Analytical Data
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Gene name
TFEB
- Application
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Alternative Names
Class E basic helix-loop-helix Protein 35;bHLHe35
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19484
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Expression Region
1-476 aa
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AA Sequence
MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL
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Molecular Weight
58.8 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
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Protein Description
TFEB (Transcription Factor EB) is a master regulator of lysosomal biogenesis and autophagy, which plays a crucial role in cellular homeostasis and metabolism. Elevated TFEB activity has been linked to the enhancement of lysosomal function and the clearance of damaged organelles and misfolded proteins, making it an intriguing target for therapeutic interventions in a variety of diseases, including neurodegenerative disorders, metabolic syndromes, and cancer. Research has shown that TFEB can effectively promote lysosomal biogenesis through the transcriptional activation of key genes involved in lysosome formation and function, contributing to improved cellular health. Furthermore, the dysregulation of TFEB has been implicated in pathologies such as Alzheimer’s and Parkinson’s disease, prompting investigations into its potential as a biomarker and therapeutic target. Recent studies are focusing on the development of TFEB-recombinant proteins to better understand its regulatory mechanisms and interactions within cellular pathways. By engineering these proteins, researchers aim to dissect the specific roles of TFEB in cellular processes, assess its impact on lysosomal dynamics, and explore its potential in drug discovery. The ability to manipulate TFEB expression and activity could pave the way for novel strategies to enhance autophagic flux and mitigate the effects of lysosomal storage diseases, thereby holding promise for the advancement of treatments targeting metabolic and neurodegenerative conditions. As such, TFEB represents a compelling focus of current biomedical research aimed at harnessing autophagy and lysosomal pathways to promote cellular health and combat disease.
