Analytical Data
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Gene name
ART5
- Application
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Alternative Names
ART5；Ecto-ADP-ribosyltransferase 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96L15
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Expression Region
23-291aa
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AA Sequence
VPILPLGL APDTFDDTYV GCAEEMEEKA APLLKEEMAH HALLRESWEA AQETWEDKRR GLTLPPGFKA QNGIAIMVYT NSSNTLYWEL NQAVRTGGGS RELYMRHFPF KALHFYLIRA LQLLRGSGGC SRGPGEVVFR GVGSLRFEPK RLGDSVRLGQ FASSSLDKAV AHRFGNATLF SLTTCFGAPI QAFSVFPKER EVLIPPHEVF LVTRFSQDGA QSLVTLWSYN QTCSHFNCAY LGGEKRRGCV SAPGALGTGD LHMTKRHLQQ P
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Molecular Weight
32 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ART5 (alpha-1,3-fucosyltransferase) is a glycosyltransferase enzyme that plays a significant role in the synthesis of glycoproteins and glycolipids through the addition of fucose residues to various carbohydrate structures. Its study has gained traction due to the critical functions these glycosylation processes serve in cell signaling, immune response, and pathogen recognition. Dysregulation of fucosylation patterns has been linked to various diseases, including cancer metastasis and autoimmune disorders, highlighting the importance of understanding ART5’s enzymatic mechanisms and regulation. Additionally, ART5 is of particular interest in the field of biopharmaceuticals, as manipulating its activity could enhance the efficacy and safety profiles of therapeutic proteins. Researchers are investigating the structure-function relationships of ART5, exploring its potential as a biomarker or therapeutic target, and assessing its implications in biotechnological applications. Ongoing studies utilize advanced techniques such as crystallography, mutagenesis, and glycomic analysis to elucidate the specific pathways and biological effects mediated by ART5, aiming to develop novel strategies for disease intervention and improvement in glycoprotein production techniques. As our comprehension of ART5 expands, it promises to inform future research and therapy development in both regenerative medicine and cancer treatment.
