SNAP29 Rabbit Pab

Total Page:16

File Type:pdf, Size:1020Kb

SNAP29 Rabbit Pab Leader in Biomolecular Solutions for Life Science SNAP29 Rabbit pAb Catalog No.: A4290 Basic Information Background Catalog No. This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple A4290 membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle Observed MW membrane docking and fusion to the plasma membrane. The protein encoded by this 29kDa gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane- Calculated MW bound, a significant fraction of it is found free in the cytoplasm. Use of multiple 28kDa polyadenylation sites has been noted for this gene. Category Primary antibody Applications WB, IHC, IP Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:1000 - 1:4000 Gene ID Swiss Prot 9342 O95721 IHC 1:50 - 1:200 Immunogen 1:50 - 1:200 IP Recombinant fusion protein containing a sequence corresponding to amino acids 1-258 of human SNAP29 (NP_004773.1). Synonyms SNAP29;CEDNIK;SNAP-29 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 SNAP29 antibody (A4290) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 15s. Immunoprecipitation analysis of 200ug extracts of HepG2 cells using 3ug SNAP29 antibody (A4290). Western blot was performed from the immunoprecipitate using SNAP29 antibody (A4290) at a dilition of 1:1000. Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- embedded human liver damage using embedded rat heart using SNAP29 embedded mouse kidney using SNAP29 SNAP29 antibody (A4290) at dilution of antibody (A4290) at dilution of 1:100 (40x antibody (A4290) at dilution of 1:100 (40x 1:100 (40x lens). lens). lens). Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..
Recommended publications
  • Protein Interaction Network of Alternatively Spliced Isoforms from Brain Links Genetic Risk Factors for Autism
    ARTICLE Received 24 Aug 2013 | Accepted 14 Mar 2014 | Published 11 Apr 2014 DOI: 10.1038/ncomms4650 OPEN Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism Roser Corominas1,*, Xinping Yang2,3,*, Guan Ning Lin1,*, Shuli Kang1,*, Yun Shen2,3, Lila Ghamsari2,3,w, Martin Broly2,3, Maria Rodriguez2,3, Stanley Tam2,3, Shelly A. Trigg2,3,w, Changyu Fan2,3, Song Yi2,3, Murat Tasan4, Irma Lemmens5, Xingyan Kuang6, Nan Zhao6, Dheeraj Malhotra7, Jacob J. Michaelson7,w, Vladimir Vacic8, Michael A. Calderwood2,3, Frederick P. Roth2,3,4, Jan Tavernier5, Steve Horvath9, Kourosh Salehi-Ashtiani2,3,w, Dmitry Korkin6, Jonathan Sebat7, David E. Hill2,3, Tong Hao2,3, Marc Vidal2,3 & Lilia M. Iakoucheva1 Increased risk for autism spectrum disorders (ASD) is attributed to hundreds of genetic loci. The convergence of ASD variants have been investigated using various approaches, including protein interactions extracted from the published literature. However, these datasets are frequently incomplete, carry biases and are limited to interactions of a single splicing isoform, which may not be expressed in the disease-relevant tissue. Here we introduce a new interactome mapping approach by experimentally identifying interactions between brain-expressed alternatively spliced variants of ASD risk factors. The Autism Spliceform Interaction Network reveals that almost half of the detected interactions and about 30% of the newly identified interacting partners represent contribution from splicing variants, emphasizing the importance of isoform networks. Isoform interactions greatly contribute to establishing direct physical connections between proteins from the de novo autism CNVs. Our findings demonstrate the critical role of spliceform networks for translating genetic knowledge into a better understanding of human diseases.
