siSTABLE Cyclophilin B Control siRNA - Mouse

A validated positive control siRNA with stabilizing modifications for use in vivo and other experimental settings with high nuclease activity. Silences mouse cyclophilin B.

siSTABLE Cyclophilin B Control siRNA is a validated positive control, guaranteed to silence cyclophilin B in mouse cells. This control siRNA is chemically modified to significantly extend siRNA stability and is recommended for use as a positive control in experiments using siSTABLE-modified siRNA against a target gene or where increased stability of the siRNA is desired.

Also known as peptidylprolyl isomerase B (PPIB), cyclophilin B is associated with the secretory pathway. This gene is abundantly expressed in most cells, and because it is non-essential, knockdown of the corresponding mRNA does not affect cell viability. Targets accession number NM_011149.


  • Experimentally validated for consistent, potent silencing of cyclophilin B in mouse cells
  • Chemically modified to significantly extend siRNA stability
  • Suitable for use in experimental settings with high nuclease activity, including in vivo studies
To request a larger quantity or in vivo processing of this control product, please email Technical Support, or call 1-800-235-9880. International customers, please call 303-604-9499 or your local Sales Representative.
Shipping ConditionAmbient
Stability at Recommended Storage ConditionsAt least 12 months
Storage Condition-20 C
Stability in 100% serum

Stability of siSTABLE siRNA in 100% Human Serum

Stability in 100% serum

The siSTABLE modification pattern dramatically extends the half-life of siRNA in the presence of 100% human serum. Unmodified siRNA degrades almost immediately while siSTABLE siRNA maintains integrity for up to 5 days.

Potent PPIB silencing

Potent Silencing by siSTABLE Cyclophilin B siRNA

Potent PPIB silencing

Western analysis of Cyclophilin B protein in HeLa cells was performed 96 and 120 hours after transfection with 100 nM of the indicated siRNAs: siSTABLE Non-Targeting siRNA #1 (D-001700-01, Lanes 1 and 4), siGENOME Cyclophilin B siRNA (D-001136-01, Lanes 2 and 5), and siSTABLE Cyclophilin B siRNA (D-001710-02, Lanes 3 and 6). Transfections were performed in 96-well plates with 5 x 103 cells/well and 0.2 µL DharmaFECT 1/well.


  1. siSTABLE siRNA in vivo:

    S. Cabodi et al., p130Cas is an essential transducer element in ErbB2 transformation. FASEB J. 24(10), 3796-3808 (October 2010).

  2. N. C. Henderson et al., Galectin-3 regulates myofibroblast activation and hepatic fibrosis. PNAS. 103(13), 5060-5065 (28 March 2006).
  3. K. Hocherl et al., Inhibition of NF-kB ameliorates sepsis-induced downregulation of aquaporin-2/V 2 receptor expression and acute renal failure in vivo. Am J Physiol Renal Physiol. 298(1), F196-F204 (January 2010).
  4. S. D. Larson et al., Effectiveness of siRNA uptake in target tissues by various delivery methods. Surgery. 142(2), 262-269 (August 2007).
  5. M. Snapyan et al., Vasculature guides migrating neuronal precursors in the adult mammalian forebrain via brain-derived neurotrophic factor signaling. J. Neurosci. 29(13), 4172-4188 (1 April 2009).
  6. S. Van de Veire et al., Further pharmacological and genetic evidence for the efficacy of PIGF inhibition in cancer and eye disease. Cell. 141(1), 178-190 (2 April 2010).
  7. J. C. Wang et al., Attenuation of fibrosis in vitro and in vivo with SPARC siRNA. Arthritis Res & Therapy. 12(2), R60 (2010).
  8. B. Yang et al., MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress p53-dependent apoptosis in MAGE-positive cell lines. Cancer Res. 67(20), 9954-9962 (15 October 2007).
  9. D. Bartlett, M. Davis, Insights into the kinetics of siRNA-mediated gene silencing from live-cell and liveanimal bioluminescent imaging. Nucleic Acids Res. 34(1), 322-333 (12 January 2006).
  10. J. M. Li et al., Local arterial nanoparticle delivery of siRNA for NOX2 knockdown to prevent restenosis in an atherosclerotic rat model. Gene Therapy. 17(10), 1279-1287 (October 2010).
  11. B. Maier et al., The unique hypusine modification of eIF5A promotes islet B cell inflammation and dysfunction in mice. J Clin Invest. 120(6), 2156-2170 (June 2010). [doi: 10.1172/JCI38924]
  12. N. Mambetsariev et al., Hyaluronic acid binding protein 2 is a novel regulator of vascular integrity. Arterioscler Thromb Vasc Biol. 30(3), 483-490 (March 2010).
  13. T. Mirzapoiazova et al., The non muscle myosin light chain kinase isoform is a viable molecular target in acute inflammatory lung injury. Am J Respir Cell Mol Biol. 44(1), 40-52 (2011).
  14. R. Natarajan et al., Activation of hypoxia-inducible factor-1 via prolyl-4 hydoxylase-2 gene silencing attenuates acute inflammatory responses in postischemic myocardium. Am J Physiol Heart Circ Physiol. 293(3), H1571-H1580 (September 2007).
  15. K. Niizuma et al., The PIDDosome mediates delayed death of hippocampal CA1 neurons after transient global cerebral ischemia in rats. PNAS. 105(42), 16368-16373 (2008).
  16. S. W. Park et al., Sphinganine-1 phosphate protects kidney and liver after hepatic ischemia and reperfusion in mice through S1P1 receptor activation. Lab Invest. 90(8), 1209-1224 (August 2010).
  17. M. Peters et al., RNA interference in hippocampus demonstrates opposing roles for CREB and PP1a in contextual and temporal long-term memory. Genes, Brain, and Behavior. 8(3), 320-329 (April 2009).
  18. C. Schmidt et al., Role of nuclear factor-kappaB-dependent induction of cytokines in the regulation of vasopressin V1A-receptors during cecal ligation and puncture-induced circulatory failure. Crit Care Med. 36(8), 2363-2372 (August 2008).
  19. P. Singleton et al., High-moleculer-weight hyaluronan is a novel inhibitor of pulmonary vascular leakiness. Am J Physiol Lung Cell Mol Physiol. 299, L639-L651 (2010).