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Render Timestamp: 2024-11-22T11:51:18.454Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-30 10:37:11.838
Product last modified at: 2024-08-31T07:01:08.954Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

TRAIL (C92B9) Rabbit mAb (BSA and Azide Free) #48318

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  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 28-30
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    This product is the carrier free version of product #3219. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

    This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

    BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

    Formulation

    Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

    For standard formulation of this product see product #3219

    Storage

    Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Specificity / Sensitivity

    TRAIL (C92B9) Rabbit mAb (BSA and Azide Free) detects endogenous levels of total human TRAIL protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys60 of human TRAIL, within the extracellular region of the protein.

    Background

    Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL), also referred to as Apo2 ligand, first identified based on its sequence homology to TNF and Fas/Apo ligand is a member of the TNF family of cytokines and either exists as a type II membrane or soluble protein (1,2). TRAIL induces apoptosis in a variety of transformed cell lines and plays a role in anti-tumor and anti-viral immune surveillance (3). TRAIL signals via binding with death receptors DR4 (TRAIL-R1) (4) and DR5 (TRAIL-R2) (5-8) which can trigger apoptosis as well as NF-κB activation (7,9). Death domains on these receptors leads to the recruitment of a death-induced signaling complex (DISC) leading to caspase-8 and subsequent caspase-3 activation. In addition, TRAIL binds with decoy receptors DcR1 (TRAIL-R3) (6,8,10,11) and DcR2 (TRAIL-R4, TRUNDD) (12,13) which lack the functional cytoplasmic death domain antagonizing TRAIL-induced apoptosis. Osteoprotegerin (OPG) has also been identified as receptor capable of inhibiting TRAIL-induced apoptosis (14). The selectivity of soluble TRAIL at triggering apoptosis in transformed cells as compared to normal cells has led to its investigation as a potential cancer therapeutic (15,16).
    1. Wiley, S.R. et al. (1995) Immunity 3, 673-82.
    2. Pitti, R.M. et al. (1996) J Biol Chem 271, 12687-90.
    3. Almasan, A. and Ashkenazi, A. Cytokine Growth Factor Rev 14, 337-48.
    4. Pan, G. et al. (1997) Science 276, 111-3.
    5. Walczak, H. et al. (1997) EMBO J 16, 5386-97.
    6. MacFarlane, M. et al. (1997) J Biol Chem 272, 25417-20.
    7. Chaudhary, P.M. et al. (1997) Immunity 7, 821-30.
    8. Schneider, P. et al. (1997) FEBS Lett 416, 329-34.
    9. Shetty, S. et al. (2002) Apoptosis 7, 413-20.
    10. Sheridan, J.P. et al. (1997) Science 277, 818-21.
    11. Degli-Esposti, M.A. et al. (1997) J Exp Med 186, 1165-70.
    12. Pan, G. et al. (1998) FEBS Lett 424, 41-5.
    13. Marsters, S.A. et al. (1997) Curr Biol 7, 1003-6.
    14. Kelley, S.K. et al. (2001) J Pharmacol Exp Ther 299, 31-8.
    15. Walczak, H. et al. (1999) Nat Med 5, 157-63.
    16. Ashkenazi, A. et al. (1999) J Clin Invest 104, 155-62.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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