GEMIN6 Protein, Human (His, Strep)

The GEMIN6 protein is a component of the SMN complex and is critical for the assembly of small nuclear ribonucleoproteins (snRNPs), which are essential for spliceosome-mediated pre-mRNA splicing. Most spliceosomal snRNPs share a common set of Sm proteins that form a heptameric protein ring on small nuclear RNAs. GEMIN6 Protein, Human (His, Strep) is the recombinant human-derived GEMIN6 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of GEMIN6 Protein, Human (His, Strep) is 167 a.a., .

GEMIN6, a crucial component of the SMN complex, is integral to the assembly of small nuclear ribonucleoproteins (snRNPs), the essential constituents of the spliceosome that play a central role in pre-mRNA splicing. The majority of spliceosomal snRNPs comprise a common set of Sm proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, and SNRPG, forming a heptameric protein ring on the Sm site of the small nuclear RNA to create the core snRNP (Sm core). In the cytosol, CLNS1A chaperone traps the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF, and SNRPG in an inactive 6S pICln-Sm complex, regulating core snRNP assembly. The SMN complex, consisting of SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, and STRAP/UNRIP, accepts the trapped 5Sm proteins from CLNS1A to form an intermediate. Binding of snRNA within 5Sm prompts eviction of the SMN complex, allowing SNRPD3 and SNRPB binding to complete the core snRNP assembly. GEMIN6 is part of both the core SMN complex and the SMN-Sm complex, interacting directly with GEMIN7 and GEMIN8, as well as with SNRPB, SNRPD2, SNRPD3, and SNRPE.

Human

E. coli

N-Strep;N-6*His

Q8WXD5 (M1-Q167)

79833

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.