Anti-Human EPHA4 / EPH Receptor A4 (Internal) Polyclonal Antibody

Total Page：16

File Type：pdf, Size：1020Kb

For Research Use Only. REV: 9/9/2014 Anti-Human EPHA4 / EPH Receptor A4 (Internal) Polyclonal Antibody CatalogID MC-2841 Target Protein EPH receptor A4 (EPHA4) Synonyms EPHA4 Antibody, CEK8 Antibody, EK8 Antibody, Ephrin type-A receptor 4 Antibody, HEK8 Antibody, SEK Antibody, TYRO1 Antibody, TYRO1 protein tyrosine kinase Antibody, Tyrosine-protein kinase TYRO1 Antibody, EPH receptor A4 Antibody, EPH-like kinase 8 Antibody Family / Subfamily Protein Kinase / Ephrin Receptor Host EPHA4 antibody was produced in Rabbit Clonality Polyclonal Immunogen Species EPHA4 / EPH Receptor A4 antibody was raised against Human Antigen Type Synthetic peptide Immunogen EPHA4 / EPH Receptor A4 antibody was raised against synthetic 18 amino acid peptide from internal region of human EPHA4. Percent identity with other species by BLAST analysis: Human, Gorilla, Gibbon, Monkey, Marmoset, Panda, Bovine, Dog, Bat, Horse, Pig (100%); Mouse, Rat, Hamster, Elephant, Rabbit, Opossum, Platypus, Xenopus (94%); Turkey, Chicken (89%); Lizard (83%). Specificity Human EPHA4. BLAST analysis of the peptide immunogen showed no homology with other human proteins. Epitope Internal Reactivity Human (human tissues have been tested in IHC with FFPE) Predicted Reactivity Gorilla, Gibbon, Monkey, Bat, Bovine, Dog, Horse, Pig, Mouse, Rat, Hamster, Rabbit, Xenopus Purification Immunoaffinity purified Presentation PBS, 0.1% sodium azide. Recommended Storage Long term: -70°C; Short term: +4°C Uses IHC - Paraffin (3 μg/ml) (Optimal dilution to be determined by the researcher) Size 50 µg Concentration 1 mg/ml For research use only. Not intended for human, diagnostic, therapeutic, or drug use. Immunohistochemistry Anti-EPHA4 antibody MC-2841 IHC of human kidney, glomerulus. Immunohistochemistry of formalin-fixed, paraffin- embedded tissue after heat-induced antigen retrieval. 15A Constitution Way · Woburn, MA 01801 · Phone: 1.800.200.5459 · Fax: 781-939-6963 · www.mblintl.com .

Copy Link

Recommended publications

Structural and Functional Insights Into the Transmembrane Domain Association of Eph Receptors
International Journal of Molecular Sciences Review Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors Amita R. Sahoo 1 and Matthias Buck 1,2,3,4,* 1 Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA; [email protected] 2 Department of Neurosciences, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA 3 Department of Pharmacology, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA 4 Case Comprehensive Cancer Center, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA * Correspondence: [email protected] Abstract: Eph receptors are the largest family of receptor tyrosine kinases and by interactions with ephrin ligands mediate a myriad of processes from embryonic development to adult tissue homeostasis. The interaction of Eph receptors, especially at their transmembrane (TM) domains is key to understanding their mechanism of signal transduction across cellular membranes. We review the structural and functional aspects of EphA1/A2 association and the techniques used to investigate their TM domains: NMR, molecular modelling/dynamics simulations and ﬂuorescence. We also introduce transmembrane peptides, which can be used to alter Eph receptor signaling and we provide a perspective for future studies. Citation: Sahoo, A.R.; Buck, M. Keywords: receptor tyrosine kinase (RTKs); Eph receptors; TM dimerization; transmembrane Structural and Functional Insights domain (TMD) into the Transmembrane Domain Association of Eph Receptors. Int. J. Mol. Sci. 2021, 22, 8593. https:// doi.org/10.3390/ijms22168593 1. The Family of Eph Receptors, Their Domain Structure and Function Erythropoietin-producing hepatocellular carcinoma receptors (Ephs) represent the Academic Editors: Dimitar B.
