Anti-Phospho-Syntide-2 mAb

  • Applications
    • ELISA
  • Target Syntide-2
  • Host Species Mouse
  • Code # CY-M1023
  • Size 100 μg
  • Price
    $284.06
Specifications

Background

Syntide-2, a peptide based on phosphorylation site two of glycogen synthase, is an exogenous substrate designed for CaM-Kinase (calcium/calmodulin dependent kinases) in the serine-threonine kinase family. CaM-kinase II is a multifunctional calcium/calmodulin dependent protein kinase involved in neuronal functions. This anti-Phospho-Syntide-2 monoclonal antibody has been validated with CaM-kinase II, however it has the potential for use in evaluating other serine/threonine kinases such as CaM-Kinase IIa, PKCμ, Akt1, Akt2, Akt3, and PKA. The relative Vmax/Km ratios of the known Ca2+-dependent protein kinases for syntide-2 were determined to be as follows: protein kinase II, 100; protein kinase C, 22; phosphorylase kinase, 2; myosin light chain kinase, 0.005.
  • Antibody Type:
    Monoclonal
  • Application:
    ELISA
  • Clone Number:
    MS-6E6
  • Concentration:
    1.0 mg/mL
  • Conjugate:
    Unlabeled
  • Description:

    Monoclonal Antibody of 100 μg targeting Syntide-2 for ELISA.

  • Formulation:
    Supplied in 20mM phosphatase buffer (pH 7.5), 300mM NaCl, 50% glycerol.
  • Host Species:
    Mouse
  • Immunogen:
    a synthetic phosphopeptide Syntide-2 (PLARTL(pS)VAGLPGKK; synthetic substrate for CaM-Kinase II)
  • Isotype:
    IgG2b
  • Product Type:
    Antibody
  • Reactivity:
    Phospho-Syntide-2 Antibody detectsphosphorylated Syntide-2 only when phosphorylated atthe serine residue in vitro. The antibody does notrecognize the unphosphorylated substrate. The antibodydetects the phosphorylated Syntide-2 by ELISA.
  • Research Area:
    Cell Biology
  • Short Description:

    Anti-Phospho-Syntide-2 Monoclonal Antibody.

  • Size:
    100 μg
  • Storage Temperature:
    -20°C
  • Target:
    Syntide-2
References
  1. Hashimoto Y, Soderling TR. Calcium calmodulindependent protein kinase II and calcium phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide. Arch Biochem Biophys. 252:418-25, (1987)
  2. CM Schworer, RJ Colbran, and TR Soderling Reversible generation of a Ca2+-independent form of Ca2+(calmodulin)- dependent protein kinase II by an autophosphorylation mechanism. J. Biol. Chem. 261:8581 – 8584, (1986)