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PPP1R3B Antibody (C-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q86XI6
Clone Names 110726167
Additional Information
Gene ID 79660
Other Names Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R3B, PPP1R4
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name PPP1R3B
Synonyms PPP1R4
Function Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity).
Tissue Location Highly expressed in the liver and, at lower levels, in skeletal muscle, including in vastus lateralis, gastrocnemius and soleus (at protein level). Highest mRNA levels are observed in skeletal muscle, and only moderate levels in liver and heart. Weak expression in placenta and lung.
Research Areas
Citations (0)
citation

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Background

The protein phosphatase-1 (PP1) catalytic subunit (PPP1CA;MIM 176875) is regulated by targeting subunits, such as PP1R3B.PP1R3B suppresses the rate at which PP1 dephosphorylates (i.e.,inactivates) glycogen phosphorylase (see PYGL; MIM 232700) andenhances the rate at which it activates glycogen synthase (seeGYS2; MIM 138571) (Doherty et al., 1995 [PubMed 7498521]).[suppliedby OMIM].

References

Montori-Grau, M., et al. Biochem. J. 405(1):107-113(2007)Lamesch, P., et al. Genomics 89(3):307-315(2007)Ceulemans, H., et al. Bioessays 24(4):371-381(2002)Doherty, M.J., et al. FEBS Lett. 375(3):294-298(1995)

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$ 277.78
Cat# BP18235b
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