Mouse GITR/TNFRSF18 APC-conjugated Antibody

  • Specificity
    Detects mouse GITR/TNFRSF18 in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant human (rh) 4‑1BB, recombinant mouse (rm) CD27, rmCD30, rmEDAR, rmFas, rhGITR, rhHVEM, rmRANK, rhTROY, and rmTNF R1 is observed.
  • Formulation
    Supplied in a saline solution containing BSA and Sodium Azide.
  • Label
  • Flow Cytometry
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
  • Stability & Storage
    Store the unopened product at 2 - 8° C. Do not use past expiration date. Protect from light.
Background: GITR/TNFRSF18

GITR (glucocorticoid-induced tumor necrosis factor receptor; also named AITR) is a member of the co‑stimulatory subset of the TNF receptor superfamily (1, 2). In mouse, the GITR gene is composed of five exons and encodes multiple length isoforms that arise from alternate splicing. The “standard”, or first reported isoform is a type I transmembrane protein, 228 amino acids (aa) in length that contains a 19 aa signal sequence, a 134 aa extracellular region, a 21 aa transmembrane segment, and a 54 aa cytoplasmic domain. The extracellular region contains four potential N-linked glycosylation sites plus three cysteine-rich pseudorepeats of about 40 aa each (3, 4). The extracellular regions of mouse and human are 57% aa identical. The cytoplasmic domain has a P-x-Q/E-E motif that is known to associate with TRAF2. This is a common characteristic of TNFRSF members with co‑stimulatory functions (4). Three other mouse GITR isoforms (B, C and D) have been reported (5). All share the same N-terminal 101 of 134 aa in the extracellular region (including pseudorepeats #1, #2 and one-half of #3). Isoform D diverges at aa #101 and continues for another 12 aa for a total length of 113 aa. This is a naturally-occurring soluble form. Isoforms B and C show splicing in their cytoplasmic tails that creates cytoplasmic domains of 118 aa and 46 aa, respectively. In both the B and C isoforms, the TRAF2 binding site is spliced out, with a p56lck binding site inserted in isoform B (4). Given its membership in the TNFRSF, it likely functions as a trimer on the cell surface (2). GITR is predominantly expressed on CD4+CD25+ regulatory T cells (Treg) and naïve CD8+ and CD4+ CD25- T cells, where its expression is up-regulated after antigen-driven activation. GITR activation provides co‑stimulatory signals for activated CD4+ CD25- T cells to enhance cell proliferation and augment cytokine production (IL-2, IL-4, IFN-gamma ). On CD4+ CD25+ Treg cells, GITR activation provides co‑stimulatory signals to induce proliferation, setting Treg cells in an active/hyperproliferactive state (6‑8).

  • References:
    1. Kwon, B. et al. (2003) Exp. Mol. Med. 35:8. 
    2. Croft, M. (2003) Nat. Rev. Immunol. 3:609. 
    3. Nocentini, G. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6216.
    4. Nocentini, G. et al. (2000) DNA Cell Biol. 19:205. 
    5. Nocentini, G. et al. (2000) Cell Death Differ. 7:408.
    6. Tone, M. et al. (2003) Proc. Natl. Acad. Sci. USA 100:15059.
    7. Ji, H. et al. (2004) J. Immunol. 172:5823.
    8. Stephens, G.L. et al. (2004) 173:5008.
  • Long Name:
    Glucocorticoid Induced TNF Receptor Family Related Gene
  • Alternate Names:
    AITR; CD357; TNFRSF18; Activation-inducible TNFR family receptor; AITRTNF receptor superfamily activation-inducible protein; CD357 antigen; GITR-D; GITRtumor necrosis factor receptor superfamily member 18; Glucocorticoid-induced TNFR-related protein; tumor necrosis factor receptor superfamily, member 18
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