[Show full text]
HCC and Cancer Mutated Genes Summarized in the Literature Gene Symbol Gene Name References*
HCC and cancer mutated genes summarized in the literature Gene symbol Gene name References* A2M Alpha-2-macroglobulin (4) ABL1 c-abl oncogene 1, receptor tyrosine kinase (4,5,22) ACBD7 Acyl-Coenzyme A binding domain containing 7 (23) ACTL6A Actin-like 6A (4,5) ACTL6B Actin-like 6B (4) ACVR1B Activin A receptor, type IB (21,22) ACVR2A Activin A receptor, type IIA (4,21) ADAM10 ADAM metallopeptidase domain 10 (5) ADAMTS9 ADAM metallopeptidase with thrombospondin type 1 motif, 9 (4) ADCY2 Adenylate cyclase 2 (brain) (26) AJUBA Ajuba LIM protein (21) AKAP9 A kinase (PRKA) anchor protein (yotiao) 9 (4) Akt AKT serine/threonine kinase (28) AKT1 v-akt murine thymoma viral oncogene homolog 1 (5,21,22) AKT2 v-akt murine thymoma viral oncogene homolog 2 (4) ALB Albumin (4) ALK Anaplastic lymphoma receptor tyrosine kinase (22) AMPH Amphiphysin (24) ANK3 Ankyrin 3, node of Ranvier (ankyrin G) (4) ANKRD12 Ankyrin repeat domain 12 (4) ANO1 Anoctamin 1, calcium activated chloride channel (4) APC Adenomatous polyposis coli (4,5,21,22,25,28) APOB Apolipoprotein B [including Ag(x) antigen] (4) AR Androgen receptor (5,21-23) ARAP1 ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1 (4) ARHGAP35 Rho GTPase activating protein 35 (21) ARID1A AT rich interactive domain 1A (SWI-like) (4,5,21,22,24,25,27,28) ARID1B AT rich interactive domain 1B (SWI1-like) (4,5,22) ARID2 AT rich interactive domain 2 (ARID, RFX-like) (4,5,22,24,25,27,28) ARID4A AT rich interactive domain 4A (RBP1-like) (28) ARID5B AT rich interactive domain 5B (MRF1-like) (21) ASPM Asp (abnormal
[Show full text]
Supplementary Table 1. in Vitro Side Effect Profiling Study for LDN/OSU-0212320. Neurotransmitter Related Steroids
Supplementary Table 1. In vitro side effect profiling study for LDN/OSU-0212320. Percent Inhibition Receptor 10 µM Neurotransmitter Related Adenosine, Non-selective 7.29% Adrenergic, Alpha 1, Non-selective 24.98% Adrenergic, Alpha 2, Non-selective 27.18% Adrenergic, Beta, Non-selective -20.94% Dopamine Transporter 8.69% Dopamine, D1 (h) 8.48% Dopamine, D2s (h) 4.06% GABA A, Agonist Site -16.15% GABA A, BDZ, alpha 1 site 12.73% GABA-B 13.60% Glutamate, AMPA Site (Ionotropic) 12.06% Glutamate, Kainate Site (Ionotropic) -1.03% Glutamate, NMDA Agonist Site (Ionotropic) 0.12% Glutamate, NMDA, Glycine (Stry-insens Site) 9.84% (Ionotropic) Glycine, Strychnine-sensitive 0.99% Histamine, H1 -5.54% Histamine, H2 16.54% Histamine, H3 4.80% Melatonin, Non-selective -5.54% Muscarinic, M1 (hr) -1.88% Muscarinic, M2 (h) 0.82% Muscarinic, Non-selective, Central 29.04% Muscarinic, Non-selective, Peripheral 0.29% Nicotinic, Neuronal (-BnTx insensitive) 7.85% Norepinephrine Transporter 2.87% Opioid, Non-selective -0.09% Opioid, Orphanin, ORL1 (h) 11.55% Serotonin Transporter -3.02% Serotonin, Non-selective 26.33% Sigma, Non-Selective 10.19% Steroids Estrogen 11.16% 1 Percent Inhibition Receptor 10 µM Testosterone (cytosolic) (h) 12.50% Ion Channels Calcium Channel, Type L (Dihydropyridine Site) 43.18% Calcium Channel, Type N 4.15% Potassium Channel, ATP-Sensitive -4.05% Potassium Channel, Ca2+ Act., VI 17.80% Potassium Channel, I(Kr) (hERG) (h) -6.44% Sodium, Site 2 -0.39% Second Messengers Nitric Oxide, NOS (Neuronal-Binding) -17.09% Prostaglandins Leukotriene,
[Show full text]
Tie2 and Eph Receptor Tyrosine Kinase Activation and Signaling
