Host: Insect cells • AA: 1-634 (full-length) • Tag: N-terminal His-GST • MW: 100 kDa
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PDE1C1 (human, recombinant)

Item No. 32042

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 3',5'-cyclic-AMP Phosphodiesterase 1C1
  • 3',5'-cyclic-GMP Phosphodiesterase 1C1
  • Calcium/Calmodulin-dependent 3',5'-cyclic Nucleotide Phosphodiesterase 1C1
  • Cam-PDE1C1
  • Phosphodiesterase 1C1
  • HCam3a
Purity
≥85 % as determined by SDS-PAGE
Endotoxin Testing
<1.0 EU/μg, determined by the LAL endotoxin assay
Source
Recombinant human N-terminal His-GST-tagged PDE1C1 expressed in insect cells
Amino Acids
1-634 (full length)
MW
100 kDa
Formulation (Request formulation change)
Lyophilized from sterile 20 mM Tris, 500 mM sodium chloride, pH 7.4, with 10% glycerol and 3 mM DTT
UniProt Accession №
Q8TAE4
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    50 µg

    $361

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    Cayman Chemical
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    Product Description

    Phosphodiesterase 1C (PDE1C) is a calcium/calmodulin-dependent PDE that hydrolyzes cAMP and cGMP.1,2 Alternative splicing of PDE1C produces three isoforms that exhibit isoform-specific tissue distribution and domain structure.1 PDE1C isoforms all contain a calcium/calmodulin binding region and a PDE catalytic domain but vary in carboxyterminal length.3 PDE1C1 is a 72 kDa isoform that is primarily expressed in the heart and brain but is also expressed in the lungs, uterus, and testes. PDE1C1 is expressed in MAA human malignant melanoma cells.4 Hippocampal PDE1C1 expression is increased in aged rats.5 Cayman’s PDE1C1 (human, recombinant) protein consists of 871 amino acids and has a calculated molecular weight of 100 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Loughney, K., Martins, T.J., Harris, E.A.S., et al. Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. The Journal of Biological Chemisty 271(2), 796-806 (1996).

    2. Yan, C., A.Z., Z., Bentley, J.K., et al. The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner. The Journal of Biological Chemisty 271(41), 25699-25706 (1996).

    3. Loughney, K., and Ferguson, K. Identification and quantification of PDE isoenzymes and subtypes by molecular biological methods. The Handbook of Immunopharmacology 1-19 (1996).

    4. Shimizu, K., Murata, T., Watanabe, Y., et al. Characterization of phosphodiesterase 1 in human malignant melanoma cell lines. Anticancer Res. 29(4), 1119-1122 (2009).

    5. Kelly, M.P., Adamowicz, W., Bove, S., et al. Select 3′,5′-cyclic nucleotide phosphodiesterases exhibit altered expression in the aged rodent brain. Cell Signal. 26(2), 383-397 (2014).