AARSD1 cDNA ORF Clone in Cloning Vector, Human

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AARSD1 cDNA ORF Clone in Cloning Vector, Human: General Information

Gene
Species
Human
NCBI Ref Seq
RefSeq ORF Size
1239 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence except for the point mutations: 60C>T not causing the amino acid variation.
Description
Full length Clone DNA of Human alanyl-tRNA synthetase domain containing 1.
Plasmid
Vector
Sequencing Primers
M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.

AARSD1 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

AARSD1 cDNA ORF Clone in Cloning Vector, Human: Alternative Names

AARSD1 cDNA ORF Clone, Human

AARSD1 Background Information

AARSD1 belongs to the class-II aminoacyl-tRNA synthetase family, Alax-L subfamily. AARSD1 binds 1 zinc ion per subunit functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). Four transcript variants have been described for AARSD1: NM_25267.3, NM_113642.2, NM_1142653.1 and NM_1142654.1. It has been determined that the latter two variants represent a distinct upstream locus, which is now represented by GeneID:1885848 (PTGES3L), while the former two variants represent readthrough transcripts between PTGES3L and this locus (AARSD1). The readthrough locus (PTGES3L-AARSD1) is now represented by GeneID:188585.
Full Name
alanyl-tRNA synthetase domain containing 1
References
  • Tatham MH, et al. (2011) Comparative proteomic analysis identifies a role for SUMO in protein quality control. Oncogene. 19(17):2120-8.
  • Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 44(2):325-40.
  • Udeshi ND, et al. (2012) Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol Cell Proteomics. 11(5):148-59.

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