Downloaded from http://cshperspectives.cshlp.org/ on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press Tie2 and Eph Receptor Tyrosine Kinase Activation and Signaling William A. Barton1, Annamarie C. Dalton1, Tom C.M. Seegar1, Juha P. Himanen2, and Dimitar B. Nikolov2 1Department of Biochemistry and Molecular Biology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298 2Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065 Correspondence: [email protected] The Eph and Tie cell surface receptors mediate a variety of signaling events during develop- ment and in the adult organism. As other receptor tyrosine kinases, they are activated on binding of extracellular ligands and their catalytic activity is tightly regulated on multiple levels. The Eph and Tie receptors display some unique characteristics, including the require- ment of ligand-induced receptor clustering for efﬁcient signaling. Interestingly, both Ephs and Ties can mediate different, even opposite, biological effects depending on the speciﬁc ligand eliciting the response and on the cellular context. Here we discuss the structural features of these receptors, their interactions with various ligands, as well as functional implications for downstream signaling initiation. The Eph/ephrin structures are already well reviewed and we only provide a brief overview on the initial binding events. We go into more detail discussing the Tie-angiopoietin structures and recognition. ANGIOPOIETINS AND TIE2 In contrast tovasculogenesis, angiogenesis is asculogenesis and angiogenesis are distinct continually required in the adult for wound re- Vcellular processes essential to the creation of pairand remodeling of reproductive tissues dur- the adult vasculature. In early embryonic devel- ing female menstruation.
[Show full text]
Decreased Eph Receptor‑A1 Expression Is Related to Grade in Ovarian Serous Carcinoma
MOLECULAR MEDICINE REPORTS 17: 5409-5415, 2018 Decreased Eph receptor‑A1 expression is related to grade in ovarian serous carcinoma YUNFENG JIN1, YI ZOU1, LINLING WAN1, MINGMING LU1, YA LIU2, GUOQIN HUANG3, JIANDONG WANG4 and QINGHUA XI1 1Department of Obstetrics and Gynecology, Affiliated Hospital of Nantong University, Nantong, Jiangsu 226001; 2Department of Obstetrics and Gynecology, Affiliated Haian People's Hospital of Nantong University, Nantong, Jiangsu 226600; 3Department of Obstetrics and Gynecology, Affiliated Maternal and Child Health Care Hospital of Nantong University, Nantong, Jiangsu 226018; 4Department of Pathology, Jinling Hospital, Nanjing University School of Medicine, Nanjing, Jiangsu 210002, P.R. China Received June 28, 2017; Accepted October 9, 2017 DOI: 10.3892/mmr.2018.8528 Abstract. Eph receptor‑A1 (EphA1) was the first member of 100%) and ovarian benign serous cystadenomas (12/12, 100%) the erythropoietin producing hepatocellular carcinoma (Eph) as well as in some borderline serous tumors (9/15, 60%) and family of receptor tyrosine kinases. Although the roles of ovarian serous carcinomas (33/76, 43.42%). EphA1 expression EphA1 in the tumorigenesis of various human cancers have was associated with grade of ovarian serous carcinomas, with been investigated, few studies have focused on ovarian carci- loss of EphA1 more often observed in high‑grade tumors noma. The present study aimed to explore the profile of EphA1 (P=0.016) and high Ki67 index tumors (P=0.007). These data expression in ovarian carcinomas, to analyzed the association suggest that EphA1 might be a useful marker for distinguishing between EphA1 expression and clinicopathologic parameters, low grade from high‑grade ovarian serous carcinoma.
