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Aspartyl-tRNA Synthetase (DARS) (C-Term) Peptide
|3 references available|
|Price||49.50 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Characteristics||Blocking peptide for DARS (C-term) antibody ABIN391827|
|Specificity||The synthetic peptide sequence used to generate the antibody AP7572b was selected from the C-term region of humanRS. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
Background: Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.
|Synonyms||MGC111579, DKFZp781B11202, DRS1, 5730439G15Rik, dars, MGC53970, MGC76305, DARS, AspRS, MGC127203, DKFZp468B2125, aats-asp, Aats-Asp, anon-EST:Liang-2.49, cDNA1, CG3821, clone 2.49, DmelCG3821, DRS, l(2)49Db, l(2)k04508, l(2)v27, l(2)vr1, poney, vr1, MGC80207, MGC154056, wu:fc17a11, zgc:154056, ECK1867, JW1855, tls|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles|
|Restrictions||For Research Use only|
Sang Lee, Gyu Park, Park et al.: "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex." in: Biochemical and biophysical research communications, Vol. 291, Issue 1, pp. 158-64, 2002 (PubMed).
Cheong, Park, Kim et al.: "Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function." in: The international journal of biochemistry & cell biology, Vol. 35, Issue 11, pp. 1548-57, 2003 (PubMed).
Bonnefond, Fender, Rudinger-Thirion et al.: "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS." in: Biochemistry, Vol. 44, Issue 12, pp. 4805-16, 2005 (PubMed).