Atypical Solute Carriers
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Unc93b Antibody (Pab)
21.10.2014Unc93b antibody (pAb) Rabbit Anti -Human/Mouse/Rat Unc93b Instruction Manual Catalog Number PK-AB718-4553 Synonyms Unc93b Antibody: Unc93b1, homolog of C. elegans Unc93 Description The endoplasmic reticulum (ER) protein Unc93b, a human homolog of the C. elegans Unc93 gene, was initially identified by a forward genetic screen using N-ethyl-N-nitrosourea where a histidine- to-arginine substitution in Unc93b caused defects in Toll-like receptor (TLR) 3, 7 and 9 signaling. Unlike Unc93a, another homolog of the C. elegans Unc93 gene whose function is unknown, Unc93b specifically interacts with TLR3, 7 and 9; the histidine-to-arginine point mutation used to identify Unc93b abolishes this interaction. Mice carrying this point mutation are highly susceptible to infection with a number of viruses, indicating that Unc93b plays an important role in innate immunity. Multiple isoforms of Unc93a are known to exist. This antibody will not cross-react with Unc93a. Quantity 100 µg Source / Host Rabbit Immunogen Unc93b antibody was raised in rabbits against a 19 amino acid peptide from near the amino terminus of human Unc93b. Purification Method Affinity chromatography purified via peptide column. Clone / IgG Subtype Polyclonal antibody Species Reactivity Human, Mouse, Rat Specificity Multiple isoforms of Unc93a are known to exist. This antibody will not cross-react with Unc93a. Formulation Antibody is supplied in PBS containing 0.02% sodium azide. Reconstitution During shipment, small volumes of antibody will occasionally become entrapped in the seal of the product vial. For products with volumes of 200 μl or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap. -
History of Cln7 Biology of Cln7 Symptoms Diagnosis Management Strategies
Understanding CLN7 HISTORY OF CLN7 BIOLOGY OF CLN7 SYMPTOMS DIAGNOSIS MANAGEMENT STRATEGIES Understanding CLN7 Batten disease is a group of rare neurodegenerative diseases, also known as neuronal ceroid lipofuscinoses (NCLs). Each NCL disease is classified by the gene that causes it. The name of each gene begins with CLN – ceroid lipofuscinosis, neuronal – followed by a unique number that indicates the subtype. Changes in the normal function of these genes, due to pathogenic variants, lead to disruption of normal protein function. This disruption results in lysosomal dysfunction, and the accumulation of molecules in the cells throughout the body. The symptoms, severity, onset, and progression across the subtypes vary. Both males and females are affected. The CLN7 subtype of Batten disease is caused by a variant in the CLN7 gene, also called the MFSD8 gene, which leads to disruption of normal CLN7 protein function. The exact function of this protein is unknown. Individuals with CLN7 typically develop neurological signs and symptoms in early childhood, such as seizures, progressive deterioration in intellectual and motor capabilities, and loss of vision. The disease ultimately leads to a shortened lifespan. Source: Batten Disease Fact Sheet. (2019, June 24). Retrieved August 8, 2019, from link. History of CLN7 History of Batten Disease Batten disease, a common name for a rare class of diseases called neuronal ceroid lipofuscinoses (NCLs), was first described in 1903 by British neurologist and pediatrician Frederick Batten. Today, there are 13 known subtypes of Batten disease. Symptoms and disease management for each subtype of Batten disease vary, although several subtypes share similar features and symptoms. -
SPNS2 Antibody (N-Term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap17856a
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 SPNS2 Antibody (N-term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP17856a Specification SPNS2 Antibody (N-term) - Product Information Application WB, IHC-P, FC,E Primary Accession Q8IVW8 Other Accession NP_001118230.1 Reactivity Human Host Rabbit Clonality Polyclonal Isotype Rabbit IgG Antigen Region 68-94 SPNS2 Antibody (N-term) - Additional Information Gene ID 124976 Other Names Protein spinster homolog 2, SPNS2 All lanes : Anti-SPNS2 Antibody (N-term) at Target/Specificity 1:1000 dilution Lane 1: human brain tissue This SPNS2 antibody is generated from lysate Lane 2: 293 whole cell lysate Lane 3: rabbits immunized with a KLH conjugated SK-BR-3 whole cell lysate Lysates/proteins at synthetic peptide between 68-94 amino 20 µg per lane. Secondary Goat Anti-Rabbit acids from the N-terminal region of human IgG, (H+L), Peroxidase conjugated at 1/10000 SPNS2. dilution. Predicted band size : 58 kDa Blocking/Dilution buffer: 5% NFDM/TBST. Dilution WB~~1:1000 IHC-P~~1:100 FC~~1:25 Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. Storage Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. Precautions SPNS2 Antibody (N-term) is for research use All lanes : Anti-SPNS2 Antibody (N-term) at only and not for use in diagnostic or 1:1000 dilution Lane 1: Human heart lysate therapeutic procedures. -
