que são enzimas? Catalizadores biológicos - Aceleram reações químicas específicas sem a formação de produtos colaterais PRODUTO SUBSTRATO COMPLEXO SITIO ATIVO ENZIMA SUBSTRATO Características das enzimas 1 - Grande maioria das enzimas são proteínas (algumas moléculas de RNA tem atividade catalítica) 2 - Funcionam em soluções aquosas diluídas, em condições muito suaves de temperatura e pH (mM, pH neutro, 25 a 37oC) Pepsina estômago – pH 2 Enzimas de organismos hipertermófilos (crescem em ambientes quentes) atuam a 95oC 3 - Apresentam alto grau de especificidade por seus reagentes (substratos) Molécula que se liga ao sítio ativo Região da enzima e que vai sofrer onde ocorre a a ação da reação = sítio ativo enzima = substrato 4 - Peso molecular: varia de 12.000 à 1 milhão daltons (Da), são portanto muito grandes quando comparadas ao substrato. 5 - A atividade catalítica das Enzimas depende da integridade de sua conformação protéica nativa – local de atividade catalítica (sitio ativo) Sítio ativo e toda a molécula proporciona um ambiente adequado para ocorrer a reação química desejada sobre o substrato A atividade de algumas enzimas podem depender de outros componentes não proteicos Enzima ativa = Holoenzimas Parte protéica das enzimas + cofator Apoenzima ou apoproteína •Íon inorgânico •Molécula complexa (coenzima) Covalentemente ligados à apoenzima GRUPO PROSTÉTICO COFATORES Elemento com ação complementar ao sitio ativo as enzimas que auxiliam na formação de um ambiente ideal para ocorrer a reação química ou participam diretamente dela
[Show full text]
Relationship of Liver Enzymes to Insulin Sensitivity and Intra-Abdominal Fat
Diabetes Care Publish Ahead of Print, published online July 31, 2007 Relationship of Liver Enzymes to Insulin Sensitivity and Intra-abdominal Fat Tara M Wallace MD*, Kristina M Utzschneider MD*, Jenny Tong MD*, 1Darcy B Carr MD, Sakeneh Zraika PhD, 2Daniel D Bankson MD, 3Robert H Knopp MD, Steven E Kahn MB, ChB. *Metabolism, Endocrinology and Nutrition, VA Puget Sound Health Care System 1Obstetrics and Gynecology, University of Washington, Seattle, WA 2Pathology and Laboratory Medicine, Veterans Affairs Puget Sound Health Care System, University of Washington, Seattle, WA 3Harborview Medical Center, University of Washington, Seattle, WA Running title: Liver enzymes and insulin sensitivity Correspondence to: Steven E. Kahn, M.B., Ch.B. VA Puget Sound Health Care System (151) 1660 S. Columbian Way Seattle, WA 98108 Email: [email protected] Received for publication 18 August 2006 and accepted in revised form 29 June 2007. 1 Copyright American Diabetes Association, Inc., 2007 Liver enzymes and insulin sensitivity ABSTRACT Objective: To determine the relationship between plasma liver enzyme concentrations, insulin sensitivity and intra-abdominal fat (IAF) distribution. Research Design and Methods: Plasma gamma-glutamyl transferase (GGT), aspartate transaminase (AST), alanine transaminase (ALT) levels, insulin sensitivity (SI), IAF and subcutaneous fat (SCF) areas were measured on 177 non-diabetic subjects (75M/102, 31-75 2 -5 years) with no history of liver disease. Based on BMI (< or ≥27.5 kg/m ) and SI (< or ≥7.0x10 min-1 pM-1) subjects were divided into lean insulin sensitive (LIS, n=53), lean insulin resistant (LIR, n=60) and obese insulin resistant (OIR, n=56) groups.
[Show full text]
GFAT and PFK Genes Show Contrasting Regulation of Chitin
www.nature.com/scientificreports OPEN GFAT and PFK genes show contrasting regulation of chitin metabolism in Nilaparvata lugens Cai‑Di Xu1,3, Yong‑Kang Liu2,3, Ling‑Yu Qiu2, Sha‑Sha Wang2, Bi‑Ying Pan2, Yan Li2, Shi‑Gui Wang2 & Bin Tang2* Glutamine:fructose‑6‑phosphate aminotransferase (GFAT) and phosphofructokinase (PFK) are enzymes related to chitin metabolism. RNA interference (RNAi) technology was used to explore the role of these two enzyme genes in chitin metabolism. In this study, we found that GFAT and PFK were highly expressed in the wing bud of Nilaparvata lugens and were increased signifcantly during molting. RNAi of GFAT and PFK both caused severe malformation rates and mortality rates in N. lugens. GFAT inhibition also downregulated GFAT, GNPNA, PGM1, PGM2, UAP, CHS1, CHS1a, CHS1b, Cht1-10, and ENGase. PFK inhibition signifcantly downregulated GFAT; upregulated GNPNA, PGM2, UAP, Cht2‑4, Cht6‑7 at 48 h and then downregulated them at 72 h; upregulated Cht5, Cht8, Cht10, and ENGase; downregulated Cht9 at 48 h and then upregulated it at 72 h; and upregulated CHS1, CHS1a, and CHS1b. In conclusion, GFAT and PFK regulated chitin degradation and remodeling by regulating the expression of genes related to the chitin metabolism and exert opposite efects on these genes. These results may be benefcial to develop new chitin synthesis inhibitors for pest control. Chitin is a linear polymer composed of N-acetylglucosamine units connected by β-1, 4-glycoside bonds and is the second most abundant biopolymer in nature. It is widely distributed in fungi, nematodes, and arthropods1. In insects, chitin is a major component of the exoskeleton, trachea, and the peritrophic matrix that lines the midgut epithelium1–4.
[Show full text]
Alanine Transaminase Assay (ALT) Catalog #8478 100 Tests in 96-Well Plate
Alanine Transaminase Assay (ALT) Catalog #8478 100 Tests in 96-well plate Product Description Alanine Aminotransferase (ALT), also known as serum glutamic-pyruvic transaminase (SGPT), catalyzes the reversible transfer of an amino group from alanine to α-ketoglutarate. The products of this transamination reaction are pyruvate and glutamate. ALT is found primarily in liver and serum, but occurs in other tissues as well. Significantly elevated serum ALT levels often suggest the existence of medical problems, such as hepatocellular injury, hepatitis, diabetes, bile duct problem and myopathy. This colorimetric assay is based on the oxidization of NADH to NAD in the presence of pyruvate and lactate dehydrogenase. The ALT activity is determined by assaying the rate of NADH oxidation, which is proportional to the reduction in absorbance at 340nm over time (ΔOD340nm/min). Kit Components Cat. No. # of vials Reagent Quantity Storage 8478a 1 Assay buffer 10 mL -20°C 8478b 1 ALT standard 10 µL -20°C 8478c 1 Substrate mix 1.0 mL -20°C 8478d 1 Cofactor 0.8 mL -20°C 8478e 1 Enzyme 0.2 mL -80°C Product Use The ALT kit measures the alanine transaminase activity of different types of samples, such as serum, plasma and tissues. ALT is for research use only. It is not approved for human or animal use, or for application in in vitro diagnostic procedures. Quality Control Serially diluted alanine transaminase solutions with concentrations ranging from 0.03125 to 1.0 U/mL are measured with the ScienCell™ Alanine Transaminase Assay kit. The decrease in OD340nm is monitored as a function of time (Figure 1) and the resulting standard of ∆OD340nm/min vs alanine transaminase activity are plotted (Figure 2).
[Show full text]
Pyridoxine (Pyridoxamine) 5'-Phosphate Oxidase In
PYRIDOXINE (PYRIDOXAMINE) 5’-PHOSPHATE OXIDASE IN ARABIDOPSIS THALIANA Except where reference is made to the work of others, the work described in this dissertation is my own or was done in collaboration with my advisory committee. This dissertation does not include proprietary or classified information. Yuying Sang Certificate of Approval: Robert D. Locy Narendra K. Singh, Chair Professor Professor Biological Sciences Biological Sciences Joe H. Cherry Joanna Wysocka-Diller Emeritus Professor Associate Professor Biological Sciences Biological Sciences Fenny Dane George T. Flowers Professor Dean Horticulture Graduate School PYRIDOXINE (PYRIDOXAMINE) 5’-PHOSPHATE OXIDASE IN ARABIDOPSIS THALIANA Yuying Sang A Dissertation Submitted to the Graduate Faculty of Auburn University in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy Auburn, Alabama December 19, 2008 PYRIDOXINE (PYRIDOXAMINE) 5’-PHOSPHATE OXIDASE IN ARABIDOPSIS THALIANA Yuying Sang Permission is granted to Auburn University to make copies of this dissertation at its discretion, upon request of individuals of institutions and at their expense. The author reserves all publication right. Signature of Author Date of Graduation iii VITA Yuying Sang, daughter of Shiqing Sang and Guilan Wang, was born on January 7, 1975, in Chiping, Shandong, People’s Republic of China. She received the Bachelor of Science degree in Biology in July 1997 from Shandong Normal University and entered the Graduate School of Kunming Institute of Botany, Chinese Academy of Sciences. In the July of 2000, she graduated with a Master of Science degree in Botany and joined East China University of Science and Technology as a lab manager in the Department of Bioengineering.
