This is a synthetic peptide designed for use in combination with anti-AARS antibody (Catalog #: ARP40370_P050). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
Each Investigator should determine their own optimal working dilution for specific applications.
限制
仅限研究用
状态
Lyophilized
溶解方式
Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
浓度
1 mg/mL
缓冲液
Final peptide concentration is 1 mg/mL in PBS.
注意事项
Avoid repeated freeze-thaw cycles.
储存条件
-20 °C
储存方法
For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
抗原
AARS
(Alanyl tRNA Synthetase (AARS))
背景
The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41 % identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41 % identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure.