TFEB protein, Human (N-His)

TFEB Protein, a transcription factor, masterfully regulates lysosomal functions, autophagy, lipid catabolism, energy metabolism, and immune responses. Recognizing E-box and CLEAR-box sequences, it controls gene expression in response to nutrient availability. MTOR phosphorylation inhibits TFEB, retaining it cytosolic, while starvation induces dephosphorylation, leading to nuclear localization and gene activation. TFEB promotes autophagy and plays a role in immune responses, including antibacterial defense. The drug eltrombopag inhibits TFEB by binding to its bHLH domain, disrupting DNA-binding. TFEB protein, Human (N-His) is the recombinant human-derived TFEB protein, expressed by E. coli , with N-His labeled tag. The total length of TFEB protein, Human (N-His) is 476 a.a., with molecular weight of ~57.0 kDa.

TFEB protein operates as a key transcription factor orchestrating diverse cellular processes, including lysosomal biogenesis, autophagy, lysosomal exocytosis, lipid catabolism, energy metabolism, and immune response. Recognizing E-box sequences, TFEB's efficient DNA-binding necessitates dimerization with itself or other MiT/TFE family members like TFE3 or MITF. It responds to amino acid availability through MTOR-mediated phosphorylation, promoting cytosolic retention and inactivation. Conversely, MTOR inhibition during starvation or lysosomal stress induces TFEB dephosphorylation, leading to nuclear localization and transcriptional activation. TFEB specifically binds CLEAR-box sequences, activating the expression of lysosomal genes and regulating lysosomal positioning. Additionally, it positively regulates autophagy, contributes to T-cell-dependent antibody responses, and plays a role in vascularization of the placenta. In response to bacterial infection, TFEB mediates itaconate-induced alkylation, activating lysosomal biogenesis and aiding in bacterial clearance. Notably, the eltrombopag drug inhibits TFEB by binding to the bHLH domain and disrupting DNA-binding.

Human

E. coli

N-His

P19484-1(M1-L476)

7942

MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL

Approximately 57.0 kDa

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  Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from sterile 20 mM PB, 150 mM Nacl, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.