[Show full text]
Pdf 2019; 572: 402-6
Theranostics 2021, Vol. 11, Issue 12 5650 Ivyspring International Publisher Theranostics 2021; 11(12): 5650-5674. doi: 10.7150/thno.55482 Research Paper Endogenous glutamate determines ferroptosis sensitivity via ADCY10-dependent YAP suppression in lung adenocarcinoma Xiao Zhang1,2#, Keke Yu3#, Lifang Ma1,2#, Zijun Qian4#, Xiaoting Tian2, Yayou Miao2, Yongjie Niu4, Xin Xu4, Susu Guo5, Yueyue Yang5, Zhixian Wang4, Xiangfei Xue5, Chuanjia Gu6,7, Wentao Fang1, Jiayuan Sun6,7, Yongchun Yu2 and Jiayi Wang1,2,5 1. Department of Thoracic Surgery, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai, 200030, China. 2. Shanghai Institute of Thoracic Oncology, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai, 200030, China. 3. Department of Bio-bank, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai, 200030, China. 4. Shanghai Municipal Hospital of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine, Shanghai, 200071, China. 5. Department of Clinical Laboratory Medicine, Shanghai Tenth People’s Hospital of Tongji University, Shanghai, 200072, China. 6. Department of Respiratory Endoscopy, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai, 200030, China. 7. Department of Respiratory and Critical Care Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai 200030, China. #These authors contributed equally to the work. Corresponding authors: Jiayuan Sun, Department of Respiratory Endoscopy, Department of Respiratory and Critical Care Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University, Shanghai 200030, China; E-mail: [email protected]. Yongchun Yu, Shanghai Chest Hospital, Shanghai Jiao Tong University, No. 241 Huaihai West Road, Shanghai, 200030, China; E-mail: [email protected]. Jiayi Wang, Department of Thoracic Surgery, Shanghai Institute of Thoracic Tumors, Shanghai Chest Hospital, Shanghai Jiao Tong University, No.
[Show full text]
Glutamine Deprivation Triggers NAGK-Dependent Hexosamine Salvage
bioRxiv preprint doi: https://doi.org/10.1101/2020.09.13.294116; this version posted September 13, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Glutamine deprivation triggers NAGK-dependent hexosamine salvage Campbell, S.L.1,2, Mesaros, C.3, Affronti, H.1,2, Tsang, T.1,2, Noji, M.1,2, Sun, K.4, Izzo, L.1,2, Trefely, S.1,2,5, Kruijning, S.1,2, Blair, I.A.3, Wellen, K.E.1,2,6 1Department of Cancer Biology, 2Abramson Family Cancer Research Institute, 3Department of Systems Pharmacology and Translational Therapeutics, 4Pancreatic Cancer Research Center, Perelman School of Medicine, University of Pennsylvania; 5Center for Metabolic Disease Research, Department of Microbiology and Immunology, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140. 6Corresponding author. Abstract Tumors of many types exhibit aberrant glycosylation, which can impact cancer progression and therapeutic responses. The hexosamine biosynthesis pathway (HBP) branches from glycolysis at fructose-6-phosphate to synthesize uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a major substrate for glycosylation in the cell. HBP enzyme gene expression is elevated in pancreatic ductal adenocarcinoma (PDA), and studies have pointed to the potential significance of the HBP as a therapeutic target. Yet, the PDA tumor microenvironment is nutrient poor, and adaptive nutrient acquisition strategies support tumorigenesis. Here, we identify that pancreatic cancer cells salvage GlcNAc via N-acetylglucosamine kinase (NAGK), particularly under glutamine limitation. Glutamine deprivation suppresses de novo HBP flux and triggers upregulation of NAGK.
