Recombinant Human Gemin6/SIP2 protein is a Human Full Length protein, in the 1 to 167 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M S E W M K K G P L E W Q D Y I Y K E V R V T A S E K N E Y K G W V L T T D P V S A N I V L V N F L E D G S M S V T G I M G H A V Q T V E T M N E G D H R V R E K L M H L F T S G D C K A Y S P E D L E E R K N S L K K W L E K N H I P I T E Q G D A P R T L C V A G V L T I D P P Y G P E N C S S S N E I I L S R V Q D L I E G H L T A S Q
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The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and 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 (Sm core). 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Gem-associated protein 6, Gemin-6, SIP2, GEMIN6
Recombinant Human Gemin6/SIP2 protein is a Human Full Length protein, in the 1 to 167 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 30% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab140556 was purified using conventional chromatography.
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and 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 (Sm core). 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Previously labelled as Gemin 6.
Gemin6 also known as SIP2 (Survival of Motor Neurons Interacting Protein 2) is a protein that plays a role in the assembly of small nuclear ribonucleoproteins (snRNPs). It has a molecular weight of approximately 39 kDa and is expressed mainly in the brain and spinal cord. This protein facilitates interactions within the SMN (Survival Motor Neuron) complex which is essential for the biogenesis of snRNPs necessary for pre-mRNA splicing.
Gemin6/SIP2 functions as a component of the SMN complex which is key to snRNP maturation and assembly. The SMN complex plays an important role in the cellular machinery responsible for processing pre-mRNA to mature mRNA. Gemin6/SIP2 binds specifically to core proteins in snRNPs aiding in their stability and function. It ensures accurate splicing of mRNA which is critical for proper gene expression and cellular function.
Several molecules are associated with the Gemin6/SIP2's role in spliceosomal snRNP assembly. It is involved in the pre-mRNA splicing pathway and links to the RNA transport pathway via the SMN complex. Proteins such as Gemin2 and Sm proteins relate closely to Gemin6/SIP2 through these pathways forming a functional network critical for RNA processing and regulation.
Gemin6/SIP2 has connections to neurodegenerative conditions such as spinal muscular atrophy (SMA). SMA is characterized by the loss of motor neurons which Gemin6/SIP2 influences through its function in the SMN complex. The dysfunction of this complex due to mutations or imbalances can contribute to the symptoms of SMA. Gemin6/SIP2 connects with SMN protein whose deficiency directly associates with the pathogenesis of SMA highlighting the significance of this protein in neurological health.
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15% SDS-PAGE analysis of ab140556 (3μg)
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