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Human CLNS1A Recombinant Protein (N-His) (HD609012)

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Overview
Catalog No.HD609012
Description
Recombinant Human CLNS1A Protein, N-His (HD609012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionP54105
Protein lengthMet1-Leu135
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.
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 NamesCLCI, CLNS1A, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, ClCI, I(Cln), ICLN, Methylosome subunit pICln, Reticulocyte pICln
Background

Methylosome subunit pICln is a ~26 kDa protein. Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins. Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 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. 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.

1. Pu, WT. et al. (1999) Molecular and cellular biology 19, 4113-20. PMID: 10330151
2. Friesen, WJ. et al. (2001) Molecular and cellular biology 21, 8289-300. PMID: 11713266
3. Chari, A. et al. (2008) Cell 135, 497-509. PMID: 18984161
4. Guderian, G. et al. (2011) The Journal of biological chemistry 286, 1976-86. PMID: 21081503
Note For research use only
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