AITRL/TNFSF18 Trimer Protein, Human (HEK293, His-Flag)
Based on 1 Customer Validation
AITRL, a type II transmembrane protein, is a ligand for glucocorticoid-induced TNFR-related protein (GITR). When AITRL binds to GITR, GITR can produce costimulatory signals that regulate T-cell proliferation and effector functions. GITR/AITRL interaction plays a role in the pathogenesis of tumor, inflammation, as well as autoimmune diseases. Besides, AITRL plays a role in endothelial cells (EC)-activation and increases STAT-1 phosphorylation and the expression of adhesion molecules (VCAM-1, ICAM-1). AITRL/TNFSF18 Trimer Protein, Human (HEK293, His-Flag) is a recombinant human AITRL (Q72-S199) trimer with N-terminal His and Flag tag, which is expressed in HEK293.
- Species: Human
- Source: HEK293
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
AITRL, a type II transmembrane protein, is a ligand for glucocorticoid-induced TNFR-related protein (GITR). When AITRL binds to GITR, GITR can produce costimulatory signals that regulate T-cell proliferation and effector functions. GITR/AITRL interaction plays a role in the pathogenesis of tumor, inflammation, as well as autoimmune diseases[1]. Besides, AITRL plays a role in endothelial cells (EC)-activation and increases STAT-1 phosphorylation and the expression of adhesion molecules (VCAM-1, ICAM-1)[2]. AITRL/TNFSF18 Trimer Protein, Human (HEK293, His-Flag) is a recombinant human AITRL (Q72-S199) trimer with N-terminal His and Flag tag, which is expressed in HEK293.
Background
GITRL (AITRL), a type II transmembrane protein, is a ligand for glucocorticoid-induced TNFR-related protein (GITR). GITR, a member of the TNFR superfamily, is expressed in T cells, natural killer cells and some myeloid cells. And GITRL is mainly expressed on antigen presenting cells (B cells, dendritic cells), macrophages and endothelial cells (ECs)[1].
When GITRL binds to GITR, GITR can produce costimulatory signals that regulate T-cell proliferation and effector functions. The interaction stimulates proliferation and cytokine production of both CD4+ Teff and Treg cells, and drives antitumor activity of CD8+ T cells[3]. Besides, GITRL plays a role in EC-activation and promotes adhesion in both mice and humans, which increases STAT-1 phosphorylation and the augmented expression of adhesion molecules such as VCAM-1 and ICAM-1[2].
Human GITRL shares < 55% common aa identity with mouse. Human GITRL consists of cytoplasmic domain (M1-W27), helical domain (L28-F48), and extracellular domain (L49-S177). Human GITRL is a trimer, but can also be a monomer or assemble in other multimeric structures[4].
GITR/GITRL interaction plays a role in the pathogenesis of tumor, inflammation, as well as autoimmune diseases[1].
In Vitro
AITRL (human, 48 h) reduces the suppressive capacity of MDSCs on CD4+ T cells (MDSCs induced from healthy donors)[5].
Verified Bioactivity
Immobilized Human GITR Ligand Trimer, His Tag at 2 μg/mL (100 μl/well) on the plate. Dose response curve for Human GITR, hFc Tag with the EC50 of 0.44 μg/mL determined by ELISA.
Technical Parameters
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Species Human
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Source HEK293
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Tag N-6*His;N-Flag
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Accession
Q9UNG2 (Q50-S177)
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Molecular Construction
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N-term
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6*His-Flag
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AITRL (Q50-S177)
Accession # Q9UNG2 -
C-term
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Protein Length
Extracellular Domain
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Synonyms
TNFSF18; Activation-Inducible TNF-Related Ligand; TNF Superfamily Member 18; GITRL; HGITRL; Glucocorticoid-Induced TNFR-Related Protein Ligand; AITRL; Tumor Necrosis Factor Superfamily Member 18; TL6; Tumor Necrosis Factor Ligand 2A; Tumor Necrosis Factor (Ligand) Superfamily, Member 18; AITR Ligand; Tumor Necrosis Factor Ligand Superfamily Member 18; GITR Ligand; Glucocorticoid-Induced TNF-Related Ligand; TNLG2A
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AA Sequence
QLETAKEPCMAKFGPLPSKWQMASSEPPCVNKVSDWKLEILQNGLYLIYGQVAPNANYNDVAPFEVRLYKNKDMIQTLTNKSKIQNVGGTYELHVGDTIDLIFNSEHQVLKNNTYWGIILLANPQFIS
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Predicted Molecular Mass
47.5 kDa
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Molecular Weight
Approximately 54-64 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by Bis-Tris PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (264 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[1]. Tian J, et al. The Role of GITR/GITRL Interaction in Autoimmune Diseases. Front Immunol. 2020 Oct 9;11:588682. [Content Brief]
[2]. Lacal PM, et al. Glucocorticoid-induced tumor necrosis factor receptor family-related ligand triggering upregulates vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 and promotes leukocyte adhesion. J Pharmacol Exp Ther. 2013 Oct;347(1):164-72. [Content Brief]
[3]. Wang F, et al. Structures of mouse and human GITR-GITRL complexes reveal unique TNF superfamily interactions. Nat Commun. 2021 Mar 2;12(1):1378. [Content Brief]
[4]. Placke T, et al. Glucocorticoid-induced TNFR-related (GITR) protein and its ligand in antitumor immunity: functional role and therapeutic modulation. Clin Dev Immunol. 2010;2010:239083. [Content Brief]
[5]. Tian J, et al. Increased GITRL Impairs the Function of Myeloid-Derived Suppressor Cells and Exacerbates Primary Sjögren Syndrome. J Immunol. 2019 Mar 15;202(6):1693-1703. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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