Synthetic phosphopeptide derived from human CPI-17 around the phosphorylation site of Threonine 38.
Conjugation:
Unconjugated
Alternative Names:
Protein phosphatase 1 regulatory subunit 14A, 17 kDa PKC-potentiated inhibitory protein of PP1, Protein kinase C-potentiated inhibitor protein of 17 kDa, CPI-17, CPI17, PPP1INL, PPP1R14A
CPI-17 is a phosphorylation-dependent inhibitory protein for smooth muscle myosin phosphate. CPI-17 was originally identified as a PKC-potentiated inhibitory protein of protein phosphatase-1, which is dominantly expressed in smooth muscle. Phosphorylation at Threonine 38, in vitro, by PKC or Rho-kinase enhances the inhibitory potency toward myosin phosphatase. CPI-17 is also phosphorylated at Threonine 38 by protein kinase N and might be involved in the calcium sensitization of smooth muscle contraction as a downstream effector of Rho and/or arachidonic acid. CPI-17 is dually phosphorylated at Serine 12 and Threonine 38 by a MYPT-associated kinase, M110 kinase.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-CPI-17 (T38) polyclonal antibody detects endogenous levels of CPI-17 polyclonal antibody protein only when phosphorylated at Thr38.
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