Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 18 (TNFRSF18) Protein (hFc), Active

Name: Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 18 (TNFRSF18) Protein (hFc), Active
Brand: Beta LifeScience
SKU: BLC-05841P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Activity Measured by its binding ability in a functional ELISA. Immobilized TNFRSF18 at 2 μg/ml can bind TNFSF18 , the EC 50 is 2.565 to 2.940 ng/ml. Biological Activity Assay

Activity Human TNFRSF18 protein hFc tag captured on COOH chip can bind Human TNFSF18 protein hFc and Flag tag with an affinity constant of 38.5 nM as detected by LSPR Assay. Biological Activity Assay

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Product Overview

Description	Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 18 (TNFRSF18) Protein (hFc), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/ug as determined by LAL method.
Activity	1. Measured by its binding ability in a functional ELISA. Immobilized TNFRSF18 at 2 μg/ml can bind TNFSF18 , the EC 50 is 2.565 to 2.940 ng/ml. 2. Human TNFRSF18 protein hFc tag captured on COOH chip can bind Human TNFSF18 protein hFc and Flag tag with an affinity constant of 38.5 nM as detected by LSPR Assay.
Uniprotkb	Q9Y5U5
Target Symbol	TNFRSF18
Synonyms	(CD357)(AITR)(GITR)
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc
Target Protein Sequence	QRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCVQPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHEGHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAEP
Expression Range	26-162aa
Protein Length	Partial
Mol. Weight	40.8 kDa
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, 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	Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway.
Subcellular Location	[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.
Database References	HGNC: 11914 OMIM: 603905 KEGG: hsa:8784 STRING: 9606.ENSP00000328207 UniGene: PMID: 28101786 a novel molecular mechanism by which MBD4 inhibits GITR expression in a DNMT1-dependent manner PMID: 28542810 Aberrant expression of GITR may contribute to systemic lupus erithematosus pathogenesis. Glucocorticoid may achieve its therapeutic effect partly by inducing GITR expression on Tresps rather than Tregs, which initiates the apoptosis of Tresp cells in SLE patients. PMID: 25293713 GITR expression can enhance the sensitivity to Bortezomib by inhibiting Bortezomib-induced NF-kappaB activation. PMID: 25973846 GITR is a crucial player in differentiation of thymic regulatory T cells and expansion of regulatory T cells, including both thymic regulatory T cells and peripheral regulatory T cells. PMID: 25961057 Data may suggest a key role of regulatory GITR+CD25 low/-CD4+ T cells subset in the modulation of the abnormal immune response in lupus erythematosus (SLE) patients. PMID: 25256257 results suggest that the GITR rs3753348 polymorphism may be involved in the development and susceptibility of CWP. PMID: 25445616 these results show a higher susceptibility to apoptosis in patients' versus controls' T(reg) cells, suggesting that GITR is a T(reg)-cell marker that would be primarily involved in T(reg)-cell survival rather than in their suppressor function. PMID: 23929911 Our findings indicate the possible involvement of GITR-GITRL pathway in the pathogenesis of pSS. PMID: 23935647 GITR acts as a potential tumor suppressor in MM. PMID: 23785514 Data indicate that the mRNAs of CTLA-4 and GITR genes were expressed at lower levels in CVID patients compared to control group. PMID: 23432692 GITR is pathologically expressed on Treg cells in systemic lupus erythematosus. PMID: 22516990 Liver tumor Tregs up-regulate the expression of glucocorticoid-induced tumor necrosis factor receptor compared with Tregs in tumor-free liver tissue and blood. PMID: 22911397 Results suggest that GITR expression might indicate a molecular link between steroid use and complicated acute sigmoid diverticulitis. Increased MMP-9 expression by GITR signalling might explain morphological changes in the colonic wall in diverticulitis. PMID: 22309286 The regulatory SNPs identified in this study will provide useful information for understanding the relevance of sequence polymorphisms in populations of different background and may serve as a basis to study parasite susceptibility in association studies PMID: 21445534 GITRL may contribute to disease pathophysiology and resistance to direct and Rituximab-induced NK reactivity in CLL PMID: 22064350 GITR, which transmits a signal that abrogates regulatory T cell functions, was elevated in early rheumatoid arthritis. PMID: 21670968 DCs transfected with mRNA encoding a humanized anti-CTLA-4 mAb and mRNA encoding a soluble human GITR fusion protein enhance the induction of anti-tumor CTLs in response to DCs. PMID: 22028176 Findings suggest that GITR-expression of TILs is associated with cancer progression. PMID: 21694467 Although GITR transgene costimulation can therapeutically enhance T helper (Th) type 2 cell responses, GITR-GITR ligand interactions are not required for development of Th2-mediated resistance or pathology. PMID: 21705620 Data indicate that CD4(+) CD25(low) GITR(+) cells represent a low percentage of the CD4(+) T-cell population (0.32-1.74%) and are mostly memory cells. PMID: 21557210 study concludes, the rs3753348 C/G SNP in the GITR is associated with Hashimoto's disease prognosis and expression on T(reg) and T(eff) cells PMID: 21592113 GITR rapidly recruits TNF receptor-associated factor 2 (TRAF2) in a ligand-dependent manner; data indicate that the cytoplasmic domain of GITR contains a single TRAF binding site where acidic residues 202/203 and 211-213 are critical for this interaction. PMID: 15944293 Since regulatory T-cells are localized in the vicinity of GITRL-expressing cells in atopic dermatitis skin, the GITR/GITRL interaction may serve to perpetuate the inflammation locally. PMID: 16955181 This protein has been shown to stimulate T cell-mediated antitumor immunity in mice, and now in a human tumor cell line. PMID: 17360848 These data suggest that, despite abnormal GITR expression during HIV infection, GITR triggering enhances HIV-specific CD4(+) T cell cytokine expression and protects HIV-specific CD4(+) T cells from apoptosis. PMID: 17538882 although GITR is an activation marker for NK cells similar to that for T cells, GITR serves as a negative regulator for NK cell activation PMID: 18230609 CD4(+)CD25(+) effector memory T-cells expressing CD134 and GITR seem to play a role in disease mechanisms, as suggested by their close association with disease activity and their participation in the inflammatory process in Wegener's granulomatosis. PMID: 18723571 mechanism of IgG4 induction by regulatory cells involves GITR-GITR-L interactions, IL-10 and TGF-beta. PMID: 18924213 Data show that in humans GITRL expression subverts NK cell immunosurveillance of AML. PMID: 19155305 mRNA level for CTLA-4, ICOS1, IL-23, IL-27, SMAD3 and GITR were lower in T regulatory cells of children with diabetes compared to the control patients PMID: 19547759

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.

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Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 18 (TNFRSF18) Protein (hFc), Active

Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 18 (TNFRSF18) Protein (hFc), Active

Product Overview

Target Details

FAQs