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Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse
Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only. -
LAG-3-Expressing Tumor-Infiltrating T Cells Are Associated with Reduced
cancers Article LAG-3-Expressing Tumor-Infiltrating T Cells Are Associated with Reduced Disease-Free Survival in Pancreatic Cancer Lena Seifert 1,2,3,†, Ioana Plesca 4,†, Luise Müller 4, Ulrich Sommer 5, Max Heiduk 1,2, Janusz von Renesse 1, David Digomann 1, Jessica Glück 1, Anna Klimova 6,7, Jürgen Weitz 1,2,3, Marc Schmitz 2,3,4 and Adrian M. Seifert 1,2,3,* 1 Department of Visceral, Thoracic and Vascular Surgery, University Hospital Carl Gustav Carus, TU Dresden, 01307 Dresden, Germany; [email protected] (L.S.); [email protected] (M.H.); [email protected] (J.v.R.); [email protected] (D.D.); [email protected] (J.G.); [email protected] (J.W.) 2 National Center for Tumor Diseases (NCT), Partner Site Dresden, 69120 Heidelberg, Germany; [email protected] 3 German Cancer Consortium (DKTK), Partner Site Dresden, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany 4 Faculty of Medicine Carl Gustav Carus, Institute of Immunology, TU Dresden, 01307 Dresden, Germany; [email protected] (I.P.); [email protected] (L.M.) 5 Faculty of Medicine Carl Gustav Carus, Institute of Pathology, TU Dresden, 01307 Dresden, Germany; [email protected] 6 Faculty of Medicine Carl Gustav Carus, Institute for Medical Informatics and Biometry, TU Dresden, 01307 Dresden, Germany; [email protected] 7 National Center for Tumor Diseases (NCT), Core Unit for Data Management and Analytics (CDMA), Citation: Seifert, L.; Plesca, I.; Müller, 01307 Dresden, Germany L.; Sommer, U.; Heiduk, M.; von * Correspondence: [email protected] Renesse, J.; Digomann, D.; Glück, J.; † These authors have contributed equally to this work. -
Effector CD4 T-Cell Transition to Memory Requires Late Cognate Interactions That Induce Autocrine IL-2
ARTICLE Received 3 Jun 2014 | Accepted 24 Sep 2014 | Published 5 Nov 2014 DOI: 10.1038/ncomms6377 Effector CD4 T-cell transition to memory requires late cognate interactions that induce autocrine IL-2 K. Kai McKinstry1,*, Tara M. Strutt1,*, Bianca Bautista1, Wenliang Zhang1, Yi Kuang1, Andrea M. Cooper2 & Susan L. Swain1 It is unclear how CD4 T-cell memory formation is regulated following pathogen challenge, and when critical mechanisms act to determine effector T-cell fate. Here, we report that following influenza infection most effectors require signals from major histocompatibility complex class II molecules and CD70 during a late window well after initial priming to become memory. During this timeframe, effector cells must produce IL-2 or be exposed to high levels of paracrine or exogenously added IL-2 to survive an otherwise rapid default contraction phase. Late IL-2 promotes survival through acute downregulation of apoptotic pathways in effector T cells and by permanently upregulating their IL-7 receptor expression, enabling IL-7 to sustain them as memory T cells. This new paradigm defines a late checkpoint during the effector phase at which cognate interactions direct CD4 T-cell memory generation. 1 Department of Pathology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655, USA. 2 Trudeau Institute, 154 Algonquin Avenue, Saranac Lake, New York 12983, USA. * These authors contributed equally to this work. Correspondence and requests for materials should be addressed to K.K.M. (email: [email protected]). NATURE COMMUNICATIONS | 5:5377 | DOI: 10.1038/ncomms6377 | www.nature.com/naturecommunications 1 & 2014 Macmillan Publishers Limited. -
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, -
Integrin Alpha 2 Antibody
Product Datasheet Integrin alpha 2 Antibody Catalog No: #49071 Package Size: #49071-1 50ul #49071-2 100ul Orders: [email protected] Support: [email protected] Description Product Name Integrin alpha 2 Antibody Host Species Rabbit Clonality Monoclonal Clone No. SN0752 Purification ProA affinity purified Applications WB, ICC/IF, IHC, IP, FC Species Reactivity Hu, Ms, Rt Immunogen Description recombinant protein Other Names BR antibody CD 49b antibody CD49 antigen like family member B antibody CD49 antigen-like family member B antibody CD49b antibody CD49b antigen antibody Collagen receptor antibody DX5 antibody Glycoprotein Ia deficiency included antibody GP Ia antibody GP Ia deficiency, included antibody GPIa antibody HPA 5 included antibody HPA5 included antibody Human platelet alloantigen system 5 antibody Integrin alpha 2 antibody Integrin alpha-2 antibody Integrin, alpha 2 (CD49B alpha 2 subunit of VLA 2 receptor) antibody ITA2_HUMAN antibody ITGA2 antibody Platelet alloantigen Br(a), included antibody Platelet antigen Br antibody Platelet glycoprotein GPIa antibody Platelet glycoprotein Ia antibody Platelet glycoprotein Ia/IIa antibody Platelet membrane glycoprotein Ia antibody Platelet receptor for collagen, deficiency of, included antibody Very late activation protein 2 receptor alpha 2 subunit antibody VLA 2 alpha chain antibody VLA 2 antibody VLA 2 subunit alpha antibody VLA-2 subunit alpha antibody VLA2 antibody VLA2 receptor alpha 2 subunit antibody VLAA2 antibody Accession No. Swiss-Prot#:P17301 Calculated MW 150 kDa Formulation 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide. Storage Store at -20°C Application Details WB: 1:1,000-5,000 IHC: 1:50-1:200 ICC: 1:100-1:500 FC: 1:50-1:100 Images Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 Western blot analysis of ITGA2 on A431 cells lysates using anti-ITGA2 antibody at 1/1,000 dilution. -
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. -
