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|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant fragment corresponding to a region within amino acids 192 and 408 of Human SARS2|
|Purification||Antigen affinity chromatography|
|Storage buffer||0.1M tris glycine, pH 7, with 20% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:100-1:1000|
|Western Blot (WB)||1:500-1:3000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA5-31472 targets SARS2 in IHC (P) and WB applications and shows reactivity with Human samples.
The PA5-31472 immunogen is recombinant fragment corresponding to a region within amino acids 192 and 408 of Human SARS2.
This gene encodes the mitochondrial seryl-tRNA synthethase precursor, a member of the class II tRNA synthetase family. The mature enzyme catalyzes the ligation of Serine to tRNA(Ser) and participates in the biosynthesis of selenocysteinyl-tRNA(sec) in mitochondria. The enzyme contains an N-terminal tRNA binding domain and a core catalytic domain. It functions in a homodimeric form, which is stabilized by tRNA binding. This gene is regulated by a bidirectional promoter that also controls the expression of mitochondrial ribosomal protein S12. Both genes are within the critical interval for the autosomal dominant deafness locus DFNA4 and might be linked to this disease. Multiple transcript variants encoding different isoforms have been identified for this gene.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
mitochondrial; mitochondrial seryl-tRNA synthetase; mtSerRS; SARS; SARSM; serine tRNA ligase 2; serine tRNA ligase 2, mitochondrial; serine--tRNA ligase; serine-tRNA ligase; serine-tRNA ligase, mitochondrial; SerRS; SERS; seryl-tRNA synthetase; seryl-tRNA synthetase, mitochondrial; seryl-tRNA(Ser/Sec) synthetase; SYS
mtSerRS; SARS; SARS2; SARSM; SerRS; SerRSmt; SERS; SYS