    [Show full text]
  • Autophagy Suppresses Ras-Driven Epithelial Tumourigenesis by Limiting the Accumulation of Reactive Oxygen Species
    OPEN Oncogene (2017) 36, 5576–5592 www.nature.com/onc ORIGINAL ARTICLE Autophagy suppresses Ras-driven epithelial tumourigenesis by limiting the accumulation of reactive oxygen species This article has been corrected since Advance Online Publication and a corrigendum is also printed in this issue. J Manent1,2,3,4,5,12, S Banerjee2,3,4,5, R de Matos Simoes6, T Zoranovic7,13, C Mitsiades6, JM Penninger7, KJ Simpson4,5, PO Humbert3,5,8,9,10 and HE Richardson1,2,5,8,11 Activation of Ras signalling occurs in ~ 30% of human cancers; however, activated Ras alone is not sufficient for tumourigenesis. In a screen for tumour suppressors that cooperate with oncogenic Ras (RasV12)inDrosophila, we identified genes involved in the autophagy pathway. Bioinformatic analysis of human tumours revealed that several core autophagy genes, including GABARAP, correlate with oncogenic KRAS mutations and poor prognosis in human pancreatic cancer, supporting a potential tumour- suppressive effect of the pathway in Ras-driven human cancers. In Drosophila, we demonstrate that blocking autophagy at any step of the pathway enhances RasV12-driven epithelial tissue overgrowth via the accumulation of reactive oxygen species and activation of the Jun kinase stress response pathway. Blocking autophagy in RasV12 clones also results in non-cell-autonomous effects with autophagy, cell proliferation and caspase activation induced in adjacent wild-type cells. Our study has implications for understanding the interplay between perturbations in Ras signalling and autophagy in tumourigenesis,
    [Show full text]
  • On the Move : Endocytic Trafficking in Cell Migration
    Erschienen in: Cellular and Molecular Life Sciences ; 72 (2015), 11. - S. 2119-2134 https://dx.doi.org/10.1007/s00018-015-1855-9 On the move: endocytic trafficking in cell migration Tanja Maritzen • Hannah Schachtner • Daniel F. Legler Abstract Directed cell migration is a fundamental process unraveling the contribution of cellular trafficking pathways underlying diverse physiological and pathophysiological to cell migration. phenomena ranging from wound healing and induction of immune responses to cancer metastasis. Recent advances Keywords Endocytosis Á Cellular motility Á Clathrin Á reveal that endocytic trafficking contributes to cell migration Chemotaxis Á Signal transduction Á Vesicular transport in multiple ways. (1) At the level of chemokines and che- mokine receptors: internalization of chemokines by scavenger receptors is essential for shaping chemotactic Introduction gradients in tissue, whereas endocytosis of chemokine re- ceptors and their subsequent recycling is key for maintaining Diverse physiological processes ranging from embryonic a high responsiveness of migrating cells. (2) At the level of development to the induction of immune responses require integrin trafficking and focal adhesion dynamics: endosomal coordinated cell migration within the organism. In addi- pathways do not only modulate adhesion by delivering in- tion, migratory abilities of cells also represent a tegrins to their site of action, but also by supplying factors determining factor in pathological settings such as metas- for focal adhesion disassembly. (3) At the level of extra- tasis and inflammatory diseases. The term cell migration cellular matrix reorganization: endosomal transport comprises a number of different migration modes with contributes to tumor cell migration not only by targeting different mechanistic requirements.
    [Show full text]
  • WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT (51) International Patent Classification: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, C12Q 1/68 (2018.01) A61P 31/18 (2006.01) DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, C12Q 1/70 (2006.01) HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, (21) International Application Number: MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, PCT/US2018/056167 OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (22) International Filing Date: SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, 16 October 2018 (16. 10.2018) TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (25) Filing Language: English (84) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (26) Publication Language: English GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, (30) Priority Data: UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, 62/573,025 16 October 2017 (16. 10.2017) US TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, ΓΕ , IS, IT, LT, LU, LV, (71) Applicant: MASSACHUSETTS INSTITUTE OF MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TECHNOLOGY [US/US]; 77 Massachusetts Avenue, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, Cambridge, Massachusetts 02139 (US).
