New England Biolabs Canada

Product Pathways - Innate Immunity

LGP2 (D3I3L) Rabbit mAb #12869

Item# Description List Price Web Price Qty
12869S LGP2 (D3I3L) Rabbit mAb - 100 µl $372.00
*On-line ordering is for Canadian customers only. Web pricing is applicable only to orders placed online at
Application Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W Human Endogenous 77 Rabbit IgG

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting


Specificity / Sensitivity

LGP2 (D3I3L) Rabbit mAb recognizes endogenous levels of total LGP2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val478 of human LGP2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, untreated (-) or treated with Human Interferon-α1 (hIFNα) #8927 (10 ng/ml, overnight; +), using LGP2 (D3I3L) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower).

Western Blotting

Western Blotting

Western blot analysis of extracts from THP-1 cells differentiated with TPA #4174 (80 nM, overnight), untreated or LPS-treated (1 μg/ml for indicated times), using LGP2 (D3I3L) Rabbit mAb (upper) or β-Actin (D6A8) #8457 (lower).

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing Myc/DDK-tagged full-length human LGP2 protein (hLGP2-Myc/DDK; +), using LGP2 (D3I3L) Rabbit mAb.


Antiviral innate immunity depends on the combination of parallel pathways triggered by virus detecting proteins in the Toll-like receptor (TLR) family and RNA helicases, such as Rig-I (retinoic acid-inducible gene I) and MDA-5 (melanoma differentiation-associated antigen 5), which promote the transcription of type I interferons (IFN) and antiviral enzymes (1-3). TLRs and helicase proteins contain sites that recognize the molecular patterns of different virus types, including DNA, single-stranded RNA (ssRNA), double-stranded RNA (dsRNA), and glycoproteins. These antiviral proteins are found in different cell compartments; TLRs (i.e. TLR3, TLR7, TLR8, and TLR9) are expressed on endosomal membranes and helicases are localized to the cytoplasm. Rig-I expression is induced by retinoic acid, LPS, IFN, and viral infection (4,5). Both Rig-I and MDA-5 share a DExD/H-box helicase domain that detects viral dsRNA and two amino-terminal caspase recruitment domains (CARD) that are required for triggering downstream signaling (4-7). Rig-I binds both dsRNA and viral ssRNA that contains a 5'-triphosphate end not seen in host RNA (8,9). Though structurally related, Rig-I and MDA-5 detect a distinct set of viruses (10,11). The CARD domain of the helicases, which is sufficient to generate signaling and IFN production, is recruited to the CARD domain of the MAVS/VISA/Cardif/IPS-1 mitochondrial protein, which triggers activation of NF-κB, TBK1/IKKε, and IRF-3/IRF-7 (12-15).

The DExD/H-box family helicase laboratory of genetics and physiology 2 (LGP2, DHX58) is a Rig-I-like receptor (RLR) that lacks the CARD domain and associated signaling ability (6,16). Research studies demonstrate that LGP2 helicase binds dsRNA and inhibits the Rig-I-like receptors Rig-I and MDA-5. Expression of LGP2 is induced by interferon, dsRNA, and viral infection (17). Studies using LGP2-deficient animals demonstrate a complicated interaction between LGP2 and the other RLRs that involves both positive and negative effects on interferon regulation (18-20). In addition, LGP2 may regulate apoptosis, contribute to CD8+ T cell survival, and protect cancer cells from ionizing radiation (21,22).

  1. Yoneyama, M. and Fujita, T. (2007) J Biol Chem 282, 15315-8.
  2. Meylan, E. and Tschopp, J. (2006) Mol Cell 22, 561-9.
  3. Thompson, A.J. and Locarnini, S.A. (2007) Immunol Cell Biol 85, 435-45.
  4. Imaizumi, T. et al. (2002) Biochem Biophys Res Commun 292, 274-9.
  5. Zhang, X. et al. (2000) Microb Pathog 28, 267-78.
  6. Yoneyama, M. et al. (2005) J Immunol 175, 2851-8.
  7. Yoneyama, M. et al. (2004) Nat Immunol 5, 730-7.
  8. Hornung, V. et al. (2006) Science 314, 994-7.
  9. Pichlmair, A. et al. (2006) Science 314, 997-1001.
  10. Kato, H. et al. (2006) Nature 441, 101-5.
  11. Childs, K. et al. (2007) Virology 359, 190-200.
  12. Meylan, E. et al. (2005) Nature 437, 1167-72.
  13. Xu, L.G. et al. (2005) Mol Cell 19, 727-40.
  14. Kawai, T. et al. (2005) Nat Immunol 6, 981-8.
  15. Seth, R.B. et al. (2005) Cell 122, 669-82.
  16. Rothenfusser, S. et al. (2005) J Immunol 175, 5260-8.
  17. Komuro, A. and Horvath, C.M. (2006) J Virol 80, 12332-42.
  18. Venkataraman, T. et al. (2007) J Immunol 178, 6444-55.
  19. Childs, K.S. et al. (2013) PLoS One 8, e64202.
  20. Satoh, T. et al. (2010) Proc Natl Acad Sci U S A 107, 1512-7.
  21. Suthar, M.S. et al. (2012) Immunity 37, 235-48.
  22. Widau, R.C. et al. (2014) Proc Natl Acad Sci U S A, [Epub ahead of print].

Application References

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