Anti-CD29 / Integrin Beta 1 Antibody [12G10] (ARG22982)
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PAPC Couples the Segmentation Clock to Somite Morphogenesis by Regulating N-Cadherin-Dependent Adhesion
© 2017. Published by The Company of Biologists Ltd | Development (2017) 144, 664-676 doi:10.1242/dev.143974 RESEARCH ARTICLE PAPC couples the segmentation clock to somite morphogenesis by regulating N-cadherin-dependent adhesion Jérome Chal1,2,3,4,5,*, Charlenè Guillot3,4,* and Olivier Pourquié1,2,3,4,5,6,7,‡ ABSTRACT specific level of the PSM called the determination front. The Vertebrate segmentation is characterized by the periodic formation of determination front is defined as a signaling threshold epithelial somites from the mesenchymal presomitic mesoderm implemented by posterior gradients of Wnt and FGF (Aulehla (PSM). How the rhythmic signaling pulse delivered by the et al., 2003; Diez del Corral and Storey, 2004; Dubrulle et al., segmentation clock is translated into the periodic morphogenesis of 2001; Hubaud and Pourquie, 2014; Sawada et al., 2001). Cells of somites remains poorly understood. Here, we focused on the role of the posterior PSM exhibit mesenchymal characteristics and paraxial protocadherin (PAPC/Pcdh8) in this process. We showed express Snail-related transcription factors (Dale et al., 2006; that in chicken and mouse embryos, PAPC expression is tightly Nieto, 2002). In the anterior PSM, cells downregulate snail/slug regulated by the clock and wavefront system in the posterior PSM. We expression and upregulate epithelialization-promoting factors such observed that PAPC exhibits a striking complementary pattern to N- as paraxis (Barnes et al., 1997; Sosic et al., 1997). This molecular cadherin (CDH2), marking the interface of the future somite boundary transition correlates with the anterior PSM cells progressively in the anterior PSM. Gain and loss of function of PAPC in chicken acquiring epithelial characteristics (Duband et al., 1987; Martins embryos disrupted somite segmentation by altering the CDH2- et al., 2009). -
Bilirubin Modulates Leukocyte Recruitment to Sites of Inflammation
Bilirubin modulates leukocyte recruitment to sites of inflammation A dissertation presented by Megan Elizabeth Vogel B.S., Ohio University 2011 To The Graduate School of the University of Cincinnati in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Internal Medicine, Division of Digestive Diseases of the College of Medicine March 2017 Committee Chair: Stephen D. Zucker, M.D. Abstract Background: Bilirubin is the principal end-product of heme catabolism. While generally thought to be little more than a metabolic by-product, there is accumulating epidemiological evidence that higher serum bilirubin levels are associated with a lower incidence of inflammatory disorders such as inflammatory bowel and cardiovascular disease. However, the mechanism(s) by which bilirubin may exert an anti-inflammatory effect remains poorly understood. The transendothelial migration of immune cells to sites of inflammation is a highly- ordered, multi-step process that is initiated when endothelial cells become activated to express adhesion molecules, including Vascular Cell Adhesion Molecule 1 (VCAM-1) and Intercellular Adhesion Molecule 1 (ICAM-1), on their luminal surface. The specific binding of leukocyte integrins to VCAM-1 and/or ICAM-1 triggers endothelial signaling cascades that result in the intracellular generation of superoxide and hydrogen peroxide. These reactive oxygen species (ROS) induce reorganization of the actin cytoskeleton, promoting leukocyte transmigration. There are many disease states in which VCAM-1 and ICAM-1 are believed to play an essential pathogenic role in mediating leukocyte trafficking. As bilirubin is a potent, chain-breaking antioxidant, our central hypothesis is that it exerts an anti-inflammatory effect by disrupting adhesion molecule-mediated leukocyte migration through the scavenging of ROS signaling intermediaries. -
Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role in CD40/CD40L Signaling
Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role in CD40/CD40L Signaling This information is current as Yoko K. Takada, Jessica Yu, Michiko Shimoda and of October 2, 2021. Yoshikazu Takada J Immunol published online 22 July 2019 http://www.jimmunol.org/content/early/2019/07/19/jimmun ol.1801630 Downloaded from Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision http://www.jimmunol.org/ • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: by guest on October 2, 2021 http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2019 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Published July 22, 2019, doi:10.4049/jimmunol.1801630 The Journal of Immunology Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role in CD40/CD40L Signaling Yoko K. Takada,*,† Jessica Yu,* Michiko Shimoda,* and Yoshikazu Takada*,† CD40L plays a major role in immune response and is a major therapeutic target for inflammation. Integrin a5b1 and CD40 simultaneously bind to CD40L. It is unclear if a5b1 and CD40 work together in CD40/CD40L signaling or how a5b1 binds to CD40L. -
Kinetic Properties of Collagen Receptors on Human Keratinocytes 2337
Journal of Cell Science 112, 2335-2345 (1999) 2335 Printed in Great Britain © The Company of Biologists Limited 1999 JCS9937 Integrin α and β subunit contribution to the kinetic properties of α2β1 collagen receptors on human keratinocytes analyzed under hydrodynamic conditions Bénédicte Masson-Gadais, Anne Pierres, Anne-Marie Benoliel, Pierre Bongrand* and Jean-Claude Lissitzky Laboratoire d’Immunologie, INSERM U 387, Hôpital de Sainte-Marguerite, BP 29, 13274 Marseille Cedex 09, France *Author for correspondence (e-mail: [email protected]) Accepted 10 May; published on WWW 24 June 1999 SUMMARY The adhesion of keratinocytes to type I collagen or with ligand recognition and also with the ligand-β1 chain laminin 5 was studied in a laminar flow chamber. These interactions responsible for bond stabilization. The latter experiments provided an insight into the binding kinetics hypothesis was supported by the finding that the partial of integrins in their natural environment and the effects of alteration of α2 chain function by inhibiting antibodies was monoclonal antibodies specific for α and β chains. Cells corrected by anti-β1 chain antibody TS2/16. These results driven by a force too low to alter the natural lifetime of a could not be ascribed to allosteric changes of the functional single bond displayed multiple arrests. Studying the region of β1 integrin subunits regulated by TS2/16 since frequency and duration of these arrests yielded fairly direct there was no competition between the binding of TS2/16 information on the rate of bond formation (on-rate) and and anti-α2 chain antibodies. dissociation (off-rate). Off-rate values obtained on collagen Interpreted within the framework of current concepts of or laminin 5 (0.06 seconds−1) were tenfold lower than values integrin-ligand binding topology, these data suggest that determined on selectins. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
CD Markers Are Routinely Used for the Immunophenotyping of Cells
ptglab.com 1 CD MARKER ANTIBODIES www.ptglab.com Introduction The cluster of differentiation (abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules. So-called CD markers are routinely used for the immunophenotyping of cells. Despite this use, they are not limited to roles in the immune system and perform a variety of roles in cell differentiation, adhesion, migration, blood clotting, gamete fertilization, amino acid transport and apoptosis, among many others. As such, Proteintech’s mini catalog featuring its antibodies targeting CD markers is applicable to a wide range of research disciplines. PRODUCT FOCUS PECAM1 Platelet endothelial cell adhesion of blood vessels – making up a large portion molecule-1 (PECAM1), also known as cluster of its intracellular junctions. PECAM-1 is also CD Number of differentiation 31 (CD31), is a member of present on the surface of hematopoietic the immunoglobulin gene superfamily of cell cells and immune cells including platelets, CD31 adhesion molecules. It is highly expressed monocytes, neutrophils, natural killer