    [Show full text]
  • Human Gene Copy Number Spectra Analysis in Congenital Heart Malformations Aoy Tomita-Mitchell Medical College of Wisconsin
    CORE Metadata, citation and similar papers at core.ac.uk Provided by epublications@Marquette Marquette University e-Publications@Marquette Mathematics, Statistics and Computer Science Mathematics, Statistics and Computer Science, Faculty Research and Publications Department of 5-1-2012 Human gene copy number spectra analysis in congenital heart malformations Aoy Tomita-Mitchell Medical College of Wisconsin Donna K. Mahnke Medical College of Wisconsin Craig Struble Marquette University, [email protected] Maureen E. Tuffnell Marquette University Karl D. Stamm Marquette University See next page for additional authors Accepted version. Physiological Genomics, Vol. 44, No. 9 (May 2012): 518-541. DOI. © 2012 The American Physiological Society. Used with permission. Authors Aoy Tomita-Mitchell, Donna K. Mahnke, Craig Struble, Maureen E. Tuffnell, Karl D. Stamm, Mats Hidestrand, Susan Harris, Mary A. Goetsch, Pippa Simpson, David P. Bick, Ulrich Broeckel, Andrew N. Pelech, James S. Tweddell, and Michael Mitchell This article is available at e-Publications@Marquette: https://epublications.marquette.edu/mscs_fac/272 NOT THE PUBLISHED VERSION; this is the author’s final, peer-reviewed manuscript. The published version may be accessed by following the link in the citation at the bottom of the page. Human Gene Copy Number Spectra Analysis in Congenital Heart Malformations Aoy Tomita-Mitchell Department of Surgery, Division of Cardiothoracic Surgery; Biotechnology and Bioengineering Center; Human and Molecular Genetics Center; Medical College of Wisconsin; Milwaukee, WI Donna K. Mahnke Department of Surgery, Division of Cardiothoracic Surgery; Biotechnology and Bioengineering Center; Human and Molecular Genetics Center; Medical College of Wisconsin; Milwaukee, WI Craig A. Struble Department of Mathematics, Statistics and Computer Science; Marquette University; Milwaukee, WI Maureen E.
    [Show full text]
  • Supplementary Table 3: Genes Only Influenced By
    Supplementary Table 3: Genes only influenced by X10 Illumina ID Gene ID Entrez Gene Name Fold change compared to vehicle 1810058M03RIK -1.104 2210008F06RIK 1.090 2310005E10RIK -1.175 2610016F04RIK 1.081 2610029K11RIK 1.130 381484 Gm5150 predicted gene 5150 -1.230 4833425P12RIK -1.127 4933412E12RIK -1.333 6030458P06RIK -1.131 6430550H21RIK 1.073 6530401D06RIK 1.229 9030607L17RIK -1.122 A330043C08RIK 1.113 A330043L12 1.054 A530092L01RIK -1.069 A630054D14 1.072 A630097D09RIK -1.102 AA409316 FAM83H family with sequence similarity 83, member H 1.142 AAAS AAAS achalasia, adrenocortical insufficiency, alacrimia 1.144 ACADL ACADL acyl-CoA dehydrogenase, long chain -1.135 ACOT1 ACOT1 acyl-CoA thioesterase 1 -1.191 ADAMTSL5 ADAMTSL5 ADAMTS-like 5 1.210 AFG3L2 AFG3L2 AFG3 ATPase family gene 3-like 2 (S. cerevisiae) 1.212 AI256775 RFESD Rieske (Fe-S) domain containing 1.134 Lipo1 (includes AI747699 others) lipase, member O2 -1.083 AKAP8L AKAP8L A kinase (PRKA) anchor protein 8-like -1.263 AKR7A5 -1.225 AMBP AMBP alpha-1-microglobulin/bikunin precursor 1.074 ANAPC2 ANAPC2 anaphase promoting complex subunit 2 -1.134 ANKRD1 ANKRD1 ankyrin repeat domain 1 (cardiac muscle) 1.314 APOA1 APOA1 apolipoprotein A-I -1.086 ARHGAP26 ARHGAP26 Rho GTPase activating protein 26 -1.083 ARL5A ARL5A ADP-ribosylation factor-like 5A -1.212 ARMC3 ARMC3 armadillo repeat containing 3 -1.077 ARPC5 ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa -1.190 activating transcription factor 4 (tax-responsive enhancer element ATF4 ATF4 B67) 1.481 AU014645 NCBP1 nuclear cap
    [Show full text]
  • CORVET, CHEVI and HOPS – Multisubunit Tethers of the Endo