[Show full text]
EPHA4 Sirna Set I EPHA4 Sirna Set I
Catalog # Aliquot Size E16-911-05 3 x 5 nmol E16-911-20 3 x 20 nmol E16-911-50 3 x 50 nmol EPHA4 siRNA Set I siRNA duplexes targeted against three exon regions Catalog # E16-911 Lot # Z2037-21 Specificity Formulation EPHA4 siRNAs are designed to specifically knock-down The siRNAs are supplied as a lyophilized powder and human EPHA4 expression. shipped at room temperature. Product Description Reconstitution Protocol EPHA4 siRNA is a pool of three individual synthetic siRNA Briefly centrifuge the tubes (maximum RCF 4,000g) to duplexes designed to knock-down human EPHA4 mRNA collect lyophilized siRNA at the bottom of the tube. expression. Each siRNA is 19-25 bases in length. The gene Resuspend the siRNA in 50 µl of DEPC-treated water accession number is NM_004438. (supplied by researcher), which results in a 1x stock solution (10 µM). Gently pipet the solution 3-5 times to mix Gene Aliases and avoid the introduction of bubbles. Optional: aliquot SEK, HEK8, TYRO1 1x stock solutions for storage. Storage and Stability Related Products The lyophilized powder is stable for at least 4 weeks at room temperature. It is recommended that the Product Name Catalog Number lyophilized and resuspended siRNAs are stored at or EPHA1, Active E13-11G below -20oC. After resuspension, siRNA stock solutions ≥2 EPHA1, Active E13-18G µM can undergo up to 50 freeze-thaw cycles without EPHA2, Active E14-11G significant degradation. For long-term storage, it is EPHA3, Active E15-11G recommended that the siRNA is stored at -70oC. For most EPHA4, Active E16-11G favorable performance, avoid repeated handling and EPHA6, Active E18-11G multiple freeze/thaw cycles.
[Show full text]
Original Article a RTK-Based Functional Rnai Screen Reveals Determinants of PTX-3 Expression
Int J Clin Exp Pathol 2013;6(4):660-668 www.ijcep.com /ISSN:1936-2625/IJCEP1301062 Original Article A RTK-based functional RNAi screen reveals determinants of PTX-3 expression Hua Liu*, Xin-Kai Qu*, Fang Yuan, Min Zhang, Wei-Yi Fang Department of Cardiology, Shanghai Chest Hospital affiliated to Shanghai JiaoTong University, Shanghai, China. *These authors contributed equally to this work. Received January 30, 2013; Accepted February 15, 2013; Epub March 15, 2013; Published April 1, 2013 Abstract: Aim: The aim of the present study was to explore the role of receptor tyrosine kinases (RTKs) in the regu- lation of expression of PTX-3, a protector in atherosclerosis. Methods: Human monocytic U937 cells were infected with a shRNA lentiviral vector library targeting human RTKs upon LPS stimuli and PTX-3 expression was determined by ELISA analysis. The involvement of downstream signaling in the regulation of PTX-3 expression was analyzed by both Western blotting and ELISA assay. Results: We found that knocking down of ERBB2/3, EPHA7, FGFR3 and RET impaired PTX-3 expression without effects on cell growth or viability. Moreover, inhibition of AKT, the downstream effector of ERBB2/3, also reduced PTX-3 expression. Furthermore, we showed that FGFR3 inhibition by anti-cancer drugs attenuated p38 activity, in turn induced a reduction of PTX-3 expression. Conclusion: Altogether, our study demonstrates the role of RTKs in the regulation of PTX-3 expression and uncovers a potential cardiotoxicity effect of RTK inhibitor treatments in cancer patients who have symptoms of atherosclerosis or are at the risk of athero- sclerosis.
