Analytical Data
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Gene name
TREH
- Application
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Alternative Names
TREH；TREA；Trehalase
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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
O43280
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Expression Region
24-556aa
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AA Sequence
LPPPCES EIYCHGELLN QVQMAKLYQD DKQFVDMPLS IAPEQVLQTF TELSRDHNHS IPREQLQAFV HEHFQAKGQE LQPWTPADWK DSPQFLQKIS DAKLRAWAGQ LHQLWKKLGK KMKPEVLSHP ERFSLIYSEH PFIVPGGRFV EFYYWDSYWV MEGLLLSEMA ETVKGMLQNF LDLVKTYGHV PNGGRVYYLQ RSQPPLLTLM MDCYLTHTND TAFLQENIET LALELDFWTK NRTVSVSLEG KNYLLNRYYV PYGGPRPESY SKDVELADTL PEGDREALWA ELKAGAESGW DFSSRWLIGG PNPNSLSGIR TSKLVPVDLN AFLCQAEELM SNFYSRLGND SQATKYRILR SQRLAALNTV LWDEQTGAWF DYDLEKKKKN REFYPSNLTP LWAGCFSDPG VADKALKYLE DNRILTYQYG IPTSLQKTGQ QWDFPNAWAP LQDLVIRGLA KAPLRRAQEV AFQLAQNWIR TNFDVYSQKS AMYEKYDVSN GGQPGGGGEY EVQEGFGWTN GVVLMLLDRY GDRLTS
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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
TREH (Trehalase) is an enzyme that plays a crucial role in the metabolism of trehalose, a unique disaccharide sugar found in various organisms, including fungi, plants, and invertebrates. Recent research has highlighted the significance of TREH in different physiological processes such as energy production, stress resistance, and cellular signaling. In humans, abnormal TREH activity is linked to certain metabolic disorders, making it a potential target for therapeutic interventions. Furthermore, TREH has been implicated in the regulation of osmotic stress responses and the survival of organisms in extreme environments, showcasing its adaptive significance. Due to its diverse biological roles, the study of TREH and its recombinant forms has garnered attention in both fundamental and applied research fields. The recombinant expression of TREH in various host systems allows for detailed functional analyses and structural studies, which can elucidate its mechanisms of action. This research is crucial for understanding how TREH might be manipulated for improved resilience in crops, enhancing biotechnological applications in industrial processes, and developing novel therapeutic strategies for metabolic diseases. As interest in trehalose biology continues to grow, TREH represents a valuable focus for ongoing research into metabolic regulation and its associated pathways, with implications spanning agriculture, biotechnology, and medicine.
