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Recombinant human ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (CD38) production in mammalian cells involves co-cloning the gene encoding the extracellular domain of the human CD38 protein (43-300aa) into an expression vector with a C-terminal hFc-tag gene, followed by transformation into mammalian cells. The cells are cultured under conditions that induce protein expression. After sufficient growth, the cells are lysed to release the recombinant protein. Purification is achieved using affinity chromatography technique. The purity of the CD38 protein is confirmed using SDS-PAGE, reaching over 85%. Human CD38 protein is a transmembrane glycoprotein that stimulates B-lymphocyte activation and acts as an enzyme that catalyzes the synthesis of cyclic ADP-ribose from NAD+ [1]. It is a part of the ADP ribosyl cyclase/CD38 gene family and is evolutionarily conserved, indicating its importance in human physiology [2]. CD38 functions as an ectoenzyme and a receptor, degrading NAD and modulating cellular NAD homeostasis [3]. Furthermore, CD38 is involved in oxytocin secretion, social behavior, and calcium regulation [4][5]. It is expressed in inflammatory conditions and is robustly induced in human macrophages under inflammatory stimuli [6]. CD38 is also implicated in diseases like cancer, where it is methylated in prostate cancer and regulates extracellular NAD+ [7]. References:[1] M. Dong, Y. Qi, S. Sun, X. Pu, Z. Yang, L. Zhanget al., Design, synthesis and biological characterization of novel inhibitors of cd38, Organic & Biomolecular Chemistry, vol. 9, no. 9, p. 3246, 2011. https://doi.org/10.1039/c0ob00768d[2] F. Malavasi, S. Deaglio, A. Funaro, E. Ferrero, A. Horenstein, E. Ortolanet al., Evolution and function of the adp ribosyl cyclase/cd38 gene family in physiology and pathology, Physiological Reviews, vol. 88, no. 3, p. 841-886, 2008. https://doi.org/10.1152/physrev.00035.2007[3] E. Chini, C. Chini, J. Netto, G. Oliveira, & W. Schooten, The pharmacology of cd38/nadase: an emerging target in cancer and diseases of aging, Trends in Pharmacological Sciences, vol. 39, no. 4, p. 424-436, 2018. https://doi.org/10.1016/j.tips.2018.02.001[4] H. Higashida, S. Yokoyama, M. Kikuchi, & T. Munesue, Cd38 and its role in oxytocin secretion and social behavior, Hormones and Behavior, vol. 61, no. 3, p. 351-358, 2012. https://doi.org/10.1016/j.yhbeh.2011.12.011[5] V. Sathish, M. Thompson, S. Sinha, G. Sieck, Y. Prakash, & C. Pabelick, Inflammation, caveolae and cd38-mediated calcium regulation in human airway smooth muscle, Biochimica Et Biophysica Acta (Bba) - Molecular Cell Research, vol. 1843, no. 2, p. 346-351, 2014. https://doi.org/10.1016/j.bbamcr.2013.11.011[6] S. Amici, M. Young, J. Narvaez-Miranda, K. Jablonski, J. Arcos, L. Rosaset al., Cd38 is robustly induced in human macrophages and monocytes in inflammatory conditions, Frontiers in Immunology, vol. 9, 2018. https://doi.org/10.3389/fimmu.2018.01593[7] J. Mottahedeh, M. Haffner, T. Grogan, T. Hashimoto, P. Crowell, H. Beltranet al., Cd38 is methylated in prostate cancer and regulates extracellular nad+, Cancer & Metabolism, vol. 6, no. 1, 2018. https://doi.org/10.1186/s40170-018-0186-3
Recombinant human ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (CD38) production in mammalian cells involves co-cloning the gene encoding the extracellular domain of the human CD38 protein (43-300aa) into an expression vector with a C-terminal hFc-tag gene, followed by transformation into mammalian cells. The cells are cultured under conditions that induce protein expression. After sufficient growth, the cells are lysed to release the recombinant protein. Purification is achieved using affinity chromatography technique. The purity of the CD38 protein is confirmed using SDS-PAGE, reaching over 85%.
