GITR Extracellular Domain (human, recombinant)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • FNFRS 18 TNF R NF?B nonlymphoid Toxoplasma antiGITR proinflammatory CD 4 25 high 127 low GL 261 SDSPAGE posttranslational PTM AITR CD 357 GITRD Activation-inducible
• Product Overview:
  Glucocorticoid-induced TNFR-related protein (GITR), also known as TNF receptor superfamily member 18 (TNFRS18), is a type I transmembrane glycoprotein and member of the tumor necrosis factor receptor superfamily with roles in acquired and innate immunity.{56065} It is composed of an extracellular domain that contains a ligand binding site, a transmembrane domain, and a cytoplasmic domain that facilitates the induction of NF-?B signaling.{56065,56063} GITR is primarily expressed in immature and mature T cells and natural killer (NK) cells but is also expressed at low levels in mast cells, eosinophils, B cells, macrophages, as well as non-lymphoid tissues, osteoclast precursor cells, keratinocytes, and retinal epithelial cells. Upon binding of its ligand GITRL (Item No. 32018), GITR binds various TNF receptor-associated factors (TRAFs) and induces signaling in a cell type-specific manner.{56061} GITR protein levels are increased in macrophages and dendritic cells in a mouse model of T. gondii infection, and administration of an agonistic anti-GITR antibody increases pro-inflammatory cytokine production in peritoneal fluid and reduces chronic phase parasite burden in the same model.{56062} Protein levels of GITR are also increased on CD4+CD25+, CD4+CD25high, and CD4+CD25+CD127low/- regulatory T cells isolated from patients with systemic lupus erythematosus (SLE) compared with healthy controls.{56066} Intratumor, but not peripheral, administration of an agonistic anti-GITR antibody increases overall survival in a GL261 murine glioma model.{56064} Cayman’s GITR Extracellular Domain (human, recombinant) protein can be used for ELISA. This protein consists of 147 amino acids, has a calculated molecular weight of 16 kDa, and a predicted N-terminus of Gln26 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the molecular mass of the protein is approximately 27 kDa due to apparent post-translational modifications.