Analytical Data
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Gene name
TOR2A
- Application
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Alternative Names
TOR2A；TORP1；Torsin-2A
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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
Q5JU69
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Expression Region
27-321aa
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AA Sequence
AWDL ASLRCTLGAF CECDFRPDLP GLECDLAQHL AGQHLAKALV VKALKAFVRD PAPTKPLVLS LHGWTGTGKS YVSSLLAHYL FQGGLRSPRV HHFSPVLHFP HPSHIERYKK DLKSWVQGNL TACGRSLFLF DEMDKMPPGL MEVLRPFLGS SWVVYGTNYR KAIFIFISNT GGKQINQVAL EAWRSRRDRE EILLQELEPV ISRAVLDNPH HGFSNSGIME ERLLDAVVPF LPLQRHHVRH CVLNELAQLG LEPRDEVVQA VLDSTTFFPE DEQLFSSNGC KTVASRIAFF L
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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
TOR2A, or Target of Rapamycin 2A, is an essential protein involved in the mTOR signaling pathway, which regulates cell growth, proliferation, and metabolism in response to nutrient availability and stress signals. This pathway plays a critical role in various biological processes, including cellular aging, autophagy, and the development of various diseases such as cancer, obesity, and neurodegenerative disorders. The reconstitution and study of TOR2A recombinant proteins have garnered significant attention in recent years, as they provide valuable insights into the mechanisms regulating cellular homeostasis and metabolic control. Specifically, understanding the structural and functional properties of TOR2A can aid in developing therapeutic strategies aimed at modulating mTOR signaling. Moreover, recombinant TOR2A proteins are instrumental in biochemical assays to investigate their interactions with other molecular partners and to explore their roles in cellular signaling networks. As research continues to unveil the complexities surrounding TOR2A and its implications in health and disease, recombinant TOR2A proteins remain crucial for advancing our understanding of this pivotal signaling pathway and its potential as a therapeutic target.
