| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Bioassay data are not available. |
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| Source | Mouse myeloma cell line, NS0-derived human RELT/TNFRSF19L protein
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| Accession # | |||||||
| N-terminal Sequence | Ser26 |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Gene | RELT |
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| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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| Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 41 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE | 55-58 kDa, reducing conditions |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Supplied as a 0.2 μm filtered solution in PBS. |
| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
RELT (Receptor Expressed in Lymphoid Tissues) is a 46 kDa (predicted) type I transmembrane glycoprotein belonging to the tumor necrosis factor receptor superfamily, designated TNFRSF19-like (TNFRSF19L) (1, 2). It is primarily expressed in hematopoietic tissues and peripheral blood leukocytes (2, 3). Human RELT cDNA encodes 430 amino acids (aa), including a 25 aa signal peptide, a 137 aa extracellular domain containing a TNF receptor cysteine-rich domain and a potential N‑linked glycosylation site, a 21 aa transmembrane domain and a 247 aa cytoplasmic region that lacks a death domain. Within the ECD, human RELT shares 78%, 75%, 75%, 78% and 72% aa sequence homology with mouse, rat, canine, porcine and bovine RELT, respectively. Among TNFRSF members, the RELT extracellular domain is most closely related to that of TROY/TNFRSF19 and OX40 (2). Neither human nor mouse RELT bind any of the ~19 TNF superfamily ligands that have been tested (1). Two related transmembrane proteins, RELL1 and RELL2, have been identified in both human and mouse (3). RELL1 and 2 can interact with and are coexpressed with RELT, and are thought to modulate its signaling (3-5). Intracellularly, RELT has been shown to bind the adaptor protein TRAF-1 and activate the NF‑ kappa B pathway, the phospholipid scramblase PLSCR1, and oxidative stress responsive proteins OSR1 (2-5). Another investigator notes association and signaling through SPAK, but not TRAF or NF kappa B (6). When overexpressed in HEK-293 cells, RELT induces p38 and JNK signaling and activates apoptosis (4-6). Immobilized RELT can also costimulate T-cell proliferation in the presence of CD3 signaling (2).
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