TRAIL, Recombinant, Mouse (TNF-Related Apoptosis Inducing Ligand, Apo2 Ligand) (BSA Free)

TNF-related apoptosis-inducing ligand (TRAIL), also called apoptosis 2 ligand (Apo2L) for its similarity in sequence, structure, and function to Fas Ligand/Apo1L, is a 33-35 kD type II transmembrane glycoprotein of the tumor necrosis factor superfamily, designated TNFSF10 (1-3). Mouse TRAIL cDNA encodes a 17 amino acid (aa) N-terminal intracellular domain, a 20 aa transmembrane domain and a 253 aa extracellular domain. Like most TNF family members, TRAIL is bioactive as a homotrimer (1). Unlike other TNF family members, a zinc ion complexed by human Cys 230 (mouse Cys 240) of each of the three monomers is critical for structural stability (4, 5). Either transmembrane or cysteine protease-released soluble sTRAIL induce apoptosis of many transformed cell lines, but rarely of normal cells (3, 6). Accordingly, TRAIL is suggested to have a role in tumor surveillance (1). Mice with genetically disrupted TRAIL have defective thymocyte apoptosis, creating faulty negative selection and some increased susceptibility to induced autoimmune diseases (7). In humans, TRAIL controls apoptosis of erythrocyte precursors and sTRAIL is inversely correlated with hemoglobin (1, 8). TRAIL transcripts are constitutively expressed in a variety of human (and presumably mouse) tissues and mononuclear cells (2, 3). Only one of two receptors that transduce apoptotic signals in humans is found in the mouse (TRAIL R2/DR5 but not TRAIL R1/DR4) (1). Mice express TRAIL receptors DcTRAIL R1/TNFRSF23 and DcTRAIL R2/TNFRSF22. These receptors lack death domains, but differ in structure from human regulatory receptors TRAIL R3 and TRAIL R4 (9). Osteoprotegerin has been identified in humans as a TRAIL receptor, but binding in mouse has not yet been demonstrated (1, 10). Mouse TRAIL shows 85% aa identity with rat TRAIL and 70% aa identity with human, bovine, and porcine TRAIL within the TNF homology domain (aa 118-291).\n\nSource: A DNA sequence encoding the extracellular domain of mouse TRAIL (Pro 118-Asn 291; Accession # P50592) (Wiley, S.R. et al., 1995, Immunity 3:673) was expressed in E. coli.\n\nMolecular Mass: The recombinant mouse TRAIL elutes as a homotrimeric protein in chromatography on a sizing column. The monomer contains 174 amino acid residues and has a predicted molecular mass of approximately 20kD.\n\nEndotoxin Level: < 1.0 EU per 1 microg of the protein as determined by the LAL method.\n\nActivity: Measured by its ability to induce cytotoxicity in the mouse L929 cell line in the presence of the metabolic inhibitor actinomycin D (Matthews, N. et al., 1987, in Lymphokines and Interferons, a Practical Approach, M.J. Clemens, A.G. Morris, and A.J.H. Gearing, eds., IRL Press, p. 221). The ED50 for this effect is typically 1.5-9.0 ng/mL.\n\nReconstitution: It is recommended that sterile 4mM HCl be added to the vial to prepare a working stock solution of no less than 100ug/ml. The carrier-free protein should be used immediately upon reconstitution to avoid losses in activity due to non-specific binding to the inside surface of the vial. For long term storage as a dilute solution, a carrier protein (e.g. 0.1% HSA or BSA) should be added to the vial.\n\nStorage and Stability: Lyophilized samples are stable for up to twelve months at -20 degrees C. Upon reconstitution, this protein, in the presence of a carrier protein, can be stored under sterile conditions at 2 degrees -8 degrees C for 2 weeks or at -20 degrees C for one month in a manual defrost freezer without detectable loss of activity. Avoid repeated freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

T8180-04MX

Size

10ug

Form

Supplied as a lyophilized powder in 20mM Tris, 400mM ammonium sulfate, 10uM zinc sulfate, pH 7.5.

Purity

(same/more than) 95%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Zauli, G. and P. Secchiero, Cytokine Growth Factor Rev. 17:245. \n2. Wiley, S.R. et al., 1995, Immunity 3:673. \n3. Pitti, R.M. et al., 1996, J. Biol. Chem. 271:12687. \n4. Bodmer, J.L. et al., 2000, J. Biol. Chem. 275:20632. \n5. Hymowitz, S.G. et al., 2000, Biochemistry 39:633.\n6. Sedger, L. M. et al., 2002, Eur. J. Immunol. 32:2246. \n7. Lamhamedi-Cherradi, S.E. et al., 2003, Nat. Immunol. 4:255. \n8. Choi, J.W., 2005, Ann. Hematol. 84:728. \n9. Schneider, P. et al., 2003, J. Biol. Chem. 278:5444. \n10. Emery, J. et al., 1998, J. Biol. Chem. 273:14363.