ACSL5 Polyclonal Antibody Gene Symbol: ACSL5

Total Page：16

File Type：pdf, Size：1020Kb

ACSL5 polyclonal antibody Gene Symbol: ACSL5 Gene Alias: ACS2, ACS5, FACL5 Catalog Number: PAB7030 Gene Summary: The protein encoded by this gene is an Regulatory Status: For research use only (RUO) isozyme of the long-chain fatty-acid-coenzyme A ligase Product Description: Goat polyclonal antibody raised family. Although differing in substrate specificity, against synthetic peptide of ACSL5. subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty Immunogen: A synthetic peptide corresponding to acids into fatty acyl-CoA esters, and thereby play a key human ACSL5. role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in uterus and spleen, and in Sequence: C-RTQIDSLYEHIQD trace amounts in normal brain, but has markedly increased levels in malignant gliomas. This gene Host: Goat functions in mediating fatty acid-induced glioma cell growth. Three transcript variants encoding two different Theoretical MW (kDa): 82.3, 76 isoforms have been found for this gene. [provided by RefSeq] Reactivity: Human References: Applications: ELISA, WB-Ti 1. Coeliac disease is associated with impaired (See our web site product page for detailed applications expression of acyl-CoA-synthetase 5. Obermuller N, information) Keith M, Kopitz J, Autschbach F, Schirmacher P, Protocols: See our web site at Gassler N. Int J Colorectal Dis. 2006 Mar;21(2):130-4. http://www.abnova.com/support/protocols.asp or product Epub 2005 Apr 5. page for detailed protocols Specificity: This antibody is expected to recognize isoform a (NP_057318.2) and isoform b (NP_976313.1 and NP_976314.1). Form: Liquid Purification: Antigen affinity purification Concentration: 0.5 mg/mL Recommend Usage: ELISA (1:16000) Western Blot (1-3 ug/mL) The optimal working dilution should be determined by the end user. Storage Buffer: In Tris saline, pH 7.3 (0.5% BSA, 0.02% sodium azide) Storage Instruction: Store at -20°C. Aliquot to avoid repeated freezing and thawing. Entrez GeneID: 51703 Page 1/1 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

DYSREGULATION of LONG-CHAIN ACYL-Coa SYNTHETASES in CANCER and THEIR TARGETING STRATEGIES in ANTICANCER THERAPY Md Amir Hossain1, Jun Ma2, Yong Yang1 1
Hossain et al RJLBPCS 2020 www.rjlbpcs.com Life Science Informatics Publications Original Review Article DOI: 10.26479/2020.0603.06 DYSREGULATION OF LONG-CHAIN ACYL-CoA SYNTHETASES IN CANCER AND THEIR TARGETING STRATEGIES IN ANTICANCER THERAPY Md Amir Hossain1, Jun Ma2, Yong Yang1 1. Academic Institute of Pharmaceutical Science, China Pharmaceutical University, Nanjing, China. 2. Ningxia Baoshihua Hospital, Ningxia, China. ABSTRACT: Cancer is a leading cause of death worldwide, and the number of cases globally continues to increase. Cancer is caused by certain changes in genes that are involved in controlling cell functions and cell division. Notably, metabolic dysregulation is one the hallmarks of cancer, and increases in fatty acid metabolism have been demonstrated to promote the growth and survival of a variety of cancers. In human, fatty acids either can be breakdown into acetyl-CoA through catabolic metabolism and aid in ATP generation or in the anabolic metabolism they can incorporate into triacylglycerol and phospholipid. Importantly, both of these pathways need activation of fatty acids, and the key players in this activation of fatty acids are the long-chain acyl-CoA synthetases (ACSLs) that are commonly dysregulated in cancer and associated with oncogenesis and survival. Therefore, it provides a rationale to target ACSLs in cancer. This review summarizes the current understanding of long-chain acyl-CoA synthetases in cancer and their targeting opportunities. KEYWORDS: Acyl-CoA synthetases, cancer, fatty acid, lipid metabolism. Article History: Received: April 15, 2020; Revised: May 10, 2020; Accepted: May 30, 2020. Corresponding Author: Prof. Yong Yang* Academic Institute of Pharmaceutical Science, China Pharmaceutical University, Nanjing, China.