[Show full text]
Functional Dependency Analysis Identifies Potential Druggable
cancers Article Functional Dependency Analysis Identifies Potential Druggable Targets in Acute Myeloid Leukemia 1, 1, 2 3 Yujia Zhou y , Gregory P. Takacs y , Jatinder K. Lamba , Christopher Vulpe and Christopher R. Cogle 1,* 1 Division of Hematology and Oncology, Department of Medicine, College of Medicine, University of Florida, Gainesville, FL 32610-0278, USA; yzhou1996@ufl.edu (Y.Z.); gtakacs@ufl.edu (G.P.T.) 2 Department of Pharmacotherapy and Translational Research, College of Pharmacy, University of Florida, Gainesville, FL 32610-0278, USA; [email protected]fl.edu 3 Department of Physiological Sciences, College of Veterinary Medicine, University of Florida, Gainesville, FL 32610-0278, USA; cvulpe@ufl.edu * Correspondence: [email protected]fl.edu; Tel.: +1-(352)-273-7493; Fax: +1-(352)-273-5006 Authors contributed equally. y Received: 3 November 2020; Accepted: 7 December 2020; Published: 10 December 2020 Simple Summary: New drugs are needed for treating acute myeloid leukemia (AML). We analyzed data from genome-edited leukemia cells to identify druggable targets. These targets were necessary for AML cell survival and had favorable binding sites for drug development. Two lists of genes are provided for target validation, drug discovery, and drug development. The deKO list contains gene-targets with existing compounds in development. The disKO list contains gene-targets without existing compounds yet and represent novel targets for drug discovery. Abstract: Refractory disease is a major challenge in treating patients with acute myeloid leukemia (AML). Whereas the armamentarium has expanded in the past few years for treating AML, long-term survival outcomes have yet to be proven. To further expand the arsenal for treating AML, we searched for druggable gene targets in AML by analyzing screening data from a lentiviral-based genome-wide pooled CRISPR-Cas9 library and gene knockout (KO) dependency scores in 15 AML cell lines (HEL, MV411, OCIAML2, THP1, NOMO1, EOL1, KASUMI1, NB4, OCIAML3, MOLM13, TF1, U937, F36P, AML193, P31FUJ).
[Show full text]
Transcriptome Analysis of Differentially Expressed Mrna Related to Pigeon Muscle Development
animals Article Transcriptome Analysis of Differentially Expressed mRNA Related to Pigeon Muscle Development Hao Ding 1,2,† , Yueyue Lin 1,2,†, Tao Zhang 1,2,* , Lan Chen 1,2, Genxi Zhang 1,2, Jinyu Wang 1,2, Kaizhou Xie 1,2 and Guojun Dai 1,2 1 College of Animal Science and Technology, Yangzhou University, Yangzhou 225000, China; [email protected] (H.D.); [email protected] (Y.L.); [email protected] (L.C.); [email protected] (G.Z.); [email protected] (J.W.); [email protected] (K.X.); [email protected] (G.D.) 2 Joint International Research Laboratory of Agriculture and Agri−Product Safety, Ministry of Education, Yangzhou University, Yangzhou 225000, China * Correspondence: [email protected] † These authors are contributed equally to this study. Simple Summary: The growth and development of skeletal muscle determine the meat production performance of pigeons and are regulated by complex gene networks. To explore the genes involved in regulating the growth and development of pigeon skeletal muscle, RNA sequencing (RNA−seq) was used to characterise gene expression proﬁles during the development and growth of pigeon breast muscle and identify differentially expressed genes (DEGs) among different stages. This study expanded the diversity of pigeon mRNA, and it was helpful to understand the role of mRNA in pigeon muscle development and growth. Abstract: The mechanisms behind the gene expression and regulation that modulate the development and growth of pigeon skeletal muscle remain largely unknown. In this study, we performed gene Citation: Ding, H.; Lin, Y.; Zhang, T.; expression analysis on skeletal muscle samples at different developmental and growth stages using Chen, L.; Zhang, G.; Wang, J.; Xie, K.; RNA sequencing (RNA−Seq).
[Show full text]