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C2548-84N3 Hamster Anti-CD154 (CD40 Ligand, Cd40l, CD40-L, Cd40lg, sCD40L, HIGM1, IGM, IMD3, Ly62, Ly-62, T-BAM, T-cell Antigen Gp39, TNF-related Activation Protein, TRAP, Tumor Necrosis Factor Ligand Superfamily Member 5, Tnfsf5) (Biotin)

Specifications
References
Clone Type
Monoclonal
Host
Hamster
Source
Mouse
Conjugate
Biotin
Isotype
IgG,k
Clone Number
MR1
Grade
Purified
Applications
FC IP
Crossreactivity
Mo
Shipping Temp
Blue Ice
Storage Temp
4°C (-20°C Glycerol)

CD154, formerly known as CD40 ligand and gp39, is a type II integral membrane protein and a member of the tumor necrosis factor (TNF) family of ligands.1-7 It is an important accessory molecule in T cell-B cell costimulatory interactions, and is expressed predominantly on activated CD4+ T lymphocytes. It is also present on the surface of activated Th0, Th1, and Th2 T cell clones. Its expression is transient and cyclosporinsensitive.

Applications
Suitable for use in Flow Cytometry, Immunoprecipitation and In vivo and in vitro blockage of CD154 function. Other applications have not been tested.
Recommended Dilution
Flow Cytometry: ≤2ug/10e6 cells Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile 40-50% glycerol, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Immunogen
Activated mouse Th1 clone D1.6
Form
Supplied as a liquid in PBS, 0.09% sodium azide. Labeled with Biotin.
Purity
Purified
Specificity
Recognizes mouse CD154 (mouse CD40 ligand/gp39), Mr 39kD. Binds to murine CD154 with high affinity, blocks binding to CD40, and blocks CD154 function. Administration to mice blocks the ability to mount primary and secondary immune responses to TD antigens, yet does not alter the immune response to TI antigens.
References
1. Noelle, R.J., M. Roy, D.M. Shepherd, I Stamenkovic, J.A. Ledbetter, and A. Aruffo. 1992. Proc. Natl. Acad. Sci. U.S.A. 89:6550.2. Aruffo, A., M. Farrington, D. Hollenbaugh, X. Li, A. Milatovich, S. Nonoyama, J. Bajorath, L.S. Grosmaire, R. Stenkamp, and M. Neubauer. 1993. Cell 72:291.3. Hollenbaugh, D., L.S. Grosmaire, C.D. Kullas, N.J. Chalupny, S. Braesch-Andersen, R.J. Noelle, I. Stamenkovic, J.A. Ledbetter, and A. Aruffo. 1992. EMBO J. 11:4313.4. Foy, TM., DM Shepherd, F.H. Durie, A. Aruffo, J.A. Ledbeter, and R.J. Noelle. 1993. J. Exp. Med. 178:1567.5. Foy, T.M., D.M. page, T.J. Waldschmidt, A. Schoneveld, J.D. Laman, S.R. Masters, L. Tygrett, J.A. Ledbetter, A. Aruffo, and E. Claassen. 1995. J. Exp. Med. 182:1377.6. Roy, M., T.J. Waldschmidt, A. Aruffo, J.A. Ledbetter, and R.J. Noelle. 1993. J. Immunol. 151:2497.7. Armitage, R.J., W.C. Fanslow, L. Stockbine, T.A. Sato, K.N. Clifford, B.M. Macduff, D.M. Anderson, S.D. Gimpel, T. Davis-Smith, and C.R. Maliszewski. 1992. Nature 357:80.
USBio References
No references available
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