Recombinant Mouse CTLA‑4 Fc Chimera (Catalog # 434-CT) inhibits IL-2 secretion by stimulated Jurkat human acute T cell leukemia cells. The ED50 for this effect is 0.03-0.15 μg/mL when stimulated with 1 μg/mL ...read more
Recombinant Mouse CTLA-4 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit IL-2 secretion by stimulated Jurkat human acute T cell leukemia cells. Linsley, P.S. et al. (1991) J. Exp. Med. 174:561. The ED50 for this effect is 0.1-0.4 µg/mL when stimulated with 1 µg/mL
Recombinant
Human B7‑1/CD80 Fc Chimera (Catalog # 140-B1)
in the presence of PHA.
Source
Mouse myeloma cell line, NS0-derived mouse CTLA-4 protein
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
41 kDa (monomer). 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
55 kDa, reducing conditions
Publications
Read Publications using 434-CT/CF in the following applications:
ligand and transmembrane spliced cytotoxic T lymphocyte associated antigen 4
Background
CTLA-4 (cytotoxic T-lymphocyte-4, designated CD152), is a type I transmembrane T cell inhibitory molecule that is a member of the Ig superfamily (1, 2). Human or mouse CTLA-4 cDNA encodes 223 amino acids (aa) including a 35 aa signal sequence, a 126 aa extracellular domain (ECD) with one Ig-like V-type domain, a 21 aa transmembrane (TM) sequence, and a 41 aa cytoplasmic sequence. It is found as a covalent homodimer of 41 ‑ 43 kDa (2) Within the ECD, mouse CTLA-4 shares 94% and 68 ‑ 71% aa sequence identity with rat and human/porcine/bovine/rabbit/feline/canine CTLA-4, respectively. A 174 aa form that lacks TM and cytoplasmic sequences (sCTLA-4) is possibly secreted (3 ‑ 5). Isoforms of 56 ‑ 79 aa that mainly contain parts of the cytoplasmic domain are reported. In mouse, an isoform lacking the Ig-like domain has ligand-independent inhibitory activity and is termed liCTLA-4 (6). CD28, which is structurally related to CTLA-4, is constitutively expressed on naïve T cells and promotes T cell activation when engaged by B7-2 on antigen-presenting cells (APC) within the immunological synapse (IS) (1, 7, 8). In contrast, CTLA-4 is recruited from intracellular vesicles to the IS beginning 1-2 days after T cell activation (2, 7, 8). It forms a linear lattice with B7-1 on APC, inducing negative regulatory signals and ending T cell activation (9). Abatacept, a therapeutic human CTLA-4-Ig fusion protein (trade name Orencia), competes with CD28 for B7-1 and B7-2 binding and has been used to antagonize T cell activation in autoimmune conditions and to enhance transplant survival (10). Mice deleted for CTLA-4 show no abnormalities until after birth, but then develop lethal autoimmune reactions due to continued T cell activation and poor control by regulatory T cells, which constitutively express CTLA-4 in wild-type mice and humans (11 ‑ 13).
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Teft, W.A. et al. (2006) Annu. Rev. Immunol. 24:65.
Magistrelli, G. et al. (1999) Eur. J. Immunol. 29:3596.
Tector, M. et al. (2009) BMC Immunol. 10:51.
Oaks, M.K. and K.M. Hallett (2000) J. Immunol. 164:5015.
Vijayakrishnan, L. et al. (2004) Immunity 20:563.
Pentcheva-Hoang, T. et al. (2004) Immunity 21:401.
Jansson, A. et al. (2005) J. Immunol 175:1575.
Darlington, P.J. et al. (2005) J. Immunol. 175:996.
Platt, A.M. et al. (2010) J. Immunol. 185:1558.
Wing, K. et al. (2008) Science 322:271.
Friedline, R.H. et al. (2009) J. Exp. Med. 206:421.
Jain, N. et al. (2010) Proc. Natl. Acad. Sci. USA 107:1524.
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CD86 - I work in tandem with CD80 CD86 belongs to the immunoglobulin superfamily of proteins that drive innate and adaptive immune responses. It is an 80kD co-stimulatory molecule for the priming and activation of naive and memory T-cells, respectively. CD86 is expressed on activated ... Read full blog post.
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