Analytical Data
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Gene name
SCLY
- Application
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Alternative Names
SCLY；SCL；Selenocysteine lyase
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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
Q96I15
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Expression Region
1-445aa
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AA Sequence
MEAAVAPGRD APAPAASQPS GCGKHNSPER KVYMDYNATT PLEPEVIQAM TKAMWEAWGN PSSPYSAGRK AKDIINAARE SLAKMIGGKP QDIIFTSGGT ESNNLVIHSV VKHFHANQTS KGHTGGHHSP VKGAKPHFIT SSVEHDSIRL PLEHLVEEQV AAVTFVPVSK VSGQAEVDDI LAAVRPTTRL VTIMLANNET GIVMPVPEIS QRIKALNQER VAAGLPPILV HTDAAQALGK QRVDVEDLGV DFLTIVGHKF YGPRIGALYI RGLGEFTPLY PMLFGGGQER NFRPGTENTP MIAGLGKAAE LVTQNCEAYE AHMRDVRDYL EERLEAEFGQ KRIHLNSQFP GTQRLPNTCN FSIRGPRLQG HVVLAQCRVL MASVGAACHS DHGDQPSPVL LSYGVPFDVA RNALRLSVGR STTRAEVDLV VQDLKQAVAQ LEDQA
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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
SCLY, or Selenocysteine Lyase, is an enzyme that plays a crucial role in the metabolism of selenium, a trace element essential for human health. Recent studies have highlighted SCLY’s importance in various biological processes, including antioxidant defense and thyroid hormone metabolism. Research indicates that SCLY is involved in the conversion of selenocysteine, a form of amino acid containing selenium, into its non-selenium counterpart, thereby regulating selenium homeostasis in the body. Disruptions in SCLY function can lead to selenium deficiency, which has been linked to numerous health issues, including increased susceptibility to oxidative stress, impaired immune function, and the development of certain diseases. Furthermore, understanding the structural and functional aspects of SCLY is essential for exploring its potential therapeutic applications, particularly in diseases where selenium plays a protective role. Ongoing investigations into SCLY’s mechanisms, regulation, and interactions at the molecular level continue to unveil its significance in both health and disease, making it a promising target for future research and potential interventions.