    © 2019. Published by The Company of Biologists Ltd | Journal of Cell Science (2019) 132, jcs189134. doi:10.1242/jcs.189134 REVIEW SUBJECT COLLECTION: CELL BIOLOGY AND DISEASE CORVET, CHEVI and HOPS – multisubunit tethers of the endo-lysosomal system in health and disease Jan van der Beek‡, Caspar Jonker*,‡, Reini van der Welle, Nalan Liv and Judith Klumperman§ ABSTRACT contact between two opposing membranes and pull them close Multisubunit tethering complexes (MTCs) are multitasking hubs that together to allow interactions between SNARE proteins (Murray form a link between membrane fusion, organelle motility and signaling. et al., 2016). SNARE assembly then provides additional fusion CORVET, CHEVI and HOPS are MTCs of the endo-lysosomal system. specificity and drives the actual fusion process (Ohya et al., 2009; They regulate the major membrane flows required for endocytosis, Stroupe et al., 2009). In this Review, we focus on the role of tethering lysosome biogenesis, autophagy and phagocytosis. In addition, proteins in endo-lysosomal fusion events. individual subunits control complex-independent transport of specific Tethering proteins can be divided into two main groups: long cargoes and exert functions beyond tethering, such as attachment to coiled-coil proteins (Gillingham and Munro, 2003) and microtubules and SNARE activation. Mutations in CHEVI subunits multisubunit tethering complexes (MTCs). MTCs form a lead to arthrogryposis, renal dysfunction and cholestasis (ARC) heterogenic group of protein complexes that consist of up to ten ∼ syndrome, while defects in CORVET and, particularly, HOPS are subunits resulting in a general length of 50 nm (Brocker et al., associated with neurodegeneration, pigmentation disorders, liver 2012; Chou et al., 2016; Hsu et al., 1998; Lürick et al., 2018; Ren malfunction and various forms of cancer.
    [Show full text]
  • Multiple Functions of the SNARE Protein Snap29 in Autophagy, Endocytic, and Exocytic Trafficking During Epithelial Formation in Drosophila
    BASIC RESEARCH PAPER Autophagy 10:12, 2251--2268; December 2014; Published with license by Taylor & Francis Multiple functions of the SNARE protein Snap29 in autophagy, endocytic, and exocytic trafficking during epithelial formation in Drosophila Elena Morelli,1 Pierpaolo Ginefra,1 Valeria Mastrodonato,1 Galina V Beznoussenko,1 Tor Erik Rusten,2 David Bilder,3 Harald Stenmark,2 Alexandre A Mironov,1 and Thomas Vaccari1,* 1IFOM - The FIRC Institute of Molecular Oncology; Milan, Italy; 2Centre for Cancer Biomedicine; Oslo University Hospital; Oslo, Norway; 3Department of Molecular and Cell Biology; University of California; Berkeley, CA USA Keywords: autophagy, dome, Notch, Snap29, SNARE, trafficking, usnp Abbreviations: Atg, autophagy-related; CEDNIK, cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma; CFP, cyan fluorescent protein; dome, domeless; EM, electron microscopy; ESCRT, endosomal sorting complex required for transport; E(spl)mb-HLH, enhancer of split mb, helix-loop-helix; FE, follicular epithelium; histone H3, His3; hop-Stat92E, hopscotch-signal transducer and activator of transcription protein at 92E; GFP, green fluorescent protein; MENE, mutant eye no eclosion; MVB, multivesicular body; N, Notch; NECD, N extracellular domain; NPF, asparagine-proline-phenylalanine; os, outstretched; ref(2)P, refractory to sigma P; Snap29, synaptosomal-associated protein 29 kDa; SNARE, soluble NSF attachment protein receptor; Socs36E, suppressor of cytokine signaling at 36E; Syb, Synaptobrevin; Syx, syntaxin; Vamp, vesicle-associated membrane protein; C V-ATPase, vacuolar H -ATPase; Vps25, vacuolar protein sorting 25; WT, wild type. How autophagic degradation is linked to endosomal trafficking routes is little known. Here we screened a collection of uncharacterized Drosophila mutants affecting membrane transport to identify new genes that also have a role in autophagy.