[Show full text]
The Identification of a Novel Isoform of Epha4 and ITS Expression in SOD1G93A Mice
Accepted Manuscript The Identification of A Novel Isoform of EphA4 and ITS Expression in SOD1G93A Mice Jing Zhao, Andrew W. Boyd, Perry F. Bartlett PII: S0306-4522(17)30051-9 DOI: http://dx.doi.org/10.1016/j.neuroscience.2017.01.038 Reference: NSC 17574 To appear in: Neuroscience Received Date: 16 September 2016 Revised Date: 18 January 2017 Accepted Date: 23 January 2017 Please cite this article as: J. Zhao, A.W. Boyd, P.F. Bartlett, The Identification of A Novel Isoform of EphA4 and ITS Expression in SOD1G93A Mice, Neuroscience (2017), doi: http://dx.doi.org/10.1016/j.neuroscience.2017.01.038 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. THE IDENTIFICATION OF A NOVEL ISOFORM OF EPHA4 AND ITS EXPRESSION IN SOD1G93A MICE JING ZHAOa, ANDREW W. BOYDb,c AND PERRY F. BARTLETTa*. a Queensland Brain Institute, University of Queensland, Qld 4072, Australia b School of Medicine, University of Queensland, Qld 4072, Australia c QIMR Berghofer Medical Research Institute, Qld 4006, Australia *Corresponding author: Prof. Perry Francis Bartlett Queensland Brain Institute The University of Queensland Brisbane, Queensland 4072, Australia E-mail:
[Show full text]
Eph Receptor A4 (EPHA4) Rabbit Polyclonal Antibody Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA890117 Eph receptor A4 (EPHA4) Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: WB Recommended Dilution: WB: 1:500~2000 Reactivity: Human, Mouse, Rat Host: Rabbit Isotype: IgG Clonality: Polyclonal Immunogen: Recombinant protein of human EPHA4 Formulation: PBS with 0.02% sodium azide, 50% glycerol, pH7.3 Concentration: 2.45 mg/ml Purification: Purified from the immunized serum by affinity chromatography (Protein A/G) Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 109.7 kDa Gene Name: EPH receptor A4 Database Link: NP_004429 Entrez Gene 13838 MouseEntrez Gene 316539 RatEntrez Gene 2043 Human P54764 Background: This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2015] Synonyms: HEK8; SEK; TYRO1 This product is to be used for laboratory only. Not for diagnostic or therapeutic use.
[Show full text]
Molecular Pathway Network of EFNA1 in Cancer and Mesenchymal Stem Cells
AIMS Cell and Tissue Engineering, 2(2): 58–77. DOI: 10.3934/celltissue.2018.2.58 Received: 31 January 2018 Accepted: 24 April 2018 Published: 26 April 2018 http://www.aimspress.com/journal/CTE Research article Molecular pathway network of EFNA1 in cancer and mesenchymal stem cells Shihori Tanabe1,*, Kazuhiko Aoyagi2, Hiroshi Yokozaki3 and Hiroki Sasaki4 1 Division of Risk Assessment, Biological Safety Research Center, National Institute of Health Sciences, Kawasaki, Japan 2 Department of Clinical Genomics, National Cancer Center Research Institute, Tokyo, Japan 3 Department of Pathology, Kobe University of Graduate School of Medicine, Kobe, Japan 4 Department of Translational Oncology, National Cancer Center Research Institute, Tokyo, Japan * Correspondence: Email: [email protected]; Phone: +81442706686; Fax: +81442706703. Abstract: Abundant molecules are dynamically activated in cancer and stem cells. To investigate the role of ephrin A1 (EFNA1) in cancer and stem cell signaling pathways, we analyzed the gene expression and molecular network of EFNA1 in mesenchymal stem cells (MSCs) and diffuse-type gastric cancer (GC). Diffuse-type GC has more mesenchymal-like feature and malignant characteristics compared to intestinal-type GC. The signaling and molecular network of EFNA1 in cancer and stem cells were analyzed using several databases, including cBioPortal for Cancer Genomics, Kyoto Encyclopedia of Genes and Genomes (KEGG). The gene expression of EFNA1 was up-regulated in diffuse-type GC compared to MSCs. The molecular pathway network of EFNA1 includes cadherin 1 (CDH1), catenin beta 1 (CTNNB1), ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1) (RAC1), EPH receptor A5 (EPHA5), and the KRAS proto-oncogene, GTPase (KRAS).
