protein

TFEB protein, Human (N-His)

HY-P701228

5 μg;10 μg;50 μg

53;90;250 USD

TFEB protein, Human (N-His)

proteins

E. coli

5 μg;10 μg;50 μg

53;90;250 USD

TFEB protein is a transcription factor that subtly regulates lysosomal function, autophagy, lipid catabolism, energy metabolism, and immune responses. It recognizes E-box and CLEAR-box sequences and controls gene expression based on nutrient availability. 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.

Human

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.

ALPHATFEB; BHLHE35; TCFEB

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

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

Room temperature in continental US; may vary elsewhere.