Recombinant Human CD96v2 Fc Chimera Protein, CF Summary
|Human CD96 |
Accession # P40200-2
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.
|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.
Human CD96, also known as Tactile (T cell-activated increased late expression), is a 160 kDa type I transmembrane glycoprotein of the Ig superfamily that shows peak expression 6-9 days after activation of T, NK, and a subpopulation of B cells (1, 2). CD96 is also frequently expressed on acute myeloid leukemia and myelodysplastic stem cells (3, 4). It is expressed on CD4+ and CD8+ T cells, plus NK cells and select B cells (5). Low expression of adhesive human CD69 is a rare cause of C syndrome, a set of developmental anomalies in cranial bone (trigonocephaly), skin and viscera, demonstrating a role for CD96 in development of these tissues (2, 6). Human CD96 has two isoforms generated by alternative splicing. Isoform 2 is the most common form of CD96 that shows a 16 amino acid (aa) deletion comparing to isoform 1. Mature human CD96 isoform 2 is a 548 amino acid (aa), type I transmembrane glycoprotein. It contains a 482 aa extracellular region that contains three Ig-like domains. The two N-terminal domains are V-type and I-type, while the distal domain is a C-type structure (2). Within the ECD, human CD96 shares 53% and 52% aa sequence identity with mouse CD96 and rat CD96, respectively (7). The ECD is highly N- and O-glycosylated (1). An 80 kDa soluble form is elevated in human serum during chronic hepatitis B (9). The most N-terminal Ig-like domain of human CD96 binds to CD155/PVR (poliovirus receptor), but CD96/CD155 interaction is species-specific (2, 7, 10). Mouse CD96 also binds Nectin-1 (7). On NK cells, costimulatory CD96 and DNAM-1 (CD226) are thought to have paired activity with inhibitory TIGIT, all of which bind CD155 and various Nectins (11, 12). CD96 can promote NK cell adhesion to, and killing of target cells, including tumors that express CD155 (10, 11).
- Wang, P.L. et al. (1992) J. Immunol. 148:2600.
- Meyer, D. et al. (2009) J. Biol. Chem. 284:2235.
- Hosen, N. et al. (2007) Proc. Natl. Acad. Sci. USA 104:11008.
- Xie, W. et al. (2010) Cytometry A 77:840.
- Eriksson,E. M. et al. (2012) PLOS One 7:e51696
- Kaname, T. et al. (2007) Am. J. Hum. Genet. 81:835.
- Seth, S. et al. (2007) Biochem. Biophys. Res. Commun. 364:959.
- Protein Accession # BAE32358.
- Gong, J. et al. (2008) Clin. Exp. Immunol. 155:207.
- Fuchs, A. et al. (2004) J. Immunol. 172:3394.
- Stanietsky, N. and O. Mandelboim (2010) FEBS Lett. 584:4895.
- Xu, Z. and B. Jin (2010) Cell. Mol. Immunol. 7:11.
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