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>   首页   >   产品   >   一抗   >   其他   >   Tyrosyl tRNA synthetase (YARS) Antibody (C-term)   

Tyrosyl tRNA synthetase (YARS) Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Tyrosyl tRNA synthetase (YARS) Antibody (C-term) AP7580b
    Western blot analysis of anti-YARS Antibody (C-term) (Cat.#AP7580b) in CEM cell line lysates (35ug/lane). YARS(arrow) was detected using the purified Pab.
  • 14 - Tyrosyl tRNA synthetase (YARS) Antibody (C-term) AP7580b
    Formalin-fixed and paraffin-embedded human lung carcinoma tissue reacted with YARS antibody (C-term) (Cat.#AP7580b), which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, E
Primary Accession P54577
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 59143 Da
Antigen Region 450-479 aa
Additional Information
Gene ID 8565
Other Names Tyrosine--tRNA ligase, cytoplasmic, Tyrosyl-tRNA synthetase, TyrRS, Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed, YARS
Target/Specificity This Tyrosyl tRNA synthetase (YARS) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 450-479 amino acids from the C-terminal region of human Tyrosyl tRNA synthetase (YARS).
Dilution WB~~1:1000
IHC-P~~1:100~500
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTyrosyl tRNA synthetase (YARS) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name YARS1 (HGNC:12840)
Function Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) (PubMed:25533949). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity (PubMed:25533949). Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine-- tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 (PubMed:25533949).
Cellular Location Cytoplasm. Nucleus Note=Cytoplasmic in normal conditions (PubMed:25533949). Resveratrol- binding in response to serum starvation promotes relocalization to the nucleus (PubMed:25533949).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.

REFERENCES

Yang,X.L., Chem. Biol. 14 (12), 1323-1333 (2007)
Jordanova,A., Nat. Genet. 38 (2), 197-202 (2006)
Bonnefond,L., Biochemistry 44 (12), 4805-4816 (2005)

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