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AB154819

Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927]

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(4 Publications)

Rabbit Recombinant Monoclonal Tyrosyl tRNA synthetase/TyrRS antibody. Suitable for WB, ICC/IF and reacts with Rat, Human samples. Cited in 4 publications.

View Alternative Names

YARS, YARS1, Tyrosyl-tRNA synthetase, TyrRS

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] (AB154819)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] (AB154819)

Immunofluorescence analysis of HeLa cells labeling Tyrosyl tRNA synthetase / TyrRS using ab154819 at 1/250 dilution.

Western blot - Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] (AB154819)
  • WB

Unknown

Western blot - Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] (AB154819)

All lanes:

Western blot - Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] (ab154819) at 1/1000 dilution

Lane 1:

C6 cell lysate at 10 µg

Lane 2:

PC12 cell lysate at 10 µg

Lane 3:

Raji cell lysate at 10 µg

Lane 4:

HeLa cell lysate at 10 µg

Lane 5:

ECV-304 cell lysate at 10 µg

Predicted band size: 59 kDa

false

  • Carrier free

    Anti-Tyrosyl tRNA synthetase/TyrRS antibody [EPR9927] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR9927

Isotype

IgG

Carrier free

No

Reacts with

Rat, Human

Applications

WB, ICC/IF

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Conditional Ambient
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Tyrosyl tRNA synthetase also known as TyrRS is an enzyme responsible for charging tRNA molecules with the amino acid tyrosine. This process known as aminoacylation is essential for accurate translation of the genetic code during protein synthesis. TyrRS has a molecular weight of approximately 58 kDa. It is expressed in various tissues playing a significant role in both cytoplasmic and mitochondrial protein synthesis in eukaryotes.
Biological function summary

TyrRS plays an important role in ensuring the fidelity of protein translation within cells. It facilitates the correct pairing of tRNA^Tyr with its corresponding tyrosine amino acid contributing to the accuracy of protein production. This enzyme is part of the aminoacyl-tRNA synthetase complex a multi-enzyme complex that catalyzes the attachment of specific amino acids to their appropriate tRNA molecules an important step in the translation process.

Pathways

TyrRS is involved in the protein synthesis pathway where it functions alongside other aminoacyl-tRNA synthetases to help maintain the genetic code's accuracy. Additionally TyrRS is implicated in the aminoacyl-tRNA biosynthesis pathway connecting its activity with enzymes responsible for similar processes. It works closely with related enzymes such as phenylalanyl-tRNA synthetase (PheRS) and tryptophanyl-tRNA synthetase (TrpRS) through these pathways ensuring coordinated protein synthesis.

TyrRS has been connected to certain neurodegenerative diseases and cancer. Mutations in the TYRRS gene have been associated with Charcot-Marie-Tooth disease a hereditary neuropathy. The enzyme's altered function in this context may lead to compromised protein synthesis. Additionally aberrant TyrRS expression has been observed in some types of cancer where it interacts with proteins like angiogenin to potentially promote tumor growth. These connections highlight the enzyme's potential role in disease progression and pathogenesis.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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).
See full target information YARS1

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

European journal of medical genetics 64:104294 PubMed34352414

2021

Novel partial loss-of-function variants in the tyrosyl-tRNA synthetase 1 (YARS1) gene involved in multisystem disease.

Applications

Unspecified application

Species

Unspecified reactive species

Clothilde Estève,Céline Roman,Cécile DeLeusse,Melissa Baravalle,Karine Bertaux,Frédéric Blanc,Patrice Bourgeois,Violaine Bresson,Aline Cano,Marie-Edith Coste,Clémence Delteil,Caroline Lacoste,Marie Loosveld,André Maues De Paula,Anne-Sophie Monnier,Véronique Secq,Nicolas Levy,Catherine Badens,Alexandre Fabre

Journal of cancer research and clinical oncology 146:329-342 PubMed31912229

2020

YARS as an oncogenic protein that promotes gastric cancer progression through activating PI3K-Akt signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Cheng Zhang,Xiaoting Lin,Qian Zhao,Yakun Wang,Fangli Jiang,Congcong Ji,Yanyan Li,Jing Gao,Jian Li,Lin Shen

Brain : a journal of neurology 141:2878-2894 PubMed30239612

2018

UBA1/GARS-dependent pathways drive sensory-motor connectivity defects in spinal muscular atrophy.

Applications

Unspecified application

Species

Unspecified reactive species

Hannah K Shorrock,Dinja van der Hoorn,Penelope J Boyd,Maica Llavero Hurtado,Douglas J Lamont,Brunhilde Wirth,James N Sleigh,Giampietro Schiavo,Thomas M Wishart,Ewout J N Groen,Thomas H Gillingwater

Neuron 96:373-386.e6 PubMed29024661

2017

Paclitaxel Reduces Axonal Bclw to Initiate IPR1-Dependent Axon Degeneration.

Applications

Unspecified application

Species

Unspecified reactive species

Sarah E Pease-Raissi,Maria F Pazyra-Murphy,Yihang Li,Franziska Wachter,Yusuke Fukuda,Sara J Fenstermacher,Lauren A Barclay,Gregory H Bird,Loren D Walensky,Rosalind A Segal
View all publications

Product promise

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