Recombinant Human CD277/BTN3A1 Fc Avi-tag Protein, CF New
Recombinant Human CD277/BTN3A1 Fc Avi-tag Protein, CF Summary
Product Specifications
Human CD277/BTN3A1 (Gln30-Gly254) Accession # O00481.3 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI8539
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD277/BTN3A1 Fc Chimera Avi-tag Protein (Catalog # AVI8539) binds to Human BTN3A1/2/3 Antibody (MAB7136) with an ED50 of 0.500‑5.00 ng/mL.
2 μg/lane of Biotinylated Recombinant Human CD277/BTN3A1 Fc Chimera Avi-tag Protein (Catalog # AVI8539) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 57‑65 kDa and 110‑130 kDa, respectively.
Reconstitution Calculator
Background: CD277/BTN3A1
Butyrophilin 3A1 (also called BTN3A1) is a 57 kDa type I transmembrane glycoprotein member of the Ig superfamily. It is expressed on a wide variety of immune cells. Similar to BTN3A2 and BTN3A3, BTN3A1 (484 amino acids) is composed of an extracellular N-terminal IgV and a membrane-proximal IgC domain followed by a transmembrane domain and a cytoplasmic tail. These Ig domains are also found in B7 family co-stimulatory molecules, suggesting structural and functional similarities between the two protein families (1). The intracellular portion of BTN3A1 contains a B30.2 domain (2). Although the B30.2 domain of BTN1A1 binds to xanthine oxidoreductase (XOR) and is conserved among BTN1A1 orthologs, this interaction with XOR is not shared by BTN3A1 (3). The B30.2 domain of butyrophilins also functions as a sensor for detecting changes in intracellular phopho-antigen (pAg) concentrations produced during tumorigenesis and microbial infections (4, 5). The specific binding of pAg by the B30.2 domain of BTN3A1 induces a conformational change in its ECD, leading to the activation of V gamma 9Vδ2 T cells (6). Thus, BTN3A1 acts as a critical protein for the activation of V gamma 9Vδ2 T cells following detection of distressed cells (7). The anti-tumor responses of V gamma 9Vδ2 T cells may be enhanced with agonistic anti-BTNA3 antibodies (8). No BTN3A1 homolog has yet been identified in rodents. However, Human BTN3A1 shares 92.4% and 91.6% sequence identity with baboon and rhesus monkey BTN3A1 respectively (9). Our Avi-tag Biotinylated human BTN3A1 Fc chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Abeler-Dorner, L. et al. (2012) Trends Immunol. 33:34.
- Rhodes, D.A. et al. (2001) Genomics 71:351.
- Jeong, J. et al. (2009) J. Biol. Chem. 284:22444.
- Harly, C. et al. (2012) Blood 120:2269.
- Constant, P. et al. (1994) Science 264:267.
- Sandstrom, A. et al. (2014) Immunity 40:490.
- Harly, C. et al. (2015) Front. Immunol. 5:657.
- Bonneville, M. et al. (2006) Curr. Opin. Immunol. 18:539.
- Wang, H. et al. (2013) J.Immunol. 191:1029.
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