siSTABLE Non-targeting siRNA #1


A negative control siRNA with stabilizing modifications for use in vivo and other experimental settings with high nuclease activity. Does not target any known human, mouse, or rat genes.
siSTABLE Non-Targeting siRNA #1 was designed to have a minimum of four mismatches to all human, mouse, and rat genes to avoid non-specific silencing due to off-targets. This negative control siRNA is chemically modified to significantly extend siRNA stability an is recommended for use as a negative control in experiments using siSTABLE modified siRNA against a target gene or where increased stability of the control is desired.

Highlights

  • BLAST analysis confirms at least 4 mismatches with all known human, mouse, and rat genes
  • Chemically modified to significantly extend siRNA stability
  • Recommended for use as a non-specific control in experiments using siSTABLE modified siRNA against the target gene or where increased stability of the control is desired

Experimental considerations

siRNA-mediated RNAi experiments should include non-targeting siRNA as a control for non-sequence-specific effects. Changes in mRNA or protein levels in cells or tissues treated with these controls reflect a non-specific baseline cellular response to which the levels in cells or tissues treated with target-specific siRNA can be compared.

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.

  
HazardousNo
Shelf Life12 Months
Shipping ConditionAmbient
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.


Citations

  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).