Recombinant Human Gem-associated protein 7 (GEMIN7)

Category: Proteins
Catalog
CSB-EP862039HU
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Product Name Recombinant Human Gem-associated protein 7 (GEMIN7)
Description The SMN complex plays a catalyst role in the assbly 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 assble 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 assbly 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 assbly of core snRNPs and their transport to the nucleus.
Synonyms SIP3
Host E.coli
Molecular Weight 41.5
Amino Acid Sequence MQTPVNIPVPVLRLPRGPDGFSRGFAPDGRRAPLRPEVPEIQECPIAQESLESQEQRARAALRERYLRSLLAMVGHQVSFTLHEGVRVAAHFGATDLDVANFYVSQLQTPIGVQAEALLRCSDIISYTFKP
Protein Length Full Length, 1-131aa
Tag N-terminal GST-tagged
Reactivity Human
Applications SDS-PAGE
Form Liquid, in Tris-based buffer, 50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
References Identification and characterization of Gemin7, a novel component of the survival of motor neuron complex.Baccon J., Pellizzoni L., Rappsilber J., Mann M., Dreyfuss G.J. Biol. Chem. 277:31957-31962(2002)
Background The SMN complex plays a catalyst role in the assbly 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 assble 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 assbly 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 assbly of core snRNPs and their transport to the nucleus.
Supplier Cusabio

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