Name: PE Human GITR (TNFRSF18) Protein (C-His)
Brand: InnoCyto
SKU: 811501
Price: 245 USD
Availability: InStock

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PE Human GITR (TNFRSF18) Protein (C-His)

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Cat #	Size	Price	Quantity
811501	25 ug	$245
811502	100 ug	$595

Bulk/Custom

Product Details

Application	Flow Cytometry
Format	Liquid, PE
Expression Host	CHO
Target Name	TNFRSF18, AITR, GITR, CD357
Species	Human
Sources	Recombinant Human Human GITR/TNFRSF18 (Gln26-Glu161) with C-terminus His-tag is expressed in CHO cell and conjugated to PE.
Accession Number	Q9Y5U5
Molecular Weight	The protein has a predicted molecular weight of 16.1 kDa. Under DTT-reducing conditions, it migrates at approximately 25 kDa on SDS-PAGE prior to conjugation.
Affinity Tag	C-His
Regulatory Status	RUO
Formulation	1xPBS buffer, pH7.4, 0.09% NaN3 with a carrier protein
Endotoxin level	Not tested
Protein Concentration	25µg size is bottled at 0.1mg/mL concentration. 100 µg size is bottled at lot specific concentration.
Storage and Handling	Briefly centrifuge the vial upon receipt. An unopened vial may be stored at 2–8°C for up to six months.
Research Areas	Co-stimulation, Tregs, Activated T cells, Cancer Immunology, Immune Checkpoints

Background Information

Glucocorticoid-induced tumor necrosis factor receptor–related protein (GITR), also known as CD357 or TNFRSF18, is a co-stimulatory receptor that plays an important role in regulating T cell activation, survival, and immune balance. GITR is constitutively expressed at high levels on regulatory T cells (Tregs) and at lower levels on naïve conventional T cells, with expression rapidly upregulated following T cell activation. It is also expressed on natural killer (NK) cells and some myeloid populations. Through its signaling, GITR influences both effector and regulatory arms of the immune system.

Structurally, GITR is a type I transmembrane glycoprotein and a member of the tumor necrosis factor receptor (TNFR) superfamily. Its extracellular region contains cysteine-rich domains typical of TNFR family members that mediate ligand binding. GITR has a single transmembrane segment and a cytoplasmic tail that lacks intrinsic enzymatic activity but recruits TNF receptor–associated factors (TRAFs), particularly TRAF2 and TRAF5. These adaptor proteins initiate downstream signaling cascades, including activation of NF-κB and MAPK pathways, which promote cell survival, proliferation, and cytokine production.

The primary ligand for GITR is GITR ligand (GITRL), also known as TNFSF18, which is expressed on activated antigen-presenting cells such as dendritic cells, macrophages, and B cells, as well as on endothelial cells in inflamed tissues. Engagement of GITR by GITRL provides a co-stimulatory signal that enhances effector T cell activation and resistance to suppression. In regulatory T cells, GITR signaling can transiently reduce suppressive function, thereby shifting the immune balance toward activation in certain contexts.

GITR has been implicated in a variety of disease settings. In autoimmune and inflammatory diseases, heightened GITR signaling may contribute to excessive T cell activation and tissue damage by weakening regulatory control. In allergic disease, GITR can promote Th2 responses and inflammation. In cancer, GITR is highly expressed on tumor-infiltrating Tregs, where it contributes to immune suppression within the tumor microenvironment. At the same time, GITR expression on effector T cells provides an opportunity to enhance anti-tumor immunity.

Therapeutically, GITR is an active target in immuno-oncology. Agonistic antibodies targeting GITR aim to simultaneously stimulate effector T cells and attenuate Treg-mediated suppression within tumors, thereby enhancing anti-tumor immune responses. These agents are being evaluated alone and in combination with immune checkpoint inhibitors. Conversely, strategies to inhibit GITR–GITRL interactions are being explored for the treatment of autoimmune and inflammatory diseases, highlighting GITR’s dual relevance as both a driver of immunity and a contributor to immune-mediated pathology.

Frequently Asked Questions

How is a fluorescence labeled recombinant protein different from a labeled antibody for the same target?

A labeled protein (e.g., a fluorescent ligand or receptor domain) binds its natural counter-receptor or binding partner directly, making it useful for functional binding assays, competition/blocking studies, and receptor occupancy measurements — whereas an antibody typically binds a specific epitope regardless of the protein's natural binding activity. Choose the labeled protein format when you need to assess biologically relevant binding interactions rather than simple target detection.

Can these proteins be used in flow cytometry, and are they compatible with other panel reagents?

Yes, fluorescence labeled proteins are commonly used in flow cytometry panels to detect receptor expression or ligand binding on live cells, and are designed to be compatible with standard antibody panels. As with any multicolor panel, confirm spectral compatibility and run proper compensation controls when combining labeled proteins with labeled antibodies.

What controls should I use with fluorescence labeled recombinant proteins?

Recommended controls include an unlabeled/unconjugated version of the same protein (for competition/blocking controls), an irrelevant labeled protein of the same conjugate as a background control, and standard unstained/FMO controls for gating. Species- or format-matched controls are noted on the product page where available.

What applications are these proteins validated for?

Common applications include receptor binding assays, flow cytometry-based ligand-receptor studies, ELISA-based detection, and blocking/competition assays to study receptor occupancy or antagonist activity. Specific validated applications and recommended usage concentrations vary by product and are detailed on the individual product page.

Have a product or application question? Consult our FAQs or contact us.

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