[Show full text]
Flawed Phospholipid Formation Or Faulty Fatty Acid Oxidation: Determining the Cause of Mitochondrial Dysfunction in Hearts Lacking Acsl1
FLAWED PHOSPHOLIPID FORMATION OR FAULTY FATTY ACID OXIDATION: DETERMINING THE CAUSE OF MITOCHONDRIAL DYSFUNCTION IN HEARTS LACKING ACSL1 Trisha J. Grevengoed A dissertation submitted to the faculty at the University of North Carolina at Chapel Hill in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Nutrition (Biochemistry) in the School of Public Health. Chapel Hill 2015 Approved by: Rosalind A. Coleman Stephen D. Hursting Liza Makowski Leslie V. Parise Steven H. Zeisel © 2015 Trisha J. Grevengoed ALL RIGHTS RESERVED ii ABSTRACT Trisha J. Grevengoed: Fatty acid activation in cardiac mitochondria: The role of ACSL1 in phospholipid formation and remodeling, substrate switching, and autophagic flux (Under the direction of Rosalind A. Coleman) Cardiovascular disease is the number one cause of death worldwide. In the heart, mitochondria provide up to 95% of energy, with most of this energy coming from metabolism of fatty acids (FA). FA must be converted to acyl-CoAs by acyl-CoA synthetases (ACS) before entry into pathways of β- oxidation or glycerolipid synthesis. ACSL1 contributes more than 90% of total cardiac ACSL activity, and mice with an inducible knockout of ACSL1 (Acsl1T-/-) have impaired cardiac FA oxidation. The effects of loss of ACSL1 on mitochondrial respiratory function, phospholipid formation, or autophagic flux have not yet been studied. Acsl1T-/- hearts contained 3-fold more mitochondria with abnormal structure and displayed lower respiratory function. Because ACSL1 exhibited a strong substrate preference for linoleate (18:2), we investigated the composition of mitochondrial phospholipids. Acsl1T-/- hearts contained 83% less tetralinoleoyl-cardiolipin (CL), the major form present in control hearts.
[Show full text]
Elucidating Biological Roles of Novel Murine Genes in Hearing Impairment in Africa
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 19 September 2019 doi:10.20944/preprints201909.0222.v1 Review Elucidating Biological Roles of Novel Murine Genes in Hearing Impairment in Africa Oluwafemi Gabriel Oluwole,1* Abdoulaye Yal 1,2, Edmond Wonkam1, Noluthando Manyisa1, Jack Morrice1, Gaston K. Mazanda1 and Ambroise Wonkam1* 1Division of Human Genetics, Department of Pathology, Faculty of Health Sciences, University of Cape Town, Observatory, Cape Town, South Africa. 2Department of Neurology, Point G Teaching Hospital, University of Sciences, Techniques and Technology, Bamako, Mali. *Correspondence to: [email protected]; [email protected] Abstract: The prevalence of congenital hearing impairment (HI) is highest in Africa. Estimates evaluated genetic causes to account for 31% of HI cases in Africa, but the identification of associated causative genes mutations have been challenging. In this study, we reviewed the potential roles, in humans, of 38 novel genes identified in a murine study. We gathered information from various genomic annotation databases and performed functional enrichment analysis using online resources i.e. genemania and g.proflier. Results revealed that 27/38 genes are express mostly in the brain, suggesting additional cognitive roles. Indeed, HERC1- R3250X had been associated with intellectual disability in a Moroccan family. A homozygous 216-bp deletion in KLC2 was found in two siblings of Egyptian descent with spastic paraplegia. Up to 27/38 murine genes have link to at least a disease, and the commonest mode of inheritance is autosomal recessive (n=8). Network analysis indicates that 20 other genes have intermediate and biological links to the novel genes, suggesting their possible roles in HI.
[Show full text]
An Investigation of Roles for SIRT1 and Dietary Polyphenols in Modulating the Ageing Process Through DNA Methylation
An investigation of roles for SIRT1 and dietary polyphenols in modulating the ageing process through DNA methylation Laura Jane Ions Thesis submitted for the degree of Doctor of Philosophy Institute for Cell and Molecular Biosciences, Newcastle University, UK September 2011 Declaration I certify that this thesis is my own work, except where stated, and has not been previously submitted for a degree or any other qualification at this or any other university. Laura J Ions September 2011 Thank you to Professor Dianne Ford and Dr Luisa Wakeling whose support, guidance and enthusiasm have been invaluable over the last four years. Abstract Dietary restriction (DR) can increase lifespan across evolutionarily distinct species, from yeast to rodents. The NAD+-dependent (class III) histone deacetylase SIRT1 in mammals, and its ortholog in other species, may play a major role in this response, but may affect ‘healthspan’ (number of years of good health), rather than lifespan per se. Ageing is accompanied by changes in genome methylation, which may be causal in the ageing process. Since histones are one of the many substrates that are deacetylated by SIRT1, we hypothesised that epigenetic effects of SIRT1 activity – and specifically effects on DNA methylation, which is associated closely with histone acetylation – mediate some of the beneficial effects of DR that contribute to increased healthspan. We also propose that dietary polyphenols may act at the cellular level in a similar way. To test this hypothesis, we first investigated effects of altering SIRT1 expression, by overexpression of a transgene or siRNA-mediated knockdown, on global DNA methylation (methylation of the LINE-1 element) in the human intestinal cell line, Caco-2.
