Recombinant Human Leucine--tRNA ligase, cytoplasmic (LARS1), partial

Code CSB-YP873736HU
MSDS
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Source Yeast
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Code CSB-EP873736HU
MSDS
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Source E.coli
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Code CSB-EP873736HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP873736HU
MSDS
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Source Baculovirus
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Code CSB-MP873736HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
LARS
Uniprot No.
Alternative Names
cytoplasmic; Cytoplasmic leucyl tRNA synthetase; Cytosolic leucyl tRNA synthetase; FLJ10595; FLJ21788; hr025Cl; HSPC 192; HSPC192; KIAA1352; LARS 1; Lars; LARS1; Leucine translase; Leucine tRNA ligase; Leucine--tRNA ligase; Leucyl tRNA synthetase cytoplasmic; Leucyl-tRNA synthetase; LeuRS; LEUS; LRS; PIG 44; PIG44; Proliferation inducing gene 44; RNTLS; SYLC_HUMAN
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs.
Gene References into Functions
  1. Leucyl-tRNA synthetase (LRS) is a leucine sensor of the mTORC1 pathway. PMID: 28963468
  2. The results showed a decrease in autophagy on addition of leucine, demonstrating crosstalk between leucine sensing, LRS translocation, RagD interaction, and mTORC1 activation. PMID: 28882589
  3. the KMSKS catalytic loop affects the aminoacylation and editing capacities of leucyl-tRNA synthetase PMID: 25817995
  4. Lack of a CP1 hairpin in LeuRS led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. PMID: 25051973
  5. the carboxy-terminal domain of human mitochondrial (mt) leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations. PMID: 24413190
  6. Identification of a mutation in LARS as a novel cause of infantile hepatopathy PMID: 22607940
  7. This work demonstrates that LRS is a key mediator for amino acid signaling to mTORC1. PMID: 22424946
  8. hcLeuRS can charge RNALeu with non-cognate amino acids and exclude the incorrect products by multiple editing pathways. PMID: 20805241
  9. leucyl-tRNA synthetase requires its C-terminal domain for its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex PMID: 16055448
  10. We identified a novel G3283A transition in the mitochondrial DNA tRNA(Leu (UUR)) gene in a patient with ptosis, ophthalmoparesis and hyporeflexia. PMID: 17363246
  11. Results show that K600 in human leucyl-tRNA synthetase affects amino acid specificity and tRNA aminoacylation. PMID: 17378584
  12. findings suggest that LARS1 may play roles in migration and growth of lung cancer cells, which suggest its potential implication in lung tumorigenesis PMID: 18446061
  13. Study of crystal structures of the editing domain from 2 eukaryotic cytosolic LeuRS; shows a conserved structural core containing the active site for hydrolysis, with distinct bacterial, archeal, or eukaryotic peripheral insertions. PMID: 19426743
  14. the introduction of bulky residues into the amino acid binding pocket failed to block deacylation of tRNA, indicating that the architecture of the amino acid binding pocket is different compared to that of other characterized LeuRSs PMID: 19702327

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Involvement in disease
Infantile liver failure syndrome 1 (ILFS1)
Subcellular Location
Cytoplasm.
Protein Families
Class-I aminoacyl-tRNA synthetase family
Database Links

HGNC: 6512

OMIM: 151350

KEGG: hsa:51520

STRING: 9606.ENSP00000377954

UniGene: Hs.432674

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