Human ULBP-4/RAET1E PE-conjugated Antibody Summary
Gly30-Asp225
Accession # Q8TD07
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of ULBP-4/RAET1E in HEK293 cells by Flow Cytometry HEK293 human embryonic kidney cells transfected with (A) ULBP-4/RAET1E or (B) irrelevant protein, and eGFP were stained with Mouse Anti-Human ULBP-4/RAET1E PE-conjugated Monoclonal Antibody (Catalog # FAB6285P). View our protocol for Staining Membrane-associated Proteins
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: ULBP-4/RAET1E
ULBP-4 (cytomegalovirus glycoprotein UL16 binding protein 4), also called RAET1E (retinoic acid early transcript 1E), Letal (lymphocyte effector cell toxicity activating ligand) and NKG2DL4 (NKG2D ligand 4), is a 40-50 kDa member of the ULBP/RAET1 family of cell surface proteins that function as ligands for NKG2D (1‑6). While most family members are GPI-anchored, only ULBP-4/RAET1E and ULBP-5/RAET1G express a transmembrane form (1, 4, 6, 7). Human ULBP-4 mRNA encodes 263 amino acids (aa) including a 30 aa signal sequence, a 195 aa extracellular domain (ECD), a 23 aa transmembrane domain, and a 15 aa cytoplasmic sequence. A soluble 35 kDa form diverges at aa 208 and is thought to antagonize the transmembrane form (5). Other potential splice variants of 220, 227 and 280 aa are transmembrane proteins (8). Within the ECD, ULBP-4 shares 34-41% aa sequence identity with family members (1, 7). Rodent NKG2D ligands Rae-1 alpha -epsilon are, like human ULBP and MIB proteins, distantly related to MHC class I proteins, but none of the families share significant sequence identity (2, 4). Low expression of ULBP‑4 mRNA is found in normal tissues, with high expression variably reported in the small intestine (3) and skin (4). Expression is stimulated by TNF-alpha and down‑regulated by retinoic acid (3). ULBP-4 is abnormally expressed on most colon cancer and some other tumor cell lines and virus-infected peripheral blood cells (3, 6). ULBP-4 binds and costimulates NKG2D-expressing effector cells including NK cells, NKT cells, gamma δ T cells, and CD8+ alpha beta T cells, activating cytolytic activity and/or cytokine production (3, 4, 7). In some gamma δ T cells, direct ULBP-4 binding to both TCR gamma δ and NKG2D has been demonstrated (6). ULBP-4 is also thought to function as a minor histocompatibility antigen in humans (1).
- Radosavljevic, M. et al. (2002) Genomics 79:114.
- Kondo, M. et al. (2010) Immunogenetics 62:441.
- Conejo-Garcia, J.R. et al. (2003) Cancer Biol. Ther. 2:446.
- Chalupny, N.J. et al. (2003) Biochem. Biophys. Res. Commun. 305:129.
- Cao, W. et al. (2007) J. Biol. Chem. 282:18922.
- Kong, Y. et al. (2009) Blood 114:310.
- Bacon, L. et al. (2004) J. Immunol. 173:1078.
- Cao, W. et al. (2008) Int. Immunol. 20:981.
Product Datasheets
Citations for Human ULBP-4/RAET1E PE-conjugated Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 6
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Fumarate Upregulates Surface Expression of ULBP2/ULBP5 by Scavenging Glutathione Antioxidant Capacity
Authors: RI Høgh, A Droujinine, SH Møller, SD Jepsen, M Mellergaar, L Andresen, S Skov
J. Immunol., 2020-03-06;0(0):.
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SETDB1 suppresses NK cell-mediated immunosurveillance in acute myeloid leukemia with granulo-monocytic differentiation
Authors: Chang, YH;Yamamoto, K;Fujino, T;Wang, TW;Sugimoto, E;Zhang, W;Yabushita, T;Suzaki, K;Pietsch, EC;Weir, BA;Crescenzo, R;Cowley, GS;Attar, R;Philippar, U;Wunderlich, M;Mizukawa, B;Zheng, Y;Enomoto, Y;Imai, Y;Kitamura, T;Goyama, S;
Cell reports
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
gammadelta T cells are effectors of immunotherapy in cancers with HLA class I defects
Authors: NL de Vries, J van de Haa, V Veninga, M Chalabi, ME Ijsselstei, M van der Pl, J van den Bu, D Ruano, JG van den Be, JB Haanen, LJ Zeverijn, BS Geurts, GF de Wit, TW Battaglia, H Gelderblom, HMW Verheul, TN Schumacher, LFA Wessels, F Koning, NFCC de Miranda, EE Voest
Nature, 2023-01-11;613(7945):743-750.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
Genetic and Molecular Basis of Heterogeneous NK Cell Responses against Acute Leukemia
Authors: DR Makanga, F Da Rin de, G David, C Willem, L Dubreuil, N Legrand, T Guillaume, P Peterlin, A Lebourgeoi, MC Béné, A Garnier, P Chevallier, K Gendzekhad, A Cesbron, K Gagne, B Clemenceau, C Retière
Cancers (Basel), 2020-07-16;12(7):.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
The pharmalogical reactivation of p53 function improves breast tumor cell lysis by granzyme B and NK cells through induction of autophagy
Authors: M Chollat-Na, T Ben Safta-, D Haferssas, G Meurice, S Chouaib, J Thiery
Cell Death Dis, 2019-09-20;10(10):695.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
Interleukin-15 stimulates natural killer cell-mediated killing of both human pancreatic cancer and stellate cells
Authors: JRM Van Audena, J De Waele, E Marcq, J Van Loenho, E Lion, JMJ Van den Be, R Jesenofsky, A Masamune, G Roeyen, P Pauwels, F Lardon, M Peeters, ELJ Smits
Oncotarget, 2017-01-01;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry
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