[Show full text]
ACSL5 Rabbit Pab
Leader in Biomolecular Solutions for Life Science ACSL5 Rabbit pAb Catalog No.: A1270 1 Publications Basic Information Background Catalog No. The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A A1270 ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into Observed MW fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid 70-76kDa degradation. This isozyme is highly expressed in uterus and spleen, and in trace amounts in normal brain, but has markedly increased levels in malignant gliomas. This Calculated MW gene functions in mediating fatty acid-induced glioma cell growth. Three transcript 73kDa/75kDa/82kDa variants encoding two different isoforms have been found for this gene. Category Primary antibody Applications WB,IHC Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 51703 Q9ULC5 IHC 1:20 - 1:100 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 500-739 of human ACSL5 (NP_057318.2). Synonyms ACSL5;ACS2;ACS5;FACL5 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using ACSL5 antibody (A1270) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane.
[Show full text]
NIH Public Access Author Manuscript Future Lipidol
NIH Public Access Author Manuscript Future Lipidol. Author manuscript; available in PMC 2010 March 29. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Future Lipidol. 2007 August ; 2(4): 465±476. Long-chain acyl-CoA synthetases and fatty acid channeling Douglas G. Mashek1, Lei O. Li2, and Rosalind A. Coleman2 1 Department of Food Science and Nutrition, University of Minnesota, St. Paul, Minnesota, 55108 2 Department of Nutrition, University of North Carolina, Chapel Hill, North Carolina, 27599 Abstract Thirteen homologous proteins comprise the long-chain acyl-CoA synthetase (ACSL), fatty acid transport protein (FATP), and bubblegum (ACSBG) subfamilies that activate long-chain and very- long-chain fatty acids to form acyl-CoAs. Gain- and loss-of-function studies show marked differences in the ability of these enzymes to channel fatty acids into different pathways of complex lipid synthesis. Further, the ability of the ACSLs and FATPs to enhance cellular FA uptake does not always require these proteins to be present on the plasma membrane; instead, FA uptake can be increased by enhancing its conversion to acyl-CoA and its metabolism in downstream pathways. Since altered fatty acid metabolism is a hallmark of numerous metabolic diseases and pathological conditions, the ACSL, FATP and ACSBG isoforms are likely to play important roles in disease etiology. A family of acyl-CoA synthetases activates intracellular long-chain fatty acids Before a fatty acid (FA) from an exogenous or endogenous source can enter any metabolic pathway with the exception of eicosanoid metabolism, it must first be activated to form an acyl-CoA.
[Show full text]
Details About Three Fatty Acid Oxidation Pathways Occurring in Man
Supplement information Details about three fatty acid oxidation pathways occurring in man Alpha oxidation Definition: Oxidation of the alpha carbon of the fatty acid, chain shortened by 1 carbon atom. Localization: Peroxisomes1 Substrates: Phytanic acid, 3-methyl fatty acids and their alcohol and aldehyde derivatives, metabolites of farnesol, geranylgeraniol, and dolichols2, 3. Steps in the pathway: Activation requires ATP and CoA. Hydroxylation requires iron, ascorbate and alpha-keto-glutarate as cofactors and secondary substrates. Lysis requires thymine pyrophosphate and magnesium ions. Dehydrogenation requires NADP. End products are transported into mitochondria for further oxidation. Enzymes and genes involved: Very long-chain acyl-CoA synthetase (E.C. 6.2.1.-) (SLC27A2, GeneID: 11001)4, phytanoyl-CoA dioxygenase (E.C. 1.14.11.18, PHYH, GeneID: 5264), 2-hydrosyphytanoyl-coA lyase (E.C. 4.1.-.-, HACL1, GeneID: 26061), and aldehyde dehydrogenase (E.C. 1.2.1.3, ALDH3A2, GeneID: 224). Disorders associated: Zellweger syndrome including RCDP type 1, where PTS2 receptor is defective and PHYH is unable to enter peroxisomes, and Refsum’s disease. Special features/ purpose: At the sub cellular level, the activation step can occur in the mitochondrion, endoplasmic reticulum, and peroxisome. Formic acid is the main byproduct of this pathway as opposed to carbon dioxide. Phytanic acid usually undergoes alpha oxidation; however, under conditions of enzyme deficiency, it undergoes omega oxidation and 3- methyladipic acid is produced as the end product5. Omega oxidation Definition: Oxidation of omega carbon of the fatty acid for generation of mono- and di- carboxylic acids. No chain shortening occurs. Localization: Fatty acid shuttles between cytosol and microsomes before entering the peroxisomes6.
