Analytical Data
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Gene name
Intein
- Application
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Alternative Names
rgy;Reverse gyrase
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Species
Mycobacterium xenopi
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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
P72065
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Expression Region
1-65aa
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AA Sequence
RPDRSHAKSA RSVAETMGNY HPHGDASIYD TLVRMAQPWS MRYPLVDGQG NFGSPGNDPP AAMRY
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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
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Protein Description
Intein-mediated protein splicing has emerged as a significant tool in the field of molecular biology and protein engineering. Inteins, or intervening proteins, are unique segments of amino acid sequences that can catalyze their own excision from a precursor protein, leading to the ligation of the flanking exteins (the remaining portions of the protein). This natural phenomenon occurs in various organisms, including bacteria, archaea, and eukaryotes, and offers a valuable mechanism for the precise and selective recombination of proteins. The ability to use inteins for protein purification, labeling, and functional analysis has been realized in numerous applications, including the production of recombinant proteins with high purity and activity. Furthermore, intein technology allows for the insertion of peptide tags or site-specific labels, facilitating downstream applications such as crystallography and drug design. Recent advances in synthetic biology have enabled researchers to engineer inteins with improved properties and expand their versatility, paving the way for novel therapeutic approaches, biosensing platforms, and biocatalysts. By harnessing the power of intein-mediated protein splicing, scientists continue to explore new avenues in protein research, enhancing our understanding of protein function and expanding the toolkit available for biotechnology. This innovative approach holds promise for advancing not only basic research but also practical applications in medicine and industry.