Human CD38 protein is a transmembrane glycoprotein that stimulates B-lymphocyte activation and acts as an enzyme that catalyzes the synthesis of cyclic ADP-ribose from NAD+ [1]. It is a part of the ADP ribosyl cyclase/CD38 gene family and is evolutionarily conserved, indicating its importance in human physiology [2]. CD38 functions as an ectoenzyme and a receptor, degrading NAD and modulating cellular NAD homeostasis [3]. Furthermore, CD38 is involved in oxytocin secretion, social behavior, and calcium regulation [4][5]. It is expressed in inflammatory conditions and is robustly induced in human macrophages under inflammatory stimuli [6]. CD38 is also implicated in diseases like cancer, where it is methylated in prostate cancer and regulates extracellular NAD+ [7].
References:[1] M. Dong, Y. Qi, S. Sun, X. Pu, Z. Yang, L. Zhanget al., Design, synthesis and biological characterization of novel inhibitors of cd38, Organic & Biomolecular Chemistry, vol. 9, no. 9, p. 3246, 2011. https://doi.org/10.1039/c0ob00768d[2] F. Malavasi, S. Deaglio, A. Funaro, E. Ferrero, A. Horenstein, E. Ortolanet al., Evolution and function of the adp ribosyl cyclase/cd38 gene family in physiology and pathology, Physiological Reviews, vol. 88, no. 3, p. 841-886, 2008. https://doi.org/10.1152/physrev.00035.2007[3] E. Chini, C. Chini, J. Netto, G. Oliveira, & W. Schooten, The pharmacology of cd38/nadase: an emerging target in cancer and diseases of aging, Trends in Pharmacological Sciences, vol. 39, no. 4, p. 424-436, 2018. https://doi.org/10.1016/j.tips.2018.02.001[4] H. Higashida, S. Yokoyama, M. Kikuchi, & T. Munesue, Cd38 and its role in oxytocin secretion and social behavior, Hormones and Behavior, vol. 61, no. 3, p. 351-358, 2012. https://doi.org/10.1016/j.yhbeh.2011.12.011[5] V. Sathish, M. Thompson, S. Sinha, G. Sieck, Y. Prakash, & C. Pabelick, Inflammation, caveolae and cd38-mediated calcium regulation in human airway smooth muscle, Biochimica Et Biophysica Acta (Bba) – Molecular Cell Research, vol. 1843, no. 2, p. 346-351, 2014. https://doi.org/10.1016/j.bbamcr.2013.11.011[6] S. Amici, M. Young, J. Narvaez-Miranda, K. Jablonski, J. Arcos, L. Rosaset al., Cd38 is robustly induced in human macrophages and monocytes in inflammatory conditions, Frontiers in Immunology, vol. 9, 2018. https://doi.org/10.3389/fimmu.2018.01593[7] J. Mottahedeh, M. Haffner, T. Grogan, T. Hashimoto, P. Crowell, H. Beltranet al., Cd38 is methylated in prostate cancer and regulates extracellular nad+, Cancer & Metabolism, vol. 6, no. 1, 2018. https://doi.org/10.1186/s40170-018-0186-3
| Cat.No | ACP03629 | Target Name | CD38 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | Mammalian cell |
| Expression Range | 43-300aa | Mol Weight | 57.4 kDa |
| Protein Length | Extracellular Domain | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P28907 |
|---|
Uniprot Id
P28907
Target Species
Human
Target Name
CD38
Target Full Name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Target Function
Synthesizes the second messengers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system.
Target Subcellular Location
Membrane; Single-pass type II membrane protein.
Target Protein Families
ADP-ribosyl cyclase family
Target Tissue Specificity
Expressed at high levels in pancreas, liver, kidney, brain, testis, ovary, placenta, malignant lymphoma and neuroblastoma.
Target Research Area
Cancer
Target Synonyms
CD38; ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1; 2'-phospho-ADP-ribosyl cyclase; 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase; 2'-phospho-cyclic-ADP-ribose transferase; ADP-ribosyl cyclase 1; ADPRC 1; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD antigen CD38
Target Background
The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants.
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