Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 18 Protein (TNFSF18), Active

Name: Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 18 Protein (TNFSF18), Active
Brand: Beta LifeScience
SKU: BLC-06039P
Availability: InStock

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 18 Protein (TNFSF18), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The biological activity as determined by stimulation of IL-8 production using human PBMC is in a concentration range of 0.1-10 ng/ml.
Uniprotkb	Q9UNG2
Target Symbol	TNFSF18
Synonyms	Activation inducible TNF related ligand; Activation-inducible TNF-related ligand; AITR ligand; AITRL; GITR ligand; GITRL; Glucocorticoid induced TNF related ligand; Glucocorticoid induced TNFR related protein ligand; Glucocorticoid-induced TNF-related ligand; hGITRL; MGC138237; TL6; TNF18_HUMAN; TNFSF18; TNLG2A; Tumor necrosis factor (ligand) superfamily member 18; Tumor necrosis factor ligand 2A; Tumor necrosis factor ligand superfamily member 18
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	ETAKEPCMAK FGPLPSKWQM ASSEPPCVNK VSDWKLEILQ NGLYLIYGQV APNANYNDVA PFEVRLYKNK DMIQTLTNKS KIQNVGGTYE LHVGDTIDLI FNSEHQVLKN NTYWGIILLA NPQFIS
Expression Range	74-199aa
Protein Length	Partial
Mol. Weight	14.3 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 m filtered PBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.