Recombinant human Seryl-tRNA synthetase,Cytoplasmic domain protein(SERS),partial CSB-EP020709HU1
Specifications
| 20ug / 100ug price = 20ug |
Alternative Name(s):
Seryl-tRNA synthetase ;SerRSSeryl-tRNA(Ser/Sec) synthetase
Species: (Organism)
Homo sapiens (Human)
Gene Names:
SERS
Tag info:
N-terminal GST-tagged
Target Protein AA Sequence:
VLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEV
Expression Region:
2-233aa
Subcellular Location:
Cytoplasm, Nucleus
Tissue Specificity:
Brain.
Protein Length:
Partial
Pathway:
Mol. Weight:
53.4 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Metabolism
Function:
Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction
Involvement in disease:
Neurodevelopmental disorder with microcephaly, ataxia, and seizures (NEDMAS)
Relevance:
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily
Reference:
Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase.Vincent C., Tarbouriech N., Haertlein M.Eur. J. Biochem. 250:77-84(1997)
