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Human GEMIN2 Recombinant Protein (N-GST & C-His) (HD415012)

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Overview
Catalog No.HD415012
Description
Recombinant Human GEMIN2 Protein, N-GST & C-His (HD415012) expressed in E. coli, spanning Thr99-Ser280. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionO14893
Protein lengthThr99-Ser280
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 48.86 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesComponent of gems 2, GEMIN2, Gem-associated protein 2, Gemin-2, SIP1, SMN-interacting protein 1, Survival of motor neuron protein-interacting protein 1
Background

Gem-associated protein 2 is a ~31 kDa protein. 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 (5Sm) 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. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.

1. Chari, A. et al. (2008) Cell 135, 497-509. PMID: 18984161
2. Liu, Q. et al. (1997) Cell 90, 1013-21. PMID: 9323129
3. Yi, H. et al. (2020) Nucleic acids research 48, 895-911. PMID: 31799625
4. Golembe, TJ. et al. (2005) Molecular and cellular biology 25, 10989-1004. PMID: 16314521
5. Zhang, R. et al. (2011) Cell 146, 384-95. PMID: 21816274
Note For research use only
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Formula
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