SignalSilence® S100A4 siRNA I #12966
Important Ordering Details
Custom Ordering Details: Product is assembled upon order. Please allow up to three business days for your product to be processed.Supporting Data
| REACTIVITY | H |
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
CST recommends transfection with 100 nM SignalSilence® S100A4 siRNA I 48 to 72 hours prior to cell lysis. For transfection procedure, follow protocol provided by the transfection reagent manufacturer. Please feel free to contact CST with any questions on use.
Each vial contains the equivalent of 100 transfections, which corresponds to a final siRNA concentration of 100 nM per transfection in a 24-well plate with a total volume of 300 μl per well.
Storage
SignalSilence® siRNA is supplied in RNAse-free water. Aliquot and store at -20ºC.
Product Description
SignalSilence® S100A4 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit S100A4 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
Quality Control
Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
Background
Despite their relatively small size (8-12 kDa) and uncomplicated architecture, S100 proteins regulate a variety of cellular processes, such as cell growth and motility, cell cycle progression, transcription, and differentiation. To date, 25 members have been identified, including S100A1-S100A18, trichohyalin, filaggrin, repetin, S100P, and S100Z, making it the largest group in the EF-hand, calcium-binding protein family. Interestingly, 14 S100 genes are clustered on human chromosome 1q21, a region of genomic instability. Research studies have demonstrated that significant correlation exists between aberrant S100 protein expression and cancer progression. S100 proteins primarily mediate immune responses in various tissue types but are also involved in neuronal development (1-4).
Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cation in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4).
Research studies have shown that S100A4 is overexpressed in highly metastatic cancers, which makes it useful as a marker of tumor progression (5,6) and may serve as a prognostic factor in several cancer types (7-10). S100A4 exerts its function via direct interaction with a number of proteins including P53, P63, nonmuscle myosin IIA, α6β4 integrin, and liprin b1 (11-15). S100A4 is present in the nucleus, cytoplasm and extracellular space. Intracellular and extracellular S100A4 both promote cell migration via interaction with different proteins. Researchers have recently discovered that S100A4 also functions as a neuroprotectant in the peripheral nervous system (16,17).
Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cation in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4).
Research studies have shown that S100A4 is overexpressed in highly metastatic cancers, which makes it useful as a marker of tumor progression (5,6) and may serve as a prognostic factor in several cancer types (7-10). S100A4 exerts its function via direct interaction with a number of proteins including P53, P63, nonmuscle myosin IIA, α6β4 integrin, and liprin b1 (11-15). S100A4 is present in the nucleus, cytoplasm and extracellular space. Intracellular and extracellular S100A4 both promote cell migration via interaction with different proteins. Researchers have recently discovered that S100A4 also functions as a neuroprotectant in the peripheral nervous system (16,17).
- Heizmann, C.W. et al. (2002) Front Biosci 7, d1356-68.
- Donato, R. (2003) Microsc Res Tech 60, 540-51.
- Marenholz, I. et al. (2004) Biochem Biophys Res Commun 322, 1111-22.
- Santamaria-Kisiel, L. et al. (2006) Biochem J 396, 201-14.
- Ismail, N.I. et al. (2008) Cancer Cell Int 8, 12.
- Ismail, T.M. et al. (2010) J Biol Chem 285, 914-22.
- Rudland, P.S. et al. (2000) Cancer Res 60, 1595-603.
- Huang, L.Y. et al. (2011) World J Gastroenterol 17, 69-78.
- Wang, L.J. et al. (2012) Appl Immunohistochem Mol Morphol 20, 71-6.
- Kang, Y.G. et al. (2012) J Surg Oncol 105, 119-24.
- Kriajevska, M.V. et al. (1994) J Biol Chem 269, 19679-82.
- Takenaga, K. et al. (1994) J Cell Biol 124, 757-68.
- Kriajevska, M. et al. (2002) J Biol Chem 277, 5229-35.
- Kim, T.H. et al. (2009) Mol Cancer Res 7, 1605-12.
- van Dieck, J. et al. (2010) Oncogene 29, 2024-35.
- Dmytriyeva, O. et al. (2012) Nat Commun 3, 1197.
- Moldovan, M. et al. (2013) Mol Med 19, 43-53.
限制使用
除非 CST 的合法授书代表以书面形式书行明确同意，否书以下条款适用于 CST、其关书方或分书商提供的书品。 任何书充本条款或与本条款不同的客书条款和条件，除非书 CST 的合法授书代表以书面形式书独接受， 否书均被拒书，并且无效。
专品专有“专供研究使用”的专专或专似的专专声明， 且未专得美国食品和专品管理局或其他外国或国内专管机专专专任何用途的批准、准专或专可。客专不得将任何专品用于任何专断或治专目的， 或以任何不符合专专声明的方式使用专品。CST 专售或专可的专品提供专作专最专用专的客专，且专用于研专用途。将专品用于专断、专防或治专目的， 或专专售（专独或作专专成）或其他商专目的而专专专品，均需要 CST 的专独专可。客专：(a) 不得专独或与其他材料专合向任何第三方出售、专可、 出借、捐专或以其他方式专专或提供任何专品，或使用专品制造任何商专专品，(b) 不得复制、修改、逆向工程、反专专、 反专专专品或以其他方式专专专专专品的基专专专或技专，或使用专品开专任何与 CST 的专品或服专专争的专品或服专， (c) 不得更改或专除专品上的任何商专、商品名称、徽专、专利或版专声明或专专，(d) 只能根据 CST 的专品专售条款和任何适用文档使用专品， (e) 专遵守客专与专品一起使用的任何第三方专品或服专的任何专可、服专条款或专似专专
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
SignalSilence is a registered trademark of Cell Signaling Technology, Inc.
All other trademarks are the property of their respective owners. Visit our
Trademark Information page.