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Recombinant Human CD38 His-tag Biotin Protein, CF

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Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD38 His-tag binds to Human CD38 Antibody (AF2404) with an ED50 of 1.50‑15.0 ng/mL.
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD38 His-tag binds to Human CD38 Antibody (AF2404) with an ED50 of 1.50‑15.0 ng/mL.
Biotinylated Recombinant Human CD-38 His-tag Protein (Catalog # BT2404) is measured by its ability to convert the substrate nicotinamide guanine dinucleotide (NGD+) to cyclic GDP-ribose.
2 μg/lane of Biotinylated Recombinant Human CD38 His-tag Protein (Catalog # BT2404) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity, Enzyme Activity
Format
Carrier-Free

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Recombinant Human CD38 His-tag Biotin Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD38 His-tag binds to Human CD38 Antibody (Catalog # AF2404) with an ED50 of 1.50-15.0 ng/mL. Measured by its ability to convert the substrate nicotinamide guanine dinucleotide (NGD+) to cyclic GDP-ribose. Graeff, R.M. et al. (1994) J. Biol. Chem. 269:30260. The specific activity is >2200 pmol/min/μg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human CD38 protein
Val43-Ile300 with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Val43
Structure / Form
Biotinylated via amines
Protein/Peptide Type
Recombinant Enzymes
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
  • Enzyme Activity
Theoretical MW
31 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
40-44 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES and NaCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human CD38 His-tag Biotin Protein, CF

  • 2'-phospho-ADP-ribosyl cyclase
  • 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase (EC:2.4.99.20)
  • 2'-phospho-cyclic-ADP-ribose transferase
  • ADPRC 1
  • ADPRC1
  • ADP-ribosyl cyclase 1
  • ADP-ribosyl Cyclase
  • ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
  • ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
  • cADPr hydrolase 1
  • CD_antigen: CD38
  • CD38 antigen (p45)
  • CD38 antigen
  • CD38 molecule
  • CD38
  • cluster of differentiation 38
  • Cyclic ADP-ribose hydrolase 1
  • Cyclic ADP-ribose Hydrolase
  • EC 2.4.99.20
  • EC 3.2.2.6
  • EC:3.2.2.6
  • NAD(+) nucleosidase
  • T10

Background

CD38, also known as ADP-ribosyl cyclase, converts NAD(P)+ into three separate products with calcium mobilizing ability: cyclic ADP-ribose, NAADP+, and ADP-ribose (1). CD38 is a Type II transmembrane glycoprotein composed of an intracellular domain, a single transmembrane helix domain, and a large extracellular domain that contains the catalytic site (2). CD38 is expressed in B and T lymphocytes, osteoclasts, and in cardiac, pancreatic, liver and kidney cells (3, 4). Through its production of cyclic ADP-ribose, CD38 modulates calcium-mediated signal transduction in many types of cells (5, 6). CD38 is also reported to bind as a receptor to trigger signaling cascades (7, 8). Through both mechanisms, CD38 influences proliferation and trafficking (8, 9). CD38 is used as a marker for poor prognosis in chronic lymphocytic leukemia and multiple myeloma and is an attractive cancer immunotherapy drug target (8-11).
  1. Schuber, F. and F.E. Lund (2004) Curr. Mol. Med. 4:249.
  2. Liu, Q. et al. (2005) Structure. 13:1331.
  3. Jackson, D.G. and J.I. Bell (1990) J. Immunol. 144:2811.
  4. Sun, L. et al. (1999) J. Cell Biol. 146:1161.
  5. Partida-Sanchez, S. et al. (2001) Nature Med. 7:1209.
  6. Kato, I. et al. (1995) J. Biol. Chem. 270:30045. 
  7. Deaglio, S. (2000) Chem. Immunol. 75:99.
  8. Chillemi,A. et al. (2013) Mol. Med. 19:99.
  9. Vaisitti, T. et al. (2015) Leukemia. 29:356.
  10. Atanackovic, D. et al. (2016) Oncoimmunology. 5:e1217374.
  11. Tai, Y-T. et al. (2017) Oncotarget. 8:112166.

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