Recombinant Human WARS Protein (N-6His)

Name: Recombinant Human WARS Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0386NP
Availability: InStock

BL-0386NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Tryptophan-tRNA ligase, Cytoplasmic is produced by our E.coli expression system and the target gene encoding Met1-Gln471 is expressed with a 6His tag at the N-terminus.
Accession	P23381
Synonym	WARS also known as Tryptophanyl-tRNA synthetase; Interferon-induced protein 53
Gene Background	There exists two types of tryptophanyl tRNA synthetases, the cytoplasmic form called WARS, the mitochondrial form called WARS2. WARS catalyzes the aminoacylation of tRNA (trp) with tryptophan and is induced by interferon. WARS regulates ERK, Akt, eNOS activation pathway, which are related with angiogenesis, cytoskelatal reorganization and shear stess-reponsive gene expression.
Molecular Mass	55.3 KDa
Apmol Mass	60 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 8% Trehalose, 4% Mannitol, 50mM NaCl, 0.05% Tween 80, pH7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
Subcellular Location	Cytoplasm.
Protein Families	Class-I aminoacyl-tRNA synthetase family
Database References	HGNC: 12729 OMIM: 191050 KEGG: hsa:7453 STRING: 9606.ENSP00000347495 UniGene: Hs.497599

Gene Functions References

Based on these results, secretion of full-length tryptophanyl-tRNA synthetase appears to work as a primary defence system against infection, acting before full activation of innate immunity. PMID: 27748732
findings establish WARS as a gene whose mutations may cause distal hereditary motor neuropathy and alter canonical and non-canonical functions of tryptophanyl-tRNA synthetase. PMID: 28369220
Overexpression of WARS predicts no recurrence and good survival for triple-negative breast cancer patients. PMID: 26209610
Tryptophanyl-tRNA synthetase expression is up-regulated in patients with rheumatoid arthritis. PMID: 24515434
Genes within recently identified loci associated with waist-hip ratio (WHR) exhibit fat depot-specific mRNA expression, which correlates with obesity-related traits. Adipose tissue (AT) mRNA expression of 6 genes (TBX15/WARS2, STAB1, PIGC, ZNRF3, GRB14) PMID: 23670221
Indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase may play critical roles in the immune pathogenesis of chronic kidney disease. PMID: 23651343
Naturally occurring fragments of the two proteins involved in translation, TyrRS and TrpRS, have opposing activities on angiogenesis. PMID: 21442253
Tryptophanyl-tRNA synthetase down-regulation by hypoxia may be a factor responsible for low TrpRS in pancreatic tumors with high metastatic ability. PMID: 21926542
Mini-tryptophanyl-tRNA synthetase inhibited ischemic angiogenesis in rats. PMID: 20963594
Tryptophanyl-tRNA synthetase is a multidomain protein exhibiting excellent allosteric communication, and this research has provided valuable structural as well as functional insights into the protein. PMID: 19768679
Low tryptophanyl-tRNA synthetase is associated with recurrence in colorectal cancer. PMID: 19900940
In this study, we show that a recombinant form of a COOH-terminal fragment of TrpRS is a potent antagonist of vascular endothelial growth factor-induced angiogenesis in a mouse model and of naturally occurring retinal angiogenesis in the neonatal mouse PMID: 11773625
Thus, protein synthesis may be linked to the regulation of angiogenesis by a natural fragment of TrpRS PMID: 11773626
Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains PMID: 11834741
The recently discovered antiangiogenic and cell-signaling activities of tryptophanyl-tRNA synthetase bioactive fragments are discussed in this review. PMID: 12416978
TrpRS may have a role in the maintenance of vascular homeostasis PMID: 14630953
results suggest that mammalian and bacterial tryptophanyl-tRNA synthetase might use different mechanisms to recognize the substrate and modeling studies indicate that transfer RNA binds with the dimeric enzyme PMID: 14660560
A crystal structure of human tryptophanyl-tRNA synthetase was solved at 2.1 A with a tryptophanyl-adenylate bound at the active site PMID: 14671330
May play an important role in the intracellular regulation of protein synthesis under conditions of oxidative stress. PMID: 15628863
These crystals captured two conformations of the human tryptophanyl-tRNA synthetase and tRNATrp complex, which are nearly identical with respect to the protein and a bound tryptophan. PMID: 16724112
The first crystal structure of human tryptophanyl-tRNA synthetase (hTrpRS) in complex with tRNA(Trp) and Trp which, together with biochemical data, reveals the molecular basis of a novel tRNA binding and recognition mechanism. PMID: 16798914
Results provide the first evidence of the involvement of heme in regulation of TrpRS aminoacylation activity. PMID: 17877375
the annexin II-S100A10 complex, which regulates exocytosis, forms a ternary complex with TrpRS. PMID: 17999956
Analysis of the molecular basis of the mechanisms of the substrate recognition and the activation reaction by tryptophanyl-tRNA synthetase. PMID: 18180246
Indoleamine 2,3-dioxygenase (IDO)-expression in antigen-presenting cells (APCs) may control autoimmune responses by depleting the available tryptophan, whereas tryptophanyl-tRNA synthetase (TTS) may counteract this effect PMID: 19363598

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.