|Other Names||Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7833b was selected from the C-term region of human KARS. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation.|
|Cellular Location||Isoform Cytoplasmic: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Secreted Note=Secretion is induced by TNF-alpha|
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Provided below are standard protocols that you may find useful for product applications.
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
Guo,M., Proc. Natl. Acad. Sci. U.S.A. 105 (7), 2331-2336 (2008)Kovaleski,B.J., J. Biol. Chem. 282 (44), 32274-32279 (2007)Kaminska,M., FEBS Lett. 581 (16), 3105-3110 (2007)
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