GITR/TNFRSF18 Antibody [Alexa Fluor® 594] Summary
| Immunogen |
Mouse myeloma cell line NS0-derived recombinant mouse GITR/TNFRSF18 Ser22-His153 Accession # Q8C4K3 |
| Specificity |
Detects mouse GITR/TNFRSF18 in direct ELISAs and Western blots. In direct ELISAs, approximately 20% cross-reactivity with recombinant human (rh) GITR is observed, less than 2% cross-reactivity with recombinant mouse (rm) 4-1BB, rmCD27, |
| Isotype |
IgG |
| Clonality |
Polyclonal |
| Host |
Goat |
| Purity Statement |
Antigen Affinity-purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Packaging, Storage & Formulations
| Storage |
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 degreesC as supplied |
| Buffer |
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for GITR/TNFRSF18 Antibody [Alexa Fluor® 594]
Background
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 p56 lck 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).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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