Recombinant Human CD96v2 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human CD155/PVR Fc Chimera
(Catalog #
9174-CD)
is immobilized at 1 μg/mL, 100 μL/well, the concentration of
Recombinant Human CD96 v2 Fc Chimera that produces 50% of the optimal binding
response is 30-150 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human CD96 protein Human CD96 (Lys25-Met503) Accession # P40200-2 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Lys25 |
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. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
80 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 |
132-152 kDa, 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 PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD96v2 Fc Chimera Protein, CF
Background
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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