Recombinant Mouse BTNL3 Fc Chimera Protein, CF

Measured by its ability to inhibit IL-2 secretion by mouse T cells in the presence of anti-CD3. The ED50 for this effect is 0.4-4 μg/mL.

2 μg/lane of Recombinant Mouse BTNL3 Fc Chimera (Catalog # 10222-BT) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 45-65 kDa and 90-130 kDa, respectively.

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

Recombinant Mouse BTNL3 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit IL-2 secretion by mouse T cells in the presence of anti-CD3. The ED₅₀ for this effect is 0.4-4 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse BTNL3 protein
  

  Recombinant Mouse BTNL3 (Glu28-Pro241) Accession # Q7TST0.3	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: Q7TST0.3
• N-terminal Sequence: Glu28
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Purity Statement: Antigen Affinity-purified
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 51 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: 45-65 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.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

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

Alternate Names for Recombinant Mouse BTNL3 Fc Chimera Protein, CF

• BTN9.1
• BTNL3
• BTNLR
• BTNLRButyrophilin-like receptor
• butyrophilin-like 3
• butyrophilin-like protein 3
• COLF4100

Background

Butyrophilin-like 3 (BTNL3), also referred to as BTNL1, Gm316, and Ng10, is a member of the BTN/MOG Ig-superfamily and shares structural resemblance to the B7 family (1). BTNL3 is a type I transmembrane protein that consists of an extracellular domain (ECD) containing two IgV domains, a single transmembrane domain, and a cytoplasmic domain with a B30.2/SPRY region. Mature mouse BTNL3 shares 30% and 80% amino acid sequence identity with human and rat BTNL3, respectively. BTNL3 mRNA has been identified in many tissues including small intestine, colon, liver, lung, bone marrow and spleen tissue, and it is highly expressed in neutrophils (2-6). The specific function of BTNL3 has yet to be fully elucidated, but BTNL3 is suggested to be a novel negative regulator for T cell activation and immune diseases (7). In humans, BTNL3 has been shown to form heterodimers with BTNL8 and overexpression of this complex leads to CD69 upregulation and T cell antigen receptor downregulation (8). In mice, BTNL3 can form heterodimers with BTNL6 and modulate local immune responses and intraepithelial lymphocytes–epithelial cell interaction pathways (9). Additionally, BTNL3 has been shown to bind directly to V gamma 4+ T cell receptor, suggesting a role in gamma δ T cell regulation (10). BTNL3 expression has also been found to be down-regulated in colon cancer tumors (11). R&D Systems in house data indicate that mouse BTNL3 protein inhibits the secretion of IL-2 from anti-CD3 activated mouse CD3+ T cells.

1. Shibui, A. et al. (1999) J. Hum. Genet. 44:249.
2. Arnett, H.A. et al. (2014) Nat Rev Immunol. 14:5596.
3. Arnett, H.A. et al. (2009) Cytokine 46:370.
4. Abeler-Dorner, L. et al. (2012) Trends Immunol. 33:34.
5. Rhodes, D. et al. (2016) Annu. Rev. Immunol. 34:151.
6. Guo, Y and Wang, AY (2015) Front. Immunol. 6:421.
7. Yamazaki, T. et al. (2010) J Immunol 185:5907.
8. Melandri, D. et al. (2018) Nat Immunol 19:1352.
9. Lebrero-Fernández, C. et al. (2016) Front Immunol. 7:1.
10. Wilcox, C.R. et al. (2019) Immunity 51:813.
11. Lebrero-Fernandez, C. et al. (2016) Immun. Inflammation Dis. 4:191.

Bioinformatics

• Uniprot:
  • Q7TST0.3()