Recombinant Human Lymphotoxin alpha1/beta2 Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Catalog# & Formulation Size Price

Recombinant Human Lymphotoxin alpha1/beta2 Protein Summary

Additional Information
Defined heterotrimer stoichiometry
Details of Functionality
Measured by its ability to induce IL-8 secretion by A375 human melanoma cells. The ED50 for this effect is 3-15 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human Lymphotoxin protein
rhLT alpha
(Leu35-Leu205)
Accession # P01374
GGGGS rhLT beta
(Gln49-Gly244)
Accession # Q06643
GGGGS rhLT beta
(Gln49-Gly244)
Accession # Q06643
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu35
Structure / Form
GS-linked heterotrimer
Protein/Peptide Type
Recombinant Proteins
Gene
LTA
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
61 kDa.
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
65-76 kDa, reducing conditions
Publications
Read Publications using
8884-LY in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Lymphotoxin alpha1/beta2 Protein

  • LT
  • Lymphotoxin alpha
  • Lymphotoxin
  • tnfb
  • TNFSF1
  • TNLG1E

Background

Lymphotoxin alpha (LT-alpha ), and Lymphotoxin beta (LT-beta ) are pro-inflammatory TNF superfamily ligands that play important roles in immune system development (1, 2). The 25 kDa mature human LT-alpha is a secreted protein that shares 75% amino acid (aa) sequence identity with mouse and rat LT-alpha (3, 4). The 33 kDa mature human LT-beta is a type II transmembrane protein that shares 73% aa sequence identity with mouse and rat LT-beta within common regions of their extracellular domains (5). Relative to the human protein, mouse and rat LT-beta have a 66 aa or 65 aa insertion within the ECD, respectively. LT-alpha can be secreted as a homotrimer that binds and activates TNF RI/TNFRSF1A, TNF RII/TNFRSF1B, HVEM/TNFRSF14, and Troy/TNFRSF19 (6-8). LT-alpha is required for development of the spleen, lymph nodes, and Peyer’s patches (9). It also regulates T cell homing to the gut and IgA induction (10). In addition, LT-alpha can form membrane-associated heterotrimers with two copies of LT-beta on the surface of B, T, LTi, and ILC3 cells (2, 5, 11). The Lymphotoxin alpha 1/ beta 2 heterotrimer binds and activates the Lymphotoxin beta R/TNFRSF3 (LT beta R) which is expressed on macrophages, dendritic cells, hepatocytes, intestinal epithelial cells (IEC), follicular dendritic cells (FDC), and high endothelial venules (HEV) (2, 12, 13). LT beta R also serves as a receptor for LIGHT/TNFSF14 (14). LT-alpha 1/ beta 2 promotes the development of FDC networks and HEV in lymphoid tissue, the class switching of immature B cells for IgA production, and the production of homeostatic IL-22 by ILCs (10, 15-17). It can be shed by ADAM17 or MMP-8 mediated cleavage, and the released heterotrimer circulates in the serum and is elevated in synovial fluid of rheumatoid arthritis patients (18).
  1. Lu, T.T. and J.L. Browning (2014) Front. Immunol. 5:47.
  2. Upadhyay, V. and Y.-X. Fu (2014) Cytokine Growth Factor Rev. 25:227.
  3. Gray, P.W. et al. (1984) Nature 312:721.
  4. Nedwin, G.E. et al. (1985) J. Cell Biochem. 29:171.
  5. Browning, J.L. et al. (1993) Cell 72:847.
  6. Schoenfeld, H.J. et al. (1991) J. Biol. Chem. 266:3863.
  7. Mauri, D.N. et al. (1998) Immunity 8:21.
  8. Hashimoto, T. et al. (2008) Cell Cycle 7:106.
  9. De Togni, P. et al. (1994) Science 264:703.
  10. Kruglov, A.A. et al. (2013) Science 342:1243.
  11. Androlewicz, M.J. et al. (1992) J. Biol. Chem. 267:2542.
  12. Sudhamsu, J. et al. (2013) Proc. Natl. Acad. Sci. USA 110:19896.
  13. Crowe, P.D. et al. (1994) Science 264:707.
  14. Eldredge, J. et al. (2006) Biochemistry 45:10117.
  15. Futterer, A. et al. (1998) Immunity 9:59.
  16. Koni, P.A. et al. (1997) Immunity 6:491.
  17. Ota, N. et al. (2011) Nat. Immunol. 12:941.
  18. Young, J. et al. (2010) Cytokine 51:78.

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Publications for Lymphotoxin (8884-LY)(3)

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