Anti-Hu CD38 FITC

Anti-Hu CD38 FITC

• Background: CD38 (NAD+ glycohydrolase) is a type II transmembrane glycoprotein able to induce activation, proliferation and differentiation of mature lymphocytes and mediate apoptosis of myeloid and lymphoid progenitor cells. Another role of CD38 is provided by enzymatic activity of its extracellular part. CD38 acts as NAD+ glycohydrolase converting NAD+ into ADP-ribose, as ADP-ribosyl cyclase producing cADPR and as cADPR hydrolase, thus affecting levels of calcium-mobilizing metabolites. ADPR produced by CD38 serves as an important second messenger of neutrophil and dendritic cell migration. CD38 belongs to markers of B cell subsets, leukemia, and a target of immunotherapy in myeloma treatment.
• Specifications: The mouse monoclonal antibody HB7 (HB-7) recognizes an extracellular epitope within amino acids 273-285 of human CD38, a 45 kDa type II transmembrane glycoprotein strongly expressed mainly on plasma cells and activated T and B lymphocytes it is an antigenic marker of lymphoid cells. Its binding is blocked by daratumumab.
• CAS Number: 9007-83-4
• Certification: RUO
• Host: Mouse
• Species Reactivity: Human
• Immunogen: BJAB cell line
• Target Antigen: CD38
• Isotype: Igg1 κ
• Clone: HB7
• Applications: Flow cytometry: The reagent is designed for analysis of human blood cells using 4 μl reagent / 100 μl of whole blood or 106 cells in a suspension. The content of a vial (0.4 mL) is sufficient for 100 tests.
• Validated Applications: WB, ICC, FC
• Format: FITC
• Buffer: Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
• References & Citations: *Goldmacher VS, Bourret LA, Levine BA, Rasmussen RA, Pourshadi M, Lambert JM, Anderson KC: Anti-CD38-blocked ricin: an immunotoxin for the treatment of multiple myeloma. Blood 1994 Nov 184(9):3017-25., URL: https://pubmed.ncbi.nlm.nih.gov/7524764/,*Zhao YJ, Zhu WJ, Wang XW, Zhang LH, Lee HC: Determinants of the membrane orientation of a calcium signaling enzyme CD38. Biochim Biophys Acta 2015 Sep1853(9):2095-103., URL: https://pubmed.ncbi.nlm.nih.gov/25447548/,*Berthelier V, Laboureau J, Boulla G, Schuber F, Deterre P: Probing ligand-induced conformational changes of human CD38. Eur J Biochem. 2000 May267(10):3056-64., URL: https://pubmed.ncbi.nlm.nih.gov/10806406/,*Li T, Qi S, Unger M, Hou YN, Deng QW, Liu J, Lam CM, Wang XW, Xin D, Zhang P, Koch-Nolte F, Hao Q, Zhang H, Lee HC, Zhao YJ: Immuno-targeting the multifunctional CD38 using nanobody. Sci Rep. 2016 Jun 26:27055. , URL: https://pubmed.ncbi.nlm.nih.gov/27251573/,*Ghose J, Viola D, Terrazas C, Caserta E, Troadec E, Khalife J, Gunes EG, Sanchez J, McDonald T, Marcucci G, Kaur B, Rosenzweig M, Keats J, Rosen S, Krishnan A, Satoskar AR, Hofmeister CC, Pichiorri F: Daratumumab induces CD38 internalization and impairs myeloma cell adhesion. Oncoimmunology. 2018 Jul 237(10):e1486948., URL: https://pubmed.ncbi.nlm.nih.gov/30288349/,*Ferrero E, Orciani M, Vacca P, Ortolan E, Crovella S, Titti F, Saccucci F, Malavasi F: Characterization and phylogenetic epitope mapping of CD38 ADPR cyclase in the cynomolgus macaque. BMC Immunol. 2004 Sep 215:21., URL: https://pubmed.ncbi.nlm.nih.gov/15383153/,*Ratuszny D, Skripuletz T, Wegner F, Groß M, Falk C, Jacobs R, Ruschulte H, Stangel M, Sühs KW: Case report: Daratumumab in a patient with severe refractory anti-NMDA receptor encephalitis. Front Neurol. 2020 Dec 2211:602102., URL: https://pubmed.ncbi.nlm.nih.gov/33414761/,*Verhoeven D, Grinwis L, Marsman C, Jansen MH, van Leeuwen E, Kuijpers TW: B-cell targeting with anti-CD38 daratumumab: implications for differentiation and memory responses. Life Sci Alliance 2023 Jul 76(9):e202302214., URL: https://pubmed.ncbi.nlm.nih.gov/37419630/,*Shrestha P, Astter Y, Davis DA, Zhou T, Yuan CM, Ramaswami R, Wang HW, Lurain K, Yarchoan R: Daratumumab induces cell-mediated cytotoxicity of primary effusion lymphoma and is active against refractory disease. Oncoimmunology 2023 Jan 712(1):2163784., URL: https://pubmed.ncbi.nlm.nih.gov/36632565/,
• Other References: *Cakir-Kiefer C, Muller-Steffner H, Oppenheimer N, Schuber F: Kinetic competence of the cADP-ribose-CD38 complex as an intermediate in the CD38/NAD+ glycohydrolase-catalysed reactions: implication for CD38 signalling. Biochem J. 2001 Sep 1358(Pt 2):399-406., URL: https://www.ncbi.nlm.nih.gov/pubmed/11513738?ordin,*Lund FE, Muller-Steffner H, Romero-Ramirez H, Moreno-García ME, Partida-Sánchez S, Makris M, Oppenheimer NJ, Santos-Argumedo L, Schuber F: CD38 induces apoptosis of a murine pro-B leukemic cell line by a tyrosine kinase-dependent but ADP-ribosyl cyclase- and NAD glycohydrolase-independent mechanism. Int Immunol. 2006 Jul18(7):1029-42., URL: https://www.ncbi.nlm.nih.gov/pubmed/16720618?ordin,*Partida-Sanchez S, Gasser A, Fliegert R, Siebrands CC, Dammermann W, Shi G, Mousseau BJ, Sumoza-Toledo A, Bhagat H, Walseth TF, Guse AH, Lund FE. Chemotaxis of mouse bone marrow neutrophils and dendritic cells is controlled by adp-ribose, the major product generated by the CD38 enzyme reaction. J Immunol. 2007 Dec 1179(11):7827-39., URL: https://www.ncbi.nlm.nih.gov/pubmed/18025229?ordin,
• Storage Conditions: Store at 2-8°C. Protect from prolonged exposure to light. Do not freeze.