    [Show full text]
  • MT1-MMP Recruits the ER-Golgi SNARE Bet1 for Efficient MT1-MMP Transport to the Plasma Membrane
    ARTICLE MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane Takuya Miyagawa1*, Kana Hasegawa1*, Yoko Aoki1*, Takuya Watanabe1*, Yuka Otagiri1, Kohei Arasaki1, Yuichi Wakana1, Kenichi Asano1, Masato Tanaka1, Hideki Yamaguchi2, Mitsuo Tagaya1,andHirokiInoue1 Metastasis is a major cause of cancer-related death. Membrane type 1–matrix metalloproteinase (MT1-MMP) is a critical protease for local invasion and metastasis. MT1-MMP is synthesized in the endoplasmic reticulum (ER) and transported in vesicles to invadopodia, specialized subdomains of the plasma membrane, through secretory and endocytic recycling pathways. The molecular mechanism underlying intracellular transport of MT1-MMP has been extensively studied, but is not fully understood. We show that MT1-MMP diverts the SNARE Bet1 from its function in ER-Golgi transport, to promote MT1- MMP trafficking to the cell surface, likely to invadopodia. In invasive cells, Bet1 is localized in MT1-MMP–positive endosomes in addition to the Golgi apparatus, and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs. MT1-MMP may also use Bet1 for its export from raft-like structures in the ER. Our results suggest the recruitment of Bet1 at an early stage after MT1-MMP expression promotes the exit of MT1-MMP from the ER and its efficient transport to invadopodia. Introduction Metastasis, which includes many complex processes such as are delivered to invadopodia via trafficking vesicles and/or tubu- invasion and dissemination to distant tissues, is a major cause lovesicular transport carriers for their maturation (Schoumacher of cancer-related death (Chaffer and Weinberg, 2011). Inva- et al., 2010; Jacob et al., 2013; Marchesin et al., 2015).
    [Show full text]
  • Loss of Function Mutation of Mouse Snap29 on a Mixed Genetic Background Phenocopy 2 Abnormalities Found in CEDNIK and 22Q11.2 Deletion Syndrome Patients
    bioRxiv preprint doi: https://doi.org/10.1101/559088; this version posted February 24, 2019. 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. 1 1 Loss of function mutation of mouse Snap29 on a mixed genetic background phenocopy 2 abnormalities found in CEDNIK and 22q11.2 Deletion Syndrome patients 3 Vafa Keser1, Jean-François Boisclair Lachance1, Sabrina Shameen Alam1, Youngshin Lim5, 4 Eleonora Scarlata2, Apinder Kaur1, Zhang Tian Fang3, Shasha Lv3, Pierre Lachapelle,3, Cristian 5 O’Flaherty2,4, Jefferey A. Golden5, Loydie A. Jerome-Majewska1,6,7 6 1. Department of Human Genetics, McGill University, Montreal, Quebec, Canada. 7 2. Department of Surgery (Urology Division), McGill University, Montreal, Quebec, Canada 8 3. Department of Ophthalmology & Visual Sciences, McGill University Health Centre at Glen 9 Site, Montreal, Quebec, Canada 10 4. Department of Pharmacology and Therapeutics, McGill University, Montreal, Quebec, 11 5. Department of Pathology, Brigham and Women’s Hospital, Harvard Medical School, Boston, 12 Massachusetts, United States of America 13 6. Department of Anatomy and Cell Biology, McGill University Health Centre at Glen Site, 14 Montreal, Quebec, Canada 15 7. Department of Pediatrics, McGill University, Montreal, Quebec, Canada 16 17 18 19 Abstract 20 Synaptosomal-associated protein 29 (SNAP29) is a member of the SNARE family of proteins 21 involved in maintenance of various intracellular protein trafficking pathways. SNAP29 maps to 22 the 22q11.2 region and is deleted in 90% of patients with 22q11.2 deletion syndrome 23 (22q11.2DS). However, the contribution of hemizygosity of SNAP29 to developmental 24 abnormalities in 22q11.2DS remains to be determined.