cells, on the surface of the endothelium – the thin megakaryocytes and some types of T-cell. Catalog Number layer of endothelial cells lining the interior 11256-1-AP Type Rabbit Polyclonal Applications ELISA, FC, IF, IHC, IP, WB 16 Publications Immunohistochemical of paraffin-embedded Figure 1: Immunofluorescence staining human hepatocirrhosis using PECAM1, CD31 of PECAM1 (11256-1-AP), Alexa 488 goat antibody (11265-1-AP) at a dilution of 1:50 anti-rabbit (green), and smooth muscle KD/KO Validated (40x objective). alpha-actin (red), courtesy of Nicola Smart. PECAM1: Customer Testimonial Nicola Smart, a cardiovascular researcher “As you can see [the immunostaining] is and a group leader at the University of extremely clean and specific [and] displays Oxford, has said of the PECAM1 antibody strong intercellular junction expression, (11265-1-AP) that it “worked beautifully as expected for a cell adhesion molecule.” on every occasion I’ve tried it.” Proteintech thanks Dr. -
Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in -
Of VLA-4 and VLA-5 VCAM-1 and Fibronectin Through Clustering Promoting Macrophage Adhesion to Chemerin Contributes to Inflammati
Chemerin Contributes to Inflammation by Promoting Macrophage Adhesion to VCAM-1 and Fibronectin through Clustering of VLA-4 and VLA-5 This information is current as of October 1, 2021. Rosie Hart and David R. Greaves J Immunol 2010; 185:3728-3739; Prepublished online 18 August 2010; doi: 10.4049/jimmunol.0902154 http://www.jimmunol.org/content/185/6/3728 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2010/08/18/jimmunol.090215 Material 4.DC1 http://www.jimmunol.org/ References This article cites 60 articles, 30 of which you can access for free at: http://www.jimmunol.org/content/185/6/3728.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on October 1, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2010 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Chemerin Contributes to Inflammation by Promoting Macrophage Adhesion to VCAM-1 and Fibronectin through Clustering of VLA-4 and VLA-5 Rosie Hart and David R. -
Cell Adhesion Molecules in Normal Skin and Melanoma
biomolecules Review Cell Adhesion Molecules in Normal Skin and Melanoma Cian D’Arcy and Christina Kiel * Systems Biology Ireland & UCD Charles Institute of Dermatology, School of Medicine, University College Dublin, D04 V1W8 Dublin, Ireland; [email protected] * Correspondence: [email protected]; Tel.: +353-1-716-6344 Abstract: Cell adhesion molecules (CAMs) of the cadherin, integrin, immunoglobulin, and selectin protein families are indispensable for the formation and maintenance of multicellular tissues, espe- cially epithelia. In the epidermis, they are involved in cell–cell contacts and in cellular interactions with the extracellular matrix (ECM), thereby contributing to the structural integrity and barrier for- mation of the skin. Bulk and single cell RNA sequencing data show that >170 CAMs are expressed in the healthy human skin, with high expression levels in melanocytes, keratinocytes, endothelial, and smooth muscle cells. Alterations in expression levels of CAMs are involved in melanoma propagation, interaction with the microenvironment, and metastasis. Recent mechanistic analyses together with protein and gene expression data provide a better picture of the role of CAMs in the context of skin physiology and melanoma. Here, we review progress in the field and discuss molecular mechanisms in light of gene expression profiles, including recent single cell RNA expression information. We highlight key adhesion molecules in melanoma, which can guide the identification of pathways and Citation: D’Arcy, C.; Kiel, C. Cell strategies for novel anti-melanoma therapies. Adhesion Molecules in Normal Skin and Melanoma. Biomolecules 2021, 11, Keywords: cadherins; GTEx consortium; Human Protein Atlas; integrins; melanocytes; single cell 1213. https://doi.org/10.3390/ RNA sequencing; selectins; tumour microenvironment biom11081213 Academic Editor: Sang-Han Lee 1. -
