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Small interfering RNA/silencing RNA (siRNA) is a class of double-stranded, non-coding RNA molecule, 20-25 base pairs in length. As part of the RNA interference pathway, it regulates gene expression by degrading mRNA after transcription, preventing translation.
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Enables polyubiquitin modification-dependent protein binding activity Involved in protein linear polyubiquitination and regulation of signal transduction Located in cytosol Part of LUBAC complex
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STIP1 Homology And U-Box Containing Protein 1 Primary Antibody Unconjugated Public Immunogen Range 1-51/303 Host Species Rabbit Target Species Human Mouse Rat Clonality Monoclonal Applications WB FCM IC Concentration Lot dependent Size 50 ul Storage Buffer Supplied in PBS (pH 7 4) containing 50% glycerol and 0 02% sodium azide
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Dyneins are a group of microtubule-activated ATPases that function as molecular motors They are divided into two subgroups of axonemal and cytoplasmic dyneins The cytoplasmic dyneins function in intracellular motility including retrograde axonal transport protein sorting organelle movement and spindle dynamics Molecules of conventional cytoplasmic dynein are comprised of 2 heavy chain polypeptides and a number of intermediate and light chains This gene encodes a member of the cytoplasmic dynein heavy chain family
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This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.
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