    [Show full text]
  • A Novel Function for SNAP29 (Synaptosomal-Associated Protein of 29 Kda) in Mast Cell Phagocytosis
    Thomas Jefferson University Jefferson Digital Commons Department of Microbiology and Immunology Faculty Papers Department of Microbiology and Immunology 1-1-2012 A Novel Function for SNAP29 (Synaptosomal-Associated Protein of 29 kDa) in Mast Cell Phagocytosis. Jordan Wesolowski Thomas Jefferson University Vernon Caldwell Thomas Jefferson University Fabienne Paumet Thomas Jefferson University Follow this and additional works at: https://jdc.jefferson.edu/mifp Part of the Medical Immunology Commons, and the Medical Microbiology Commons Let us know how access to this document benefits ouy Recommended Citation Wesolowski, Jordan; Caldwell, Vernon; and Paumet, Fabienne, "A Novel Function for SNAP29 (Synaptosomal-Associated Protein of 29 kDa) in Mast Cell Phagocytosis." (2012). Department of Microbiology and Immunology Faculty Papers. Paper 31. https://jdc.jefferson.edu/mifp/31 This Article is brought to you for free and open access by the Jefferson Digital Commons. The Jefferson Digital Commons is a service of Thomas Jefferson University's Center for Teaching and Learning (CTL). The Commons is a showcase for Jefferson books and journals, peer-reviewed scholarly publications, unique historical collections from the University archives, and teaching tools. The Jefferson Digital Commons allows researchers and interested readers anywhere in the world to learn about and keep up to date with Jefferson scholarship. This article has been accepted for inclusion in Department of Microbiology and Immunology Faculty Papers by an authorized administrator of the Jefferson Digital Commons. For more information, please contact: [email protected]. A Novel Function for SNAP29 (Synaptosomal-Associated Protein of 29 kDa) in Mast Cell Phagocytosis Jordan Wesolowski, Vernon Caldwell, Fabienne Paumet* Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania, United States of America Abstract Mast cells play a critical role in the innate immune response to bacterial infection.
    [Show full text]
  • 207787 Karampini New Suppl
    Hemostasis SUPPLEMENTARY APPENDIX Defective AP-3-dependent VAMP8 trafficking impairs Weibel-Palade body exocytosis in Hermansky-Pudlak Syndrome type 2 blood outgrowth endothelial cells Ellie Karampini,1,* Maaike Schillemans,1,* Menno Hofman,1 Floris van Alphen,2 Martin de Boer,3 Taco W. Kuijpers,3,4 Maartje van den Biggelaar,1 Jan Voorberg1,5 and Ruben Bierings1,6 1Molecular and Cellular Hemostasis, Sanquin Research and Landsteiner Laboratory, Amsterdam UMC, University of Amsterdam, Amster- dam; 2Research Facilities, Sanquin Research and Landsteiner Laboratory, Amsterdam UMC, University of Amsterdam, Amsterdam; 3Blood Cell Research, Sanquin Research and Landsteiner Laboratory, Amsterdam UMC, University of Amsterdam, Amsterdam; 4Pediatric Hema- tology, Immunology and Infectious Disease, Amsterdam UMC, University of Amsterdam, Amsterdam; 5Experimental Vascular Medicine, Amsterdam UMC, University of Amsterdam, Amsterdam and 6Hematology, Erasmus University Medical Center, Rotterdam, the Netherlands *EK and MS contributed equally to this work. ©2019 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol.2018.207787 Received: October 7, 2018. Accepted: January 9, 2019. Pre-published: January 10, 2019. Correspondence: RUBEN BIERINGS - [email protected] Supplementary Figure 1 Supplementary Figure 1: P-selectin (CD62P) and CD63 trafficking in HPS-2 BOECs. (A) WT and HPS-2 BOECs were immunostained for vWF (magenta) and CD62P (cyan). Boxed regions are magnified on the right. The yellow arrowheads show WPB in both channels. In both WT and HPS-2 BOEC WPBs are positive for CD62P. (B) Flow cytometric analysis of CD63 membrane expression under steady state conditions in WT and HPS-2 BOECs. (Bi) Representative histogram plot of WT and HPS-2 BOEC stained with mouse anti-CD63 (Bii) Quantification of 6 independent experiments.
    [Show full text]