ELISA with Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Prima 4136

HPLC of Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Primary 4136

SDS-PAGE gel of Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein ( 4136

Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Primary Amine Labeling) 4136

$525.00 – $1,750.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Gln50-Ser177

SKU: 4136parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	N-His-Flag
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Glucocorticoid-induced TNFR-related protein (TNFRSF18, GITR, CD357), expressed by T cells, and its ligand (TNFSF18, GITRL), expressed by myeloid populations, provide co-stimulatory signals that boost T cell activity. Due to the important role that GITR plays in regulating immune functions, agonistic stimulation of GITR is a promising therapeutic concept.
molecular weight	The protein has a predicted MW of 47.5 kDa. Due to glycosylation, the protein migrates to 50-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Primary Amine Labeling) 4136

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Glucocorticoid-induced TNFR-related protein (TNFRSF18, GITR, CD357), expressed by T cells, and its ligand (TNFSF18, GITRL), expressed by myeloid populations, provide co-stimulatory signals that boost T cell activity. Due to the important role that GITR plays in regulating immune functions, agonistic stimulation of GITR is a promising therapeutic concept.
Protein names Tumor necrosis factor ligand superfamily member 18 (Activation-inducible TNF-related ligand) (AITRL) (Glucocorticoid-induced TNF-related ligand) (hGITRL)
Gene names TNFSF18,TNFSF18 AITRL GITRL TL6 UNQ149/PRO175
Protein family Tumor necrosis factor family
Mass 9606Da
Function Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (PubMed:23892569). Promotes leukocyte adhesion to endothelial cells (PubMed:23892569). Regulates migration of monocytes from the splenic reservoir to sites of inflammation (By similarity).
Subellular location Cell membrane ; Single-pass type II membrane protein .
Tissues Expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells.
Structure Homodimer (By similarity). Homotrimer.
Target Relevance information above includes information from UniProt accession: Q9UNG2
The UniProt Consortium

Data

ELISA with Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Prima

Immobilized Human GITR, hFc Tag at 2µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human GITR Ligand Trimer, His Tag with the EC50 of 11.4ng/ml determined by ELISA.

HPLC of Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (Primary

The purity of Biotinylated Human GITR Ligand Trimer is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Human GITR Ligand/TNFSF18 Trimer Protein (

Biotinylated Human GITR Ligand Trimer on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.