[Show full text]
ACSL5 (Human) IP-WB Antibody Pair
ACSL5 (Human) IP-WB Antibody functions in mediating fatty acid-induced glioma cell Pair growth. Three transcript variants encoding two different isoforms have been found for this gene. [provided by Catalog Number: H00051703-PW2 RefSeq] Regulation Status: For research use only (RUO) Product Description: This IP-WB antibody pair set comes with one antibody for immunoprecipitation and another to detect the precipitated protein in western blot. Reactivity: Human Applications: IP-WB (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product page for detailed protocols Supplied Product: Antibody pair set content: 1. Antibody pair for IP: rabbit polyclonal anti-ACSL5 (300 ul) 2. Antibody pair for WB: mouse purified polyclonal anti-ACSL5 (50 ug) Storage Instruction: Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use. Entrez GeneID: 51703 Gene Symbol: ACSL5 Gene Alias: ACS2, ACS5, FACL5 Gene Summary: The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in uterus and spleen, and in trace amounts in normal brain, but has markedly increased levels in malignant gliomas. This gene Page 1/1 Powered by TCPDF (www.tcpdf.org).
[Show full text]
Download
www.aging-us.com AGING 2021, Vol. 13, No. 12 Research Paper Immune infiltration and a ferroptosis-associated gene signature for predicting the prognosis of patients with endometrial cancer Yin Weijiao1,2, Liao Fuchun1, Chen Mengjie1, Qin Xiaoqing1, Lai Hao3, Lin Yuan3, Yao Desheng1 1Department of Gynecologic Oncology, Guangxi Medical University Cancer Hospital, Nanning, Guangxi Zhuang Autonomous Region 530021, PR China 2Henan Key Laboratory of Cancer Epigenetics, Cancer Hospital, The First Affiliated Hospital, College of Clinical Medicine, Medical College of Henan University of Science and Technology, Luoyang, PR China 3Department of Gastrointestinal Surgery, Guangxi Medical University Cancer Hospital, Nanning, Guangxi Zhuang Autonomous Region 530021, PR China Correspondence to: Yao Desheng; email: [email protected] Keywords: ferroptosis, endometrial cancer, prognosis Received: March 24, 2021 Accepted: June 4, 2021 Published: June 24, 2021 Copyright: © 2021 Weijiao et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT Ferroptosis, a form of programmed cell death induced by excess iron-dependent lipid peroxidation product accumulation, plays a critical role in cancer. However, there are few reports about ferroptosis in endometrial cancer (EC). This article explores the relationship between ferroptosis-related gene (FRG) expression and prognosis in EC patients. One hundred thirty-five FRGs were obtained by mining the literature, retrieving GeneCards and analyzing 552 malignant uterine corpus endometrial carcinoma (UCEC) samples, which were randomly assigned to training and testing groups (1:1 ratio), and 23 normal samples from The Cancer Genome Atlas (TCGA).
[Show full text]
Differential Expression and Prognostic Role of Selected Genes in Colorectal Cancer Patients
ANTICANCER RESEARCH 33: 4855-4866 (2013) Differential Expression and Prognostic Role of Selected Genes in Colorectal Cancer Patients PAVEL PITULE1,2, ONDREJ VYCITAL3, JAN BRUHA3, PETR NOVAK3, PETR HOSEK1,4, VLADISLAV TRESKA3, IVONA HLAVATA5, PAVEL SOUCEK1,5, MILENA KRALICKOVA1,2 and VACLAV LISKA1,3,6 1Biomedical Center, 2Department of Histology and Embryology and 6Department of Surgery, Faculty of Medicine in Pilsen, Charles University in Prague, Pilsen, Czech Republic; 3Department of Surgery, Teaching Hospital and Medical School, Pilsen, Czech Republic; 4Department of Biomedical Informatics, Faculty of Biomedical Engineering, Czech Technical University in Prague, Kladno, Czech Republic; 5Department of Toxicogenomics, National Institute of Public Health, Prague, Czech Republic Abstract. Aim: Colorectal cancer (CRC) is one of the regulation of CLDN23 had shorter OS (p=0.045). In the most common malignant diseases. The aim of our study was group of patients without distant metastases, longer OS and to describe the expression status of 12 selected candidate disease-free interval (DFI) were found for patients with genes, by comparing paired samples of healthy colon higher SLC26A2 expression in tumour tissues (p=0.036 and mucosa and tumour tissues and to correlate obtained data p=0.011, respectively). In the same group, lower expression with clinical and pathological features, with the goal of of VSNL1 in healthy tissue corresponded to a longer DFI revealing associations for individual gene expressions and (p=0.020), smaller decrease of SLC26A2 and ACSL5 meant tumour behaviour. Materials and Methods: Samples from longer DFI (p=0.041 and p=0.040, respectively), as did 53 patients with CRC were analyzed.
