Analytical Data
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Gene name
pylS
- Application
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Alternative Names
pylS；Pyrrolysine--tRNA ligase
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Species
E.coli
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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
Q46E77
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Expression Region
1-419aa
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AA Sequence
MDKKPLDVLISATGLWMSRTGTLHKIKHYEVSRSKIYIEMACGDHLVVNNSRSCRTARAFRHHKYRKTCKRCRVSDEDINNFLTRSTEGKTSVKVKVVSAPKVKKAMPKSVSRAPKPLENPVSAKASTDTSRSVPSPAKSTPNSPVPTSAPAPSLTRSQLDRVEALLSPEDKISLNIAKPFRELESELVTRRKNDFQRLYTNDREDYLGKLERDITKFFVDRDFLEIKSPILIPAEYVERMGINNDTELSKQIFRVDKNLCLRPMLAPTLYNYLRKLDRILPDPIKIFEVGPCYRKESDGKEHLEEFTMVNFCQMGSGCTRENLESLIKEFLDYLEIDFEIVGDSCMVYGDTLDIMHGDLELSSAVVGPVPLDREWGIDKPWIGAGFGLERLLKVMHGFKNIKRASRSESYYNGISTNL
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Molecular Weight
51.8 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
The study of pylS recombinant proteins has gained significant attention in recent years due to their crucial role in the biosynthesis of pyrrolysine, the 22nd genetically encoded amino acid. Pyrrolysine is incorporated into proteins in certain Archaea and bacteria through a unique tRNA and synthetase system, which is distinct from the standard genetic code. Understanding the mechanisms of pylS and its associated pathways provides insights into the evolution of translation and the potential for expanding the genetic code in synthetic biology applications. Researchers aim to explore pylS's functionality, structure, and interaction with other cellular components, which could lead to innovations in protein engineering, therapeutics, and biotechnological applications. Furthermore, the ability to incorporate non-canonical amino acids into proteins opens up new avenues for creating novel biomolecules with tailored properties, thereby enhancing our ability to design proteins for specific functions in various fields, including medicine and materials science. As the demand for customized proteins grows, the exploration of pylS and its recombinant forms stands as a promising frontier in both fundamental and applied research.
