Description
IARS2 Antibody | 63-233 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: Predicted species reactivity based on immunogen sequence: Monkey
Immunogen: This IARS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 600-628 amino acids from the Central region of human IARS2.
Research Area: Other
Tested Application: WB, IHC-P
Application: For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:10~50
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 114 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: Isoleucine--tRNA ligase, mitochondrial, Isoleucyl-tRNA synthetase, IleRS, IARS2
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: IARS2 belongs to the class-I aminoacyl-tRNA synthetase family. Members of class I have two highly conserved sequence motifs. They aminoacylate at the 2'-OH of an adenosine nucleotide, and are usually monomeric or dimeric (one or two subunits, respectively) . Both classes of aminoacyl-tRNA synthetases are multidomain proteins. The catalytic domains of all the aaRSs of a given class are found to be homologous to one another, while class I and class II aaRSs are unrelated to one another. The class I aaRSs have the ubiquitous Rossmann fold and have the antiparallel beta-strands architecture while the class II aaRSs have a unique fold made up of antiparallel beta-strands.