[Show full text]
Barkbase: Epigenomic Annotation of Canine Genomes
G C A T T A C G G C A T genes Article BarkBase: Epigenomic Annotation of Canine Genomes Kate Megquier 1, Diane P. Genereux 1 , Jessica Hekman 1 , Ross Swofford 1, Jason Turner-Maier 1, Jeremy Johnson 1, Jacob Alonso 1, Xue Li 1,2, Kathleen Morrill 1,2, Lynne J. Anguish 3, Michele Koltookian 1, Brittney Logan 2, Claire R. Sharp 4 , Lluis Ferrer 5, Kerstin Lindblad-Toh 1,6, Vicki N. Meyers-Wallen 7, Andrew Hoffman 8,9 and Elinor K. Karlsson 1,2,10,* 1 Vertebrate Genomics, Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA; [email protected] (K.M.); [email protected] (D.P.G.); [email protected] (J.H.); swoff[email protected] (R.S.); [email protected] (J.T.-M.); [email protected] (J.J.); [email protected] (J.A.); [email protected] (X.L.); [email protected] (K.M.); [email protected] (M.K.); [email protected] (K.L.-T.) 2 Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA; [email protected] 3 Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; [email protected] 4 School of Veterinary and Life Sciences, College of Veterinary Medicine, Murdoch University, Perth, Murdoch, WA 6150, Australia; [email protected] 5 Departament de Medicina i Cirurgia Animals Veterinary School, Universitat Autonoma de Barcelona, 08193 Barcelona, Spain; [email protected] 6 Science for Life Laboratory, Department of Medical Biochemistry &
[Show full text]
Association of Long-Chain Acyl-Coenzyme a Synthetase 5 Expression in Human Breast Cancer by Estrogen Receptor Status and Its Clinical Significance
ONCOLOGY REPORTS 37: 3253-3260, 2017 Association of long-chain acyl-coenzyme A synthetase 5 expression in human breast cancer by estrogen receptor status and its clinical significance MEng-CHI YEn1*, JUNG-YU KAN2,3*, CHIA-Jung HSIEH4,5, PO-LIn KuO2, MIng-FEng HOu2,3 and YA-LIng HSu4 1Department of Emergency Medicine, Kaohsiung Medical university Hospital, Kaohsiung 807; 2graduate Institute of Clinical Medicine, College of Medicine, Kaohsiung Medical university, Kaohsiung 807; 3Department of Breast Surgery, Kaohsiung Medical university Hospital, Kaohsiung 807; 4graduate Institute of Medicine, College of Medicine, Kaohsiung Medical university, Kaohsiung 807; 5Department of Chinese Medicine, Kaohsiung Medical university Hospital, Kaohsiung 807, Taiwan, R.O.C. Received February 6, 2017; Accepted April 21, 2017 DOI: 10.3892/or.2017.5610 Abstract. The lipid metabolic enzymes are considered suggest that ACSL1, ACSL4 and ACSL5 expression is regu- candidate therapeutic targets for breast cancer. Long-chain lated by ER signaling pathways and ACSL5 is a potential novel acyl-coenzyme A (CoA) synthase (ACSL) is one of lipid biomarker for predicting prognosis of breast cancer patients. metabolic enzymes and converts free-fatty acid to fatty acid-CoA. Five ACSL isoforms including ACSL1, ACSL3, Introduction ACSL4, ACSL5 and ACSL6 are identified in human. High ACSL4 expression has been observed in aggressive breast Dysregulation of metabolic pathways, including regulation cancer phenotype. However, the role of other isoforms is still of glucose transporter, tricarboxylic acid cycle (TCA cycle), little-known. We therefore, analyzed the expression of ACSL pentose phosphate pathway and mitochondria respiratory isoforms in each subtype of breast cancer within METABRIC chain are observed in many types of cancers (1).
[Show full text]