CLN7 Disease
CLN7 disease Description CLN7 disease is an inherited disorder that primarily affects the nervous system. The signs and symptoms of this condition typically begin between ages 2 and 7. The initial features are usually vision loss and problems with movement that might seem like clumsiness. Additional signs and symptoms of CLN7 disease include muscle twitches ( myoclonus), difficulty coordinating movements (ataxia), recurrent seizures (epilepsy), and speech impairment. Mental functioning and motor skills (such as sitting and walking) decline with age. Individuals with CLN7 disease typically do not survive past their teens. CLN7 disease is one of a group of disorders known as neuronal ceroid lipofuscinoses ( NCLs), which may also be collectively referred to as Batten disease. All these disorders affect the nervous system and typically cause worsening problems with vision, movement, and thinking ability. The different NCLs are distinguished by their genetic cause. Each disease type is given the designation "CLN," meaning ceroid lipofuscinosis, neuronal, and then a number to indicate its subtype. Frequency The incidence of CLN7 disease is unknown; more than 70 cases have been described in the scientific literature. CLN7 disease was first diagnosed in the Turkish population and was thought to be limited to individuals in that group. However, CLN7 disease has now been identified in people around the world. Collectively, all forms of NCL affect an estimated 1 in 100,000 individuals worldwide. Causes Mutations in the MFSD8 gene cause CLN7 disease. The MFSD8 gene provides instructions for making a protein whose function is unknown. The MFSD8 protein is embedded in the membrane of cell compartments called lysosomes, which digest and recycle different types of molecules. -
Cellular Transport Notes About Cell Membranes
Cellular Transport Notes @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey About Cell Membranes • All cells have a cell membrane • Functions: – Controls what enters and exits the cell to maintain an internal balance called homeostasis TEM picture of a – Provides protection and real cell membrane. support for the cell @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey 1 About Cell Membranes (continued) 1.Structure of cell membrane Lipid Bilayer -2 layers of phospholipids • Phosphate head is polar (water loving) Phospholipid • Fatty acid tails non-polar (water fearing) • Proteins embedded in membrane Lipid Bilayer @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey Polar heads Fluid Mosaic love water Model of the & dissolve. cell membrane Non-polar tails hide from water. Carbohydrate cell markers Proteins @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey 2 About Cell Membranes (continued) • 4. Cell membranes have pores (holes) in it • Selectively permeable: Allows some molecules in and keeps other molecules out • The structure helps it be selective! Pores @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey Structure of the Cell Membrane Outside of cell Carbohydrate Proteins chains Lipid Bilayer Transport Protein Phospholipids Inside of cell (cytoplasm) @ 2011 Center for Pre-College Programs, New Jersey Institute of Technology, Newark, New Jersey 3 Types of Cellular Transport • Passive Transport celldoesn’tuseenergy 1. Diffusion 2. Facilitated Diffusion 3. Osmosis • Active Transport cell does use energy 1. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
The Novel Membrane-Bound Proteins MFSD1 and MFSD3 Are Putative SLC Transporters Affected by Altered Nutrient Intake
J Mol Neurosci DOI 10.1007/s12031-016-0867-8 The Novel Membrane-Bound Proteins MFSD1 and MFSD3 are Putative SLC Transporters Affected by Altered Nutrient Intake Emelie Perland1,2 & Sofie V. Hellsten2 & Emilia Lekholm2 & Mikaela M. Eriksson2 & Vasiliki Arapi2 & Robert Fredriksson2 Received: 29 August 2016 /Accepted: 21 November 2016 # The Author(s) 2016. This article is published with open access at Springerlink.com Abstract Membrane-bound solute carriers (SLCs) are essen- Introduction tial as they maintain several physiological functions, such as nutrient uptake, ion transport and waste removal. The SLC Membrane-bound transporters are physiologically important family comprise about 400 transporters, and we have identi- as they keep the homeostasis of soluble molecules within cel- fied two new putative family members, major facilitator su- lular compartments, and