Recombinant Human AITRL / TNFSF18 Protein

Name: Recombinant Human AITRL / TNFSF18 Protein
Brand: Beta LifeScience
SKU: BL-1723SG
Availability: InStock

Collections: Co-stimulatory receptors, Cytokines and growth factors, Recombinant proteins, Tumor necrosis factors and receptors (tnfs)

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Product Overview

Tag	N/A
Host Species	Human
Accession	Q9UNG2
Synonym	Activation-inducible TNF-related ligand, AITRL, Glucocorticoid-induced TNF-related ligand, GITRL, hGITRL, Tumor necrosis factor ligand superfamily member 18, TNFSF18, TL-6, Recombinant Human Activation-Induced TNFR Member Ligand (TNFSF18).
Background	TNFSF18 is a transmembrane glycoprotein which is expressed in vascular endothelial cells as well as neurons, antigen presenting cells, CD4-- CD8- double negative thymic precursors, and in the eye. TNFSF18 works to mediate the interactions between T cells and endothelial cells, and T cell growth. It has been shown that TNFSF18's expression is transiently up-regulated by proinflammatory stimulation.
Description	Recombinant Human AITRL (TNFSF18) was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	14.2 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human AITRL / TNFSF18 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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. Promotes leukocyte adhesion to endothelial cells. Regulates migration of monocytes from the splenic reservoir to sites of inflammation.
Subcellular Location	Cell membrane; Single-pass type II membrane protein.
Protein Families	Tumor necrosis factor family
Database References	HGNC: 11932 OMIM: 603898 KEGG: hsa:8995 STRING: 9606.ENSP00000385470 UniGene: Hs.248197
Tissue Specificity	Expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells.

Gene Functions References

GITRL levels are significantly elevated in rheumatoid arthritis serum and synovial fluid and are positively correlated with autoantibody production in rheumatoid arthritis, suggesting a role of GITRL in the development of rheumatoid arthritis. PMID: 27098050
GITRL modulates the activities of p38 MAPK and STAT3 to promote Th17 cell differentiation in autoimmune arthritis. PMID: 26657118
An increase in GITRL may impair the balance of Th17/Treg, and contribute to the pathopoiesis of Hashimoto's thyroiditis. PMID: 25429429
Serum GITRL levels were higher in SLE patients. PMID: 23251213
Glucocorticoid-induced TNF-related ligand (GITRL) confers pseudoexpression to tumor cells by platelets, which results in GITRL expression by megakaryocytes and their platelet progeny. PMID: 22649191
observation suggests a link between cytokine-regulated keratinocyte GITRL expression and its role in inflammatory responses in AD PMID: 22417213
GITRL upregulation induced by IFN-beta on dendritic cells downregulates CTLA-4 on regulatory T (Treg) cells, facilitating proliferation of anergic Treg cells in multiple sclerosis treatment of multiple sclerosis patients. PMID: 22112394
GITRL expression on Kupffer cells may mediate acute rejection in liver transplantation PMID: 21693309
The incorporation of an isoleucine zipper motif could markedly improve the costimulation of hsGITRL. PMID: 20228835
Upregulation by proinflammatory cytokines suggests GITRL may play important role in ocular immunity. High level of constitutive GITRL expression on photoreceptor inner segments suggests photoreceptors participate in regulation of ocular inflammation. PMID: 15326137
Regulates ossteoclasst genersation and substantiate the major role played by the endothelium in bone physiology. PMID: 16179414
Using a GITRL-transfected cell line, we demonstrate that GITRL promotes NK cell cytotoxicity and IFN-gamma production. PMID: 16397134
GITRL could be a potential candidate for regulation of the ocular immune privilege and the balance between immune privilege and inflammation PMID: 16874737
Constitutive expression of GITRL by tumor cells diminishes natural killer cell antitumor immunity. PMID: 17360848
although huGITRL is not capable of alleviating Treg suppression of responder T cells, huGITRL overexpression on monocyte-derived DC enhances their capacity to induce antigen-specific T cell responses PMID: 17449724
These observations raise the possibility that the GITRL-mediated inflammatory activation of macrophages is involved in the pathogenesis of inflammatory diseases. PMID: 17602748
Levels of AITRL were significantly increased in serum of breast cancer patients PMID: 17914571
hGITRL ectodomain displays considerable self-association/dissociation in solution with a dynamic equilibrium between trimeric and monomeric forms over the range of protein concentrations studied. PMID: 18040044
identify multiple oligomeric species of hGITRL that possess distinct kinetics of ERK activation. PMID: 18378892
The strong correlation of tumor incidence and elevated soluble GITRL levels indicates that soluble GITRL is released from cancers in vivo, leading to impaired NK cell immunosurveillance of tumors PMID: 18689545

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.