[Show full text]
(RTK) Ephb1, Ephb2 and Ephb4 in Colorectal Cancer
The Pattern of Expression of Receptor Tyrosine Kinases (RTK) EphB1, EphB2 and EphB4 in Colorectal Cancer Rashid Saeed Alrahbi Submitted for total fulfilment of the requirements of the degree of Master Department of Surgery North West Academic Centre (NWAC) University of Melbourne 2015 I Abstract Colorectal cancer (CRC) is a global health problem. It is the second leading cause of cancer related death worldwide and in Australia. Around 25% of CRC will experience recurrences postoperatively in the absence of lymph node metastasis and liver metastasis. We need to develop better diagnostic tools and more effective therapeutics. This will come through a thorough understanding of the molecular events in CRC progression. Erythropoietin producing hepatoma (Eph) receptors are the largest family of the receptor tyrosine kinases (RTK). They are divided into two subfamilies, A and B, Together with their cognate ligands, they play integral role in different body organs during embryo development and in adulthood. EphB receptors are considered as key coordinator of proliferation and migration of the intestinal stem cells (ISCs). They are Wnt signalling target genes. They are distributed in a complimentary pattern with their ligands, ephrinB1 and ephrinB2, along the intestinal crypt axis. Adenomatous polyposis coli gene mutation is considered as the initiating step in CRC development. It leads to Wnt signalling mutation and adenoma- carcinoma progression. Despite activation of Wnt signalling pathway, EphB receptors are inactivated during adenoma-carcinoma progression EphB1 and EphB2 receptors function as tumour suppressors in CRC, whereas for the EphB4 some studies found that EphB4 receptor is underexpressed whilst others found it overexpressed with the progression of the disease.
[Show full text]
Investigating the Role of Ephrins and Their Receptors in Mouse Folliculogenesis and Ovulation
Western University Scholarship@Western Electronic Thesis and Dissertation Repository 4-23-2015 12:00 AM Investigating the role of ephrins and their receptors in mouse folliculogenesis and ovulation Adrian Buensuceso The University of Western Ontario Supervisor Dr. Bonnie Deroo The University of Western Ontario Graduate Program in Biochemistry A thesis submitted in partial fulfillment of the equirr ements for the degree in Doctor of Philosophy © Adrian Buensuceso 2015 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Endocrinology Commons Recommended Citation Buensuceso, Adrian, "Investigating the role of ephrins and their receptors in mouse folliculogenesis and ovulation" (2015). Electronic Thesis and Dissertation Repository. 2780. https://ir.lib.uwo.ca/etd/2780 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. INVESTIGATING THE ROLE OF EPHRINS AND THEIR RECEPTORS IN MOUSE FOLLICULOGENESIS AND OVULATION (Thesis format: Integrated-Article) by Adrian Vincent Carlos Buensuceso Graduate Program in Biochemistry A thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy The School of Graduate and Postdoctoral Studies The University of Western Ontario London, Ontario, Canada © Adrian Buensuceso 2015 Abstract Follicle stimulating hormone (FSH) promotes granulosa cell (GC) proliferation, differentiation, and steroidogenesis. This series of events is critical for female fertility, and culminates in the formation of mature follicles responsive to the surge of luteinizing hormone (LH) that triggers ovulation. Ephrins ( Efn genes) and Eph receptors ( Eph genes) are membrane-associated signaling molecules that mediate communication at sites of cell-cell contact, and have been extensively studied in the context of embryonic development.
[Show full text]