it is crucial to study their basic his- perfamily domain containing 1 (MFSD1) and 3 (MFSD3). tology and function to understand the human body. The solute They cluster phylogenetically with SLCs of MFS type, and carrier (SLC) superfamily is the largest group of membrane- both proteins are conserved in chordates, while MFSD1 is also bound transporters in human and it includes 395 members, found in fruit fly. Based on homology modelling, we predict divided in 52 families (Hediger et al. 2004). SLCs utilize 12 transmembrane regions, a common feature for MFS trans- ATP-independent mechanisms to move nutrients, ions, drugs porters. The genes are expressed in abundance in mice, with and waste over lipid membranes, and SLC deficiencies are specific protein staining along the plasma membrane in neu- associated with several human diseases (Hediger et al. -
Function in Immune System Spns2 Transporter the Role of Sphingosine-1-Phosphate
The Journal of Immunology The Role of Sphingosine-1-Phosphate Transporter Spns2 in Immune System Function Anastasia Nijnik,*,† Simon Clare,* Christine Hale,* Jing Chen,* Claire Raisen,* Lynda Mottram,* Mark Lucas,* Jeanne Estabel,* Edward Ryder,* Hibret Adissu,‡ Sanger Mouse Genetics Project,1 Niels C. Adams,* Ramiro Ramirez-Solis,* Jacqueline K. White,* Karen P. Steel,* Gordon Dougan,* and Robert E. W. Hancock† Sphingosine-1-phosphate (S1P) is lipid messenger involved in the regulation of embryonic development, immune system functions, and many other physiological processes. However, the mechanisms of S1P transport across cellular membranes remain poorly understood, with several ATP-binding cassette family members and the spinster 2 (Spns2) member of the major facilitator superfamily known to mediate S1P transport in cell culture. Spns2 was also shown to control S1P activities in zebrafish in vivo and to play a critical role in zebrafish cardiovascular development. However, the in vivo roles of Spns2 in mammals and its involvement in the different S1P-dependent physiological processes have not been investigated. In this study, we charac- terized Spns2-null mouse line carrying the Spns2tm1a(KOMP)Wtsi allele (Spns2tm1a). The Spns2tm1a/tm1a animals were viable, indi- cating a divergence in Spns2 function from its zebrafish ortholog. However, the immunological phenotype of the Spns2tm1a/tm1a mice closely mimicked the phenotypes of partial S1P deficiency and impaired S1P-dependent lymphocyte trafficking, with a depletion of lymphocytes in circulation, an increase in mature single-positive T cells in the thymus, and a selective reduction in mature B cells in the spleen and bone marrow. Spns2 activity in the nonhematopoietic cells was critical for normal lymphocyte development and localization. -
Variants Affecting the C-Terminal Tail of UNC93B1 Are Not a Common Risk Factor for Systemic Lupus Erythematosus
G C A T T A C G G C A T genes Article Variants Affecting the C-Terminal Tail of UNC93B1 Are Not a Common Risk Factor for Systemic Lupus Erythematosus Sarah Kiener 1,2 , Camillo Ribi 3 , Irene Keller 4, Carlo Chizzolini 5 , Marten Trendelenburg 6, Uyen Huynh-Do 7 , Johannes von Kempis 8, on behalf of Swiss SLE Cohort Study (SSCS) † and Tosso Leeb 1,2,* 1 Institute of Genetics, Vetsuisse Faculty, University of Bern, 3012 Bern, Switzerland; [email protected] 2 Dermfocus, University of Bern, 3001 Bern, Switzerland 3 Division of Immunology and Allergy, Department of Medicine, Lausanne University Hospital (CHUV) and University of Lausanne (UNIL), 1011 Lausanne, Switzerland; [email protected] 4 Interfaculty Bioinformatics Unit, University of Bern, 3012 Bern, Switzerland; [email protected] 5 Department of Pathology and Immunology, School of Medicine, Geneva University, 1211 Geneva, Switzerland; [email protected] 6 Laboratory for Clinical Immunology, Department of Biomedicine and Division of Internal Medicine, University Hospital of Basel, 4031 Basel, Switzerland; [email protected] 7 Division of Nephrology and Hypertension, Inselspital, Bern University Hospital, 3010 Bern, Switzerland; [email protected] 8 Division of Rheumatology, Cantonal Hospital St. Gallen, 9007 St. Gallen, Switzerland; [email protected] * Correspondence: [email protected]; Tel.: +41-31-684-2326 † Association of the Swiss SLE Cohort Study (ASSCS), 4031 Basel, Switzerland. Citation: Kiener, S.; Ribi, C.; Keller, I.; Abstract: Systemic lupus erythematosus (SLE) is a heterogeneous multifactorial disease. Upregulated Chizzolini, C.; Trendelenburg, M.; TLR7 signaling is a known risk factor for SLE. -
Phospho-SGK Pser422 Antibody
