|Application ||WB, IF, ICC, E|
|Other Accession||AAB82297, 2570925|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||31585 Da|
|Application Notes||SIP1 antibody can be used for detection of SIP1 by Western blot at 0.5 - 1 µg/mL. Antibody can also be used for immunocytochemistry starting at 4 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Reconstitution & Storage||SIP1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||SIP1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.|
|Cellular Location||Nucleus, gem. Cytoplasm. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm|
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Provided below are standard protocols that you may find useful for product applications.
SIP1 Antibody: SIP1 is one of the proteins found in the SMN complex, which consists of the survival of motor neuron (SMN) protein and several gemin proteins. The SMN complex is localized to a subnuclear compartment called gems (gemini of coiled bodies) and is required for assembly of spliceosomal snRNPs and for pre-mRNA splicing. SIP1 interacts directly with the SMN and it is required for formation of the SMN complex. A knockout mouse targeting the mouse homolog of this gene exhibited disrupted snRNP assembly and motor neuron degeneration. However, knockdown of the SIP1 mRNA in motor neurons showed normal motor axons while that of SMN mRNA did show abnormal motor axon outgrowth, indicating that SIP1 may have additional roles outside of the SMN complex.
Liu Q, Fischer U, Wang F, et al. The spinal muscle atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell1997; 90:1013-21.
Ogawa C, Usui K, Aoki M, et al. Gemin2 plays an important role in stabilizing the survival of motor neuron complex. J. Biol. Chem.2007; 282:11122-34.
Jablonka S, Holtmann B, Meister G, et al. Gene targeting of Gemin2 in mice reveals a correlation between defects in the biogenesis of U snRNPs and motoneuron cell death. Proc. Natl. Acad. Sci. USA2002; 99:10126-31.
McWhorter ML, Boon KL, Horan ES, et al. The SMN binding protein Gemin2 is not involved in motor axon outgrowth. Dev. Neurobiol.2008; 68:182-94.
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