Anti-NAMPT mAb

  • Applications
    • ELISA
    • IP
  • Target NAMPT
  • Host Species Mouse
  • Species Reactivities Human
  • Code # CY-M1035
  • Size 100 µg
  • Price
    $401.02
Specifications

Alternative Names

Nicotinamide phosphoribosyltransferase, pre-B-cell colony-enhancing factor 1, PBEF, Visfatin

Background

Nicotinamide phosphoribosyltransferase (NAMPT), also known as pre-B-cell colony-enhancing factor, is the rate-limiting enzyme that converts nicotinamide to nicotinamide mononucleotide (NMN) from nicotinamide in the salvage pathway of NAD+ biosynthesis in mammals. Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) converts NMN to NAD+. The expression of NAMPT is upregulated during activation of immune cells such as monocytes, macrophages, dendritic cells, T and B cells, as well as in amniotic epithelial cells upon stimulation with several inflammatory cytokines. NAMPT-specific inhibitor, FK866 was found to deplete intracellular NAD content, resulting in apoptotic cell death in many cancer cell lines without any DNA damaging effect. Recently, Nakahata K et al, demonstrated that NAMPT is required to modulate circadian gene expression and circadian oscillation of NAD+.
  • Antibody Type:
    Monoclonal
  • Application:
    ELISA, IP
  • Clone Number:
    AF-1E12
  • Concentration:
    1.0 mg/mL
  • Conjugate:
    Unlabeled
  • Description:

    Monoclonal Antibody of 100 µg targeting NAMPT for ELISA, IP.

  • Formulation:
    Supplied in 20mM phosphatase buffer (pH 7.5), 300mM NaCl, 50% glycerol.
  • Host Species:
    Mouse
  • Immunogen:
    His-tagged human NAMPT
  • Isotype:
    IgG2a
  • Product Type:
    Antibody
  • Research Area:
    Immunology
  • Short Description:

    Anti-NAMPT Monoclonal Antibody.

  • Size:
    100 µg
  • Species Reactivity:
    Human
  • Storage Temperature:
    -20°C
  • Target:
    NAMPT
References
  1. Revollo, J. R, Grimm, A. A, Imai, S. (2004) J. Biol. Chem. 279: 50764-50763, 2004.
  2. Rongvaux A, Shea RJ, Mulks MH, Gigot D, Urbain J, et al. (2002) Eur J Immunol 32: 3225–3234.
  3. Iqbal J, Zaidi M (2006) Biochem Biophys Res Commun 342: 1312–1318.
  4. Nau GJ, Richmond JF, Schlesinger A, Jennings EG, Lander ES, et al. (2002) Proc Natl Acad Sci 99: 1503–1508.
  5. Huang Q, Liu D, Majewski P, Schulte LC, Korn JM, et al. (2001) Science 294: 870–875.
  6. Ognjanovic S, Bao S, Yamamoto SY, Garibay-Tupas J, Samal B, et al. (2001) J Mol Endocrinol 26: 107–117.7. Max Hasmann and Isabel Schemainda (2003) Cancer Res. 63: 7436 - 7442.
  7. M. Hasmann and I. Schemainda (2003) Cancer Res. 63, 7436-7442.
  8. Kathryn Moynihan Ramsey, et al. (2009) Science 324, 651
  9. Yasukazu Nakahata, et al. (2009) Science 324, 654