Lot Number: RD2191861I Phospho-SGK pSer422 Antibody Product Data Sheet Tested Species Reactivity Details Human (Hu) Catalog Number: PA5-35427 Mouse (Ms) Size: 100 µl Rat (Rt) Class: Polyclonal Type: Antibody Tested Applications Dilution * Clone: Western Blot (WB) 1:500-1:2000 Host / Isotype: Rabbit / IgG * Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own A synthesized peptide derived from experiment using appropriate negative and positive controls. Immunogen: human SGK around the phosphorylation site of Serine 422 Form Information Form: Liquid Concentration: Lot Specific Purification: Antigen affinity chromatography Storage Buffer: PBS, pH 7.5, with 50% glycerol Preservative: 0.02% sodium azide Storage Conditions: -20° C, Avoid Freeze/Thaw Cycles Product Specific Information General Information Concentration is lot-specific and will vary from 0.5-0.6 mg/ml Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, For Research Use Only. Not for use in diagnostic procedures. Not for transcription factors, neuronal excitability, cell growth, proliferation, resale without express authorization. survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity -
Phosphorylation of Synaptic Vesicle Protein 2A at Thr84 by Casein Kinase 1 Family Kinases Controls the Specific Retrieval of Synaptotagmin-1
2492 • The Journal of Neuroscience, February 11, 2015 • 35(6):2492–2507 Cellular/Molecular Phosphorylation of Synaptic Vesicle Protein 2A at Thr84 by Casein Kinase 1 Family Kinases Controls the Specific Retrieval of Synaptotagmin-1 Ning Zhang,1* X Sarah L. Gordon,2* XMaximilian J. Fritsch,1* Noor Esoof,1* XDavid G. Campbell,1 Robert Gourlay,1 Srikannathasan Velupillai,1 XThomas Macartney,1 XMark Peggie,1 Daan M.F. van Aalten,1 Michael A. Cousin,2* and Dario R. Alessi1* 1Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom, and 2Centre for Integrative Physiology, University of Edinburgh, Edinburgh EH8 9XD, Scotland, United Kingdom Synapticvesicleprotein2A(SV2A)isaubiquitouscomponentofsynapticvesicles(SVs).IthasrolesinbothSVtraffickingandneurotransmitter release. We demonstrate that Casein kinase 1 family members, including isoforms of Tau–tubulin protein kinases (TTBK1 and TTBK2), phos- phorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1. We show by crystallographic and other analyses that the phosphorylated Thr84 residue binds to a pocket formed by three conserved Lys residues (Lys314, Lys326, and Lys328) on the surface of the synaptotagmin-1 C2B domain. Finally, we observed dysfunctionalsynaptotagmin-1retrievalduringSVendocytosisbyablatingitsphospho-dependentinteractionwithSV2A,knockdownofSV2A, or rescue with a phosphorylation-null Thr84 SV2A mutant in primary cultures of mouse neurons. This study reveals fundamental details of how phosphorylation of Thr84 on SV2A controls its interaction with synaptotagmin-1 and implicates SV2A as a phospho-dependent chaperone required for the specific retrieval of synaptotagmin-1 during SV endocytosis. -
Hollow Fiber Membrane Contactors for Post-Combustion Carbon Capture: a Review of Modeling Approaches
membranes Review Hollow Fiber Membrane Contactors for Post-Combustion Carbon Capture: A Review of Modeling Approaches Joanna R. Rivero 1 , Grigorios Panagakos 2,∗ , Austin Lieber 1 and Katherine Hornbostel 1 1 Department of Mechanical Engineering and Material Science, University of Pittsburgh, 3700 O’Hara St, Pittsburgh, PA 15213, USA; [email protected] (J.R.R.); [email protected] (A.L.); [email protected] (K.H.) 2 Department of Chemical Engineering, Carnegie Mellon University, 5000 Forbes Ave, Pittsburgh, PA 15213, USA * Correspondence: [email protected] Received: 30 October 2020; Accepted: 25 November 2020; Published: 30 November 2020 Abstract: Hollow fiber membrane contactors (HFMCs) can effectively separate CO2 from post-combustion flue gas by providing a high contact surface area between the flue gas and a liquid solvent. Accurate models of carbon capture HFMCs are necessary to understand the underlying transport processes and optimize HFMC designs. There are various methods for modeling HFMCs in 1D, 2D, or 3D. These methods include (but are not limited to): resistance-in-series, solution-diffusion, pore flow, Happel’s free surface model, and porous media modeling. This review paper discusses the state-of-the-art methods for modeling carbon capture HFMCs in 1D, 2D, and 3D. State-of-the-art 1D, 2D, and 3D carbon capture HFMC models are then compared in depth, based on their underlying assumptions. Numerical methods are also discussed, along with modeling to scale up HFMCs from the lab scale to the commercial scale. Keywords: hollow fiber membrane contactor modeling; post-combustion carbon capture; carbon capture membrane modeling 1. Introduction In 2018, the Intergovernmental Panel on Climate Change issued a report detailing the irreversible impact of a global temperature rise of 1.5 ◦C[1].