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Recombinant Human CD38 Fc Chimera Avi-tag Protein, CF

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2 μg/lane of Biotinylated Recombinant Human CD38 Fc Chimera Avi-tag Protein (Catalog # AVI10920) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 69-77 kDa and 140-150 kDa, respectively.
2 μg/lane of Biotinylated Recombinant Human CD38 Fc Chimera Avi-tag Protein (Catalog # AVI10920) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

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

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Recombinant Human CD38 Fc Chimera Avi-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA.<br />When Human CD38 Antibody (Catalog&nbsp;# <a class="NoLineLink" href="http://www.rndsystems.com/product_results.aspx?k=AF2404">AF2404</a>) is immobilized at 1.00&nbsp;μg/mL (100&nbsp;µL/well), Biotinylated Recombinant Human CD38 Fc Chimera Avi-tag binds with an ED<sub>50</sub> of 1.00-6.00 ng/mL.<br /><br />Measured by its ability to convert the substrate nicotinamide guanine dinucleotide (NGD<SUP>+</SUP>) to cyclic GDP-ribose. Graeff, R.M. <EM>et al</EM>. (1994) J. Biol. Chem. <STRONG>269</STRONG>:30260.<br />The specific activity is &gt;700 pmol/min/μg, as measured under the described conditions.<br /><br />
Accession #
N-terminal Sequence
Val43
Structure / Form
Biotinylated via Avi-tag.
Protein/Peptide Type
Recombinant Enzymes
Endotoxin Note
<0.100 EU per 1 µg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
  • Enzyme Activity
Theoretical MW
58 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
69-77 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
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 Fc Chimera Avi-tag 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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