Product Name
Tyrosyl-tRNA synthetase (SYYC), Recombinant Protein
Full Product Name
Recombinant Human Tyrosyl-tRNA synthetase, cytoplasmic
Product Synonym Names
Tyrosyl-tRNA synthetase; TyrRS
Product Gene Name
SYYC recombinant protein
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Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
Full Length, 2-528aa
3D Structure
ModBase 3D Structure for P54577
Purity/Purification
Greater than 90% as determined by SDS-PAGE.
Form/Format
20mM Tris-HCl based buffer, pH8.0
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.
Other Notes
Small volumes of SYYC recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
SYYC recombinant protein
Catalyzes the attachment of tyrosine to tRNA (Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA (Tyr).
NCBI/Uniprot data below describe general gene information for SYYC. It may not necessarily be applicable to this product.
NCBI Accession #
NP_003671.1
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NCBI GenBank Nucleotide #
NM_003680.3
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UniProt Primary Accession #
P54577
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UniProt Secondary Accession #
O43276; Q53EN1; B3KWK4; D3DPQ4[Other Products]
UniProt Related Accession #
P54577[Other Products]
NCBI Official Full Name
tyrosine--tRNA ligase, cytoplasmic
NCBI Official Synonym Full Names
tyrosyl-tRNA synthetase
NCBI Official Symbol
YARS??[Similar Products]
NCBI Official Synonym Symbols
YRS; YTS; TYRRS; CMTDIC
??[Similar Products]
NCBI Protein Information
tyrosine--tRNA ligase, cytoplasmic
UniProt Protein Name
Tyrosine--tRNA ligase, cytoplasmic
UniProt Synonym Protein Names
Tyrosyl-tRNA synthetase; TyrRS
UniProt Gene Name
YARS??[Similar Products]
UniProt Synonym Gene Names
TyrRS??[Similar Products]
NCBI Summary for SYYC
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine. [provided by RefSeq, Jul 2008]
UniProt Comments for SYYC
YARS: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). Defects in YARS are the cause of Charcot-Marie-Tooth disease dominant intermediate type C (CMTDIC). CMTDIC is a form of Charcot-Marie-Tooth disease characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Belongs to the class-I aminoacyl-tRNA synthetase family.
Protein type: Aminoacyl-tRNA synthetase; EC 6.1.1.1; Ligase; Translation; Translation regulation
Chromosomal Location of Human Ortholog: 1p35.1
Cellular Component: aminoacyl-tRNA synthetase multienzyme complex; cytoplasm; cytosol; extracellular space; nuclear body
Molecular Function: interleukin-8 receptor binding; protein binding; RNA binding; tRNA binding; tyrosine-tRNA ligase activity
Biological Process: apoptosis; tRNA aminoacylation for protein translation
Disease: Charcot-marie-tooth Disease, Dominant Intermediate C
Research Articles on SYYC
1. Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS.
Precautions
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