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p-CaM I Antibody (Thr 117)-R: sc-17022-R

 |  Datasheet

(Based on data analysis)
  • p-CaM I (Thr 117)-R Antibody is a rabbit polyclonal IgG provided at 200 µg/ml
  • recommended for detection of Thr 117 phosphorylated CaM I of mouse, rat and human origin by WB and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
  • blocking peptide, sc-17022 P
 

See additional CaM Antibodies.

Also see CaM Inhibitors for functional analysis of cellular responses to CaM.


Ordering Information
Recommended Support Products:
(click button of application of choice)
WB   siRNA  
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 Ordering Information
Product NameCatalog #UnitPriceQtyAdd 
p-CaM I (Thr 117) P sc-17022 P
(peptide)
 100 µg/0.5 ml $61
p-CaM I (Thr 117)-R Antibody sc-17022-R 200 µg/ml $279
 siRNA Gene Silencers (click product name for more information)
Product NameCatalog #UnitPriceQtyAdd 
CaM I siRNA (h) sc-29896 10 µM $258
CaM I siRNA (m) sc-29897 10 µM $258
CaM I (h)-PR sc-29896-PR 10 µM, 20 µl $23
CaM I (m)-PR sc-29897-PR 10 µM, 20 µl $23
 shRNA Plasmids (click product name for more information)
Product NameCatalog #UnitPriceQtyAdd 
CaM I shRNA Plasmid (h) sc-29896-SH 20 µg $520
CaM I shRNA Plasmid (m) sc-29897-SH 20 µg $520
 shRNA Lentiviral Particles (click product name for more information)
Product NameCatalog #UnitPriceQtyAdd 
CaM I shRNA (h) Lentiviral Particles sc-29896-V 200 µl $625
CaM I shRNA (m) Lentiviral Particles sc-29897-V 200 µl $625

The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in the calcium level can result in a myriad of physiological responses, most of which are mediated by calmodulin. Calmodulin (CaM), a 148-amino acid universal calcium sensor, directly modulates the activity of protein kinases and phosphatases, ion channels and nitric oxide synthetases. Approximately 15% of CaM in the cell is phosphorylated and this phospho-rylation is mediated by casein kinase II on Thr 79, Ser 81, Ser 101 and Thr 117. Although CaM is constitutively phosphorylated, insulin increases phosphate incorporation into serine, threonine and tyrosine residues in intact cells. Phosphocalmodulin (p-CaM) exhibits altered biological activity. For example, p-CaM reduces activation of the erythrocyte plasma membrane Ca2+ pump. This strongly suggests that phosphorylation of CaM is an important component of intracellular signaling.