Recombinant Human CD38 Fc Chimera Biotinylated Protein, CF

Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD38 Fc Chimera Protein (Catalog # BT10920) binds to Human CD38 Antibody (MAB2404) with an ED50 of 1.00-10.0 ng/mL.

2 μg/lane of Biotinylated Recombinant Human CD38 Fc Chimera Protein (Catalog # BT10920) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 64-76 kDa and 130-150 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human CD38 Fc Chimera Biotinylated Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD38 Fc Chimera binds to Human CD38 Antibody (Catalog # MAB2404) with an ED₅₀ of 1.00-10.0 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived human CD38 protein
  

  Human CD38 (Val43-Ile300) Accession # P28907.2	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• N-terminal Sequence: Val43
• Structure / Form: Disulfide-linked homodimer, Biotinylated via amines
• Protein/Peptide Type: Recombinant Enzymes
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 32 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: 64-76 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in MES and NaCl with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

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 Biotinylated 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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