|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||19011 Da|
|Other Names||Protein phosphatase 1 regulatory subunit 1A, Protein phosphatase inhibitor 1, I-1, IPP-1, PPP1R1A, IPP1|
|Target/Specificity||A synthetic peptide corresponding to residues in the N-terminus of human IPP-1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||IPP-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases.|
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Provided below are standard protocols that you may find useful for product applications.
The inhibitor of protein phosphatase 1 (IPP-1, I-1) is an endogenous inhibitor of protein phophastase 1 (PP-1), a signal transducer in many cellular pathways. IPP-1 is a member of heat-stable PP1 inhibitory subunits, which includes DARPP-32, (a homologue of IPP-1) and IPP-2. First discovered in rabbit skeletal muscle, IPP-1 is expressed in various mammalian tissues. IPP-1 inhibition of PP-1 is controlled through phosphorylation at Thr35 by cAMP-dependent protein kinase and a tetra-peptide consensus motif in various PP-1 binding proteins (1). IPP-1 is a hormonal control in muscle contraction, pituitary cell growth, synaptic plasticity by neurotransmitters, and glycogen metabolism (2). In vivo, IPP-1 is phosphorylated at Ser-67 by NCLK, which also initiates inhibition of PP-1 by IPP-1 (3). Triggered by increase in calcium level, IPP-1 is inactivated by PP2B through de-phosphorylation (4).
1. Egloff MD, et al. EMBO J 16:1876-1887, 1997.
2. Oliver CJ, Shenolikar S, Front Biosci 3:D961-972, 1998.
3. Huang K, Paudel HK, PNAS 97:5824-5829, 2000.
4. Castellani GC, Learn Mem 12:423-432, 2005.
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