Recombinant Human Lymphotoxin alpha1/beta2 Avi Protein, CF Summary
Additional Information |
Biotinylated His-tag |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human Lymphotoxin beta R Fc Chimera (Catalog # 629-LR) is
immobilized at 25 ng/mL
(100 μL/well), the concentration of Biotinylated Recombinant Human Lymphotoxin alpha1/beta2 His-tag Avi-tag
(Catalog # AVI8884)
that produces 50% of the optimal binding response is 0.75-4.5 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Lymphotoxin protein Human Lymphotoxin alpha (Leu35-Leu205) Accession # P01374 | GGGGS | Human Lymphotoxin beta (Gln49-Gly244) Accession # Q06643-1 | GGGGS | Human Lymphotoxin beta (Gln49-Gly244) Accession # Q06643-1 | HHHHHH, Avi-tag | N-terminus | | | | | | |
|
Accession # |
|
N-terminal Sequence |
Leu35 |
Structure / Form |
GS-linked heterotrimer, biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
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
Dilutions |
|
Theoretical MW |
63 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 |
69-80 kDa |
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 Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in 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 Avi Protein, CF
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).
- Lu, T.T. and J.L. Browning (2014) Front. Immunol. 5:47.
- Upadhyay, V. and Y.-X. Fu (2014) Cytokine Growth Factor Rev. 25:227.
- Gray, P.W. et al. (1984) Nature 312:721.
- Nedwin, G.E. et al. (1985) J. Cell Biochem. 29:171.
- Browning, J.L. et al. (1993) Cell 72:847.
- Schoenfeld, H.J. et al. (1991) J. Biol. Chem. 266:3863.
- Mauri, D.N. et al. (1998) Immunity 8:21.
- Hashimoto, T. et al. (2008) Cell Cycle 7:106.
- De Togni, P. et al. (1994) Science 264:703.
- Kruglov, A.A. et al. (2013) Science 342:1243.
- Androlewicz, M.J. et al. (1992) J. Biol. Chem. 267:2542.
- Sudhamsu, J. et al. (2013) Proc. Natl. Acad. Sci. USA 110:19896.
- Crowe, P.D. et al. (1994) Science 264:707.
- Eldredge, J. et al. (2006) Biochemistry 45:10117.
- Futterer, A. et al. (1998) Immunity 9:59.
- Koni, P.A. et al. (1997) Immunity 6:491.
- Ota, N. et al. (2011) Nat. Immunol. 12:941.
- Young, J. et al. (2010) Cytokine 51:78.
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