GITR (Aglyco-Fc-Fusion)
GITR (Aglyco-Fc-Fusion)
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GITR (glucocorticoid-induced tumor necrosis factor receptor family-related gene), is a type I membrane protein whose extracellular domain contains 3 cysteine-rich domain (CRD) repeats. It has two isoforms, one is the intact molecule and another one is secreted form. The hGITR gene mapped to chromosome 1p36, near a cluster of five genes encoding TNFR homologs.
Interacting protein(s): GITRL
Related products: TNF-Receptor Superfamily
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Quick Specs
Species: | Human |
Catalog no.: | P7035G |
Synonym: | TNFRSF18, AITR, GITR-D |
Tag: | Aglycosylated mouse IgG2a-Fc |
GenBank accession: | NM_004195 |
SwissPro accession: | Q9Y5U5 |
Construction: | h.GITR (Q26 - E161)-m.IgG-Fc |
Expression host: | 293T |
MW (Calculated): | 41,706 daltons |
MW (SDS-PAGE): | 45 Kd |
Abs 0.1% (= 1 mg/ml): | 1.116 |
Purity: | >95 % by SDS-PAGE |
Description
GITR (glucocorticoid-induced tumor necrosis factor receptor family-related gene), is a type I membrane protein whose extracellular domain contains 3 cysteine-rich domain (CRD) repeats. It has two isoforms, one is the intact molecule and another one is secreted form. The hGITR gene mapped to chromosome 1p36, near a cluster of five genes encoding TNFR homologs.
GITR expresses at low levels in lymph node, peripheral blood leukocytes and weakly in spleen and can be induced via antigen-receptor activation. At the cytoplasmic side, GITR specifically binds to TRAF1, TRAF2, and TRAF3, but not TRAF5 and TRAF6, it also binds to SIVA1/SIVA at its C-terminus. GITR was initially noted to be selectively enriched on the surface of regulatory T cells, making this an attractive potential surface marker for these rare cells. However, subsequent studies revealed GITR to also be up-regulated on activated T cells in humans, thus undermining its utility as a regulatory T cell marker.
It is thought that GITR plays a key role in dominant immunological self-tolerance maintained by CD25+/CD4+ regulatory T cells. Knockout studies in mice also suggest the role of this receptor is in the regulation of CD3-driven T-cell activation and programmed cell death.
Amino Acid Sequence.
References
1. Tian J, Zhang B, Rui K, Wang S. The Role of GITR/GITRL Interaction in Autoimmune Diseases. Front Immunol. 2020;11:588682. Epub 20201009. doi: 10.3389/fimmu.2020.588682. PubMed PMID: 33163004; PubMed Central PMCID: PMC7581784.
2. Identification of a new member of the tumor necrosis factor family and its receptor, a human ortholog of mouse GITR. Gurney A.L., Marsters S.A., Huang R.M., Pitti R.M., Mark D.T., Baldwin D.T., Gray A.M., Dowd A.D., Brush A.D., Heldens A.D., Schow A.D., Goddard A.D., Wood W.I., Baker K.P., Godowski P.J., Ashkenazi A. Curr. Biol. 9:215-218 (1999)
3. Identification of a novel activation-inducible protein of the tumor necrosis factor receptor superfamily and its ligand. Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D., Wang S.-X., Kwon B.S. J. Biol. Chem. 274:6056-6061 (1999)
4. Identification of three novel mRNA splice variants of GITR. Nocentini G., Ronchetti S., Bartoli A., Spinicelli S., Delfino D., Brunetti L., Migliorati G., Riccardi C. Cell Death Differ. 7:408-410 (2000)
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