Integrin Α2β1 in Nonactivated Conformation Can Induce Focal
www.nature.com/scientificreports OPEN Integrin α2β1 in nonactivated conformation can induce focal adhesion kinase signaling Received: 17 February 2017 Maria Salmela1, Johanna Jokinen1,2, Silja Tiitta1, Pekka Rappu1, R. Holland Cheng 2 & Jyrki Accepted: 2 May 2017 Heino1 Published: xx xx xxxx Conformational activation of integrins is generally required for ligand binding and cellular signalling. However, we have previously reported that the nonactivated conformation of α2β1 integrin can also bind to large ligands, such as human echovirus 1. In this study, we show that the interaction between the nonactivated integrin and a ligand resulted in the activation of focal adhesion kinase (FAK) in a protein kinase C dependent manner. A loss-of-function mutation, α2E336A, in the α2-integrin did not prevent the activation of FAK, nor did EDTA-mediated inactivation of the integrin. Full FAK activation was observed, since phosphorylation was not only confirmed in residue Y397, but also in residues Y576/7. Furthermore, initiation of downstream signaling by paxillin phosphorylation in residue Y118 was evident, even though this activation was transient by nature, probably due to the lack of talin involvement in FAK activation and the absence of vinculin in the adhesion complexes formed by the nonactivated integrins. Altogether these results indicate that the nonactivated integrins can induce cellular signaling, but the outcome of the signaling differs from conventional integrin signaling. The well-established model of integrin function stresses the importance of the conformational change from a nonactivated, bent conformation to an active, extended state prior to ligand binding and outside-in signaling1. Despite the fact that the conformational activation of integrins is often required for ligand binding, nonactivated integrins may have specific biological functions as well. -
Human Peripheral Blood Gamma Delta T Cells: Report on a Series of Healthy Caucasian Portuguese Adults and Comprehensive Review of the Literature
cells Article Human Peripheral Blood Gamma Delta T Cells: Report on a Series of Healthy Caucasian Portuguese Adults and Comprehensive Review of the Literature 1, 2, 1, 1, Sónia Fonseca y, Vanessa Pereira y, Catarina Lau z, Maria dos Anjos Teixeira z, Marika Bini-Antunes 3 and Margarida Lima 1,* 1 Laboratory of Cytometry, Unit for Hematology Diagnosis, Department of Hematology, Hospital de Santo António (HSA), Centro Hospitalar Universitário do Porto (CHUP), Unidade Multidisciplinar de Investigação Biomédica, Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto (UMIB/ICBAS/UP), 4099-001 Porto Porto, Portugal; [email protected] (S.F.); [email protected] (C.L.); [email protected] (M.d.A.T.) 2 Department of Clinical Pathology, Centro Hospitalar de Vila Nova de Gaia/Espinho (CHVNG/E), 4434-502 Vila Nova de Gaia, Portugal; [email protected] 3 Laboratory of Immunohematology and Blood Donors Unit, Department of Hematology, Hospital de Santo António (HSA), Centro Hospitalar Universitário do Porto (CHUP), Unidade Multidisciplinar de Investigação Biomédica, Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto (UMIB/ICBAS/UP), 4099-001Porto, Portugal; [email protected] * Correspondence: [email protected]; Tel.: + 351-22-20-77-500 These authors contributed equally to this work. y These authors contributed equally to this work. z Received: 10 February 2020; Accepted: 13 March 2020; Published: 16 March 2020 Abstract: Gamma delta T cells (Tc) are divided according to the type of Vδ and Vγ chains they express, with two major γδ Tc subsets being recognized in humans: Vδ2Vγ9 and Vδ1. -
Targeting Costimulatory Molecules in Autoimmune Disease
Targeting costimulatory molecules in autoimmune disease Natalie M. Edner1, Gianluca Carlesso2, James S. Rush3 and Lucy S.K. Walker1 1Institute of Immunity & Transplantation, Division of Infection & Immunity, University College London, Royal Free Campus, London, UK NW3 2PF 2Early Oncology Discovery, Early Oncology R&D, AstraZeneca, Gaithersburg, MD, USA 3Autoimmunity, Transplantation and Inflammation Disease Area, Novartis Institutes for Biomedical Research, Basel, Switzerland *Correspondence: Professor Lucy S.K. Walker. Institute of Immunity & Transplantation, Division of Infection & Immunity, University College London, Royal Free Campus, London, UK NW3 2PF. Tel: +44 (0)20 7794 0500 ext 22468. Email: [email protected]. 1 Abstract Therapeutic targeting of immune checkpoints has garnered significant attention in the area of cancer immunotherapy, and efforts have focused in particular on the CD28 family members CTLA-4 and PD-1. In autoimmunity, these same pathways can be targeted to opposite effect, to curb the over- exuberant immune response. The CTLA-4 checkpoint serves as an exemplar, whereby CTLA-4 activity is blocked by antibodies in cancer immunotherapy and augmented by the provision of soluble CTLA-4 in autoimmunity. Here we review the targeting of costimulatory molecules in autoimmune disease, focusing in particular on the CD28 family and TNFR family members. We present the state-of-the-art in costimulatory blockade approaches, including rational combinations of immune inhibitory agents, and discuss the future opportunities and challenges in this field. 2 The risk of autoimmune disease is an inescapable consequence of the manner in which the adaptive immune system operates. To ensure effective immunity against a diverse array of unknown pathogens, antigen recognition systems based on random gene rearrangement and mutagenesis have evolved to anticipate the antigenic universe. -