Recombinant Cyno/Rhesus APRIL/TNFSF13 HA Tag Protein, CF Summary
| Details of Functionality |
Measured in a cell proliferation assay using anti-IgM stimulated mouse B cells. The
ED50 for this effect is 2.50-30.0 ng/mL in the presence of goat
anti-mouse IgM. |
| Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey APRIL/TNFSF13 protein HA (YPYDVPDYA) | GCN4-IZ | GS Linker | Cyno/Rhesus APRIL (Ala 105-Leu 250) Accession # XP_005582818.1 | | N-terminus | | | C-terminus | |
|
| N-terminal Sequence |
Tyr of HA tag |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>90%, 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 |
22 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 |
24-28 kDa, under reducing conditions |
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 Tris and NaCl with Trehalose. See Certificate of Analysis for details. |
| Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 200 μg/mL in water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cyno/Rhesus APRIL/TNFSF13 HA Tag Protein, CF
Background
APRIL (a proliferation-inducing ligand), also known as TNFSF13, TALL2, TRDL1, and CD256, is a member of the TNF ligand superfamily (1). It is synthesized as a 32 kDa proprotein which is cleaved by furin in the Golgi to release the active 17 kDa soluble molecule (2-4). Secreted cyno/rhesus APRIL, which consists almost entirely of a single TNF homology domain, shares 98.6% amino acid sequence identity with human and rat APRIL. Both APRIL and its close relative BAFF bind and signal through the TNF superfamily receptors TACI and BCMA, while BAFF additionally functions through BAFF R (2, 5, 6). APRIL binds to heparan sulfate proteoglycans (HSPGs) independently of its binding to TACI and BCMA (6, 7). The interaction with HSPGs induces APRIL oligomerization, and this augments TACI-, or BMCA-mediated effects (7, 8). HSPGs are also critical for the tumor growth-promoting effects attributed to APRIL (6). APRIL can form bioactive heterotrimers with BAFF, and these circulate in the serum of patients with rheumatic immune disorders (10). TWE-PRIL is a bioactive hybrid protein produced by gene splicing. It consists of the intracellular domain, transmembrane segment, and stalk region of TWEAK fused to the TNF homology domain of APRIL (11). TWE-PRIL is expressed in monocytes and activated T cells and, in contrast to APRIL, is presented on the cell surface (11). APRIL enhances the proliferation and survival of plasma cells and also promotes T cell-dependent humoral responses (2, 12, 13). In the context of autoimmune disorders, however, APRIL can inhibit pathologic humoral responses as well as disease progression (14). Its expression by CD4
+ T cells inhibits the production of Th2 cytokines and allergic inflammation (15). APRIL levels are elevated in the serum during coronary artery disease (16), and it is also elevated in many cancers primarily due to expression by tumor-infiltrating neutrophils (4, 7, 17).
- Planelles, L. et al. (2008) Curr. Mol. Med. 8:829.
- Yu, G. et al. (2000) Nat. Immunol. 1:252.
- Lopez-Fraga, M. et al. (2001) EMBO Reports 2:945.
- Kelly, K. et al. (2000) Cancer Res. 60:1021.
- Day, E.S. et al. (2005) Biochemistry 44:1919.
- Bossen, C. et al. (2006) J. Biol. Chem. 281:13964.
- Hendriks, J. et al. (2005) Cell Death Differ. 12:637.
- Schwaller, J. et al. (2007) Blood 109:331.
- Ingold, K. et al. (2005) J. Exp. Med. 201:1375.
- Roschke, V. et al. (2002) J. Immunol. 169:4314.
- Pradet-Balade, B. et al. (2002) EMBO J. 21:5711.
- Benson, M.J. et al. (2008) J. Immunol. 180:3655.
- He, B. et al. (2004) J. Immunol. 172:3268.
- Fernandez, L. et al. (2012) Ann. Rheum. Dis. 72:1367.
- Xiao, Y. et al. (2011) Eur. J. Immunol. 41:164.
- Sandberg, W.J. et al. (2009) Thromb. Haemost. 102:704.
- Mhawech-Fauceglia, P. et al. (2008) Eur. J. Cancer 44:2097.
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