Anti-ITGA9 Monoclonal Antibody, Clone FQS0833 (DCABH-3776) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-ITGA9 monoclonal antibody, clone FQS0833 (DCABH-3776) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit monoclonal to Integrin alpha 9 Antigen Description Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Immunogen Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) Isotype IgG Source/Host Rabbit Species Reactivity Mouse, Rat, Human Clone FQS0833 Purity Tissue culture supernatant Conjugate Unconjugated Applications WB, IHC-P Positive Control NIH3T3, A673, HepG2, and A549 cell lysates, Human lung and Human skin tissues Format Liquid Size 100 μl Buffer Preservative: 0.01% Sodium azide; Constituents: 50% Glycerol, 0.05% BSA Preservative 0.01% Sodium Azide Storage store at -20°C. Avoid freeze / thaw cycles. Ship Shipped at 4°C. GENE INFORMATION Gene Name ITGA9 integrin, alpha 9 [ Homo sapiens ] Official Symbol ITGA9 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Synonyms ITGA9; integrin, alpha 9; integrin alpha-9; ALPHA RLC; integrin; alpha 4 like; ITGA4L; RLC; integrin alpha-RLC; ALPHA-RLC; Entrez Gene ID 3680 Protein Refseq NP_002198 UniProt ID Q13797 Chromosome Location 3p21.3 Pathway Arrhythmogenic right ventricular cardiomyopathy (ARVC), organism-specific biosystem; Arrhythmogenic right ventricular cardiomyopathy (ARVC), conserved biosystem; Axon guidance, organism-specific biosystem; Cell adhesion molecules (CAMs), organism-specific biosystem; Cell adhesion molecules (CAMs), conserved biosystem; Developmental Biology, organism- specific biosystem; Dilated cardiomyopathy, organism-specific biosystem. -
Table 3: Average Gene Expression Profiles by Chromosome
Supplemental Data Table 1: Experimental Setup Correlation Array Reverse Fluor Array Extraction Coefficient Print Batch (Y/N) mean (range) DLD1-I.1 I A N DLD1-I.2 I B N 0.86 DLD1-I.3 I C N (0.79-0.90) DLD1-I.4 I C Y DLD1 DLD1-II.1 II D N DLD1-II.2 II E N 0.86 DLD1-II.3 II F N (0.74-0.94) DLD1-II.4 II F Y DLD1+3-II.1 II A N DLD1+3-II.2 II A N 0.85 DLD1 + 3 DLD1+3-II.3 II B N (0.64-0.95) DLD1+3-II.4 II B Y DLD1+7-I.1 I A N DLD1+7-I.2 I A N 0.79 DLD1 + 7 DLD1+7-I.3 I B N (0.68-0.90) DLD1+7-I.4 I B Y DLD1+13-I.1 I A N DLD1+13-I.2 I A N 0.88 DLD1 + 13 DLD1+13-I.3 I B N (0.84-0.91) DLD1+13-I.4 I B Y hTERT-HME-I.1 I A N hTERT-HME-I.2 I B N 0.85 hTERT-HME hTERT-HME-I.3 I C N (0.80-0.92) hTERT-HME-I.4 I C Y hTERT-HME+3-I.1 I A N hTERT-HME+3-I.2 I B N 0.84 hTERT-HME + 3 hTERT-HME+3-I.3 I C N (0.74-0.90) hTERT-HME+3-I.4 I C Y Supplemental Data Table 2: Average gene expression profiles by chromosome arm DLD1 hTERT-HME Ratio.7 Ratio.1 Ratio.3 Ratio.3 Chrom. -
Integrin Alpha 9 Antibody Product Data Sheet Tested Species Reactivity Details Human (Hu) Catalog Number: PA5-27771
Lot Number: QE2031191G Integrin alpha 9 Antibody Product Data Sheet Tested Species Reactivity Details Human (Hu) Catalog Number: PA5-27771 Size: 100 µL Tested Applications Dilution * Class: Polyclonal Western Blot (WB) 1:500-1:3000 Type: Antibody Immunohistochemistry (Paraffin) 1:100-1:1000 Clone: (IHC (P)) 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 experiment using appropriate negative and positive controls. Recombinant fragment corresponding to a region within Immunogen: amino acids 1 and 255 of Human Integrin alpha 9 Form Information Form: Liquid Concentration: 1mg/ml Purification: Antigen affinity chromatography PBS, pH 7, with 1% BSA, 20% Storage Buffer: glycerol Preservative: 0.01% thimerosal Storage Conditions: -20° C, Avoid Freeze/Thaw Cycles Product Specific Information General Information PA5-27771 targets Integrin alpha 9 in IHC (P) and WB applications and This gene encodes an alpha integrin. Integrins are heterodimeric integral shows reactivity with Human samples. membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, The PA5-27771 immunogen is recombinant fragment corresponding to a when bound to the beta 1 chain, forms an integrin that is a receptor for region within amino acids 1 and 255 of Human Integrin alpha 9. VCAM1, cytotactin and osteopontin. Expression of this gene has been found For Research Use Only. Not for use in diagnostic procedures. Not for to be upregulated in small cell lung cancers. resale without express authorization.