#32361 TFEB (D4L2P) Rabbit mAb
|TFEB (D4L2P) Rabbit mAb recognizes endogenous levels of total mouse TFEB protein.|
|Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro413 of mouse TFEB protein.|
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Western blot analysis of extracts from A20, CTLL-2, and EL4 cell lines using TFEB (D4L2P) Rabbit mAb.
Western blot analysis of extracts from 634T wild-type or two 634T cell lines with a TFEB knockout using TFEB (D4L2P) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). Knockout cells were kindly provided by Dr. Reuben Shaw, Salk Institute for Biological Studies, La Jolla, CA.
Immunoprecipitation of TFEB from A20 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is TFEB (D4L2P) Rabbit mAb. Western blot was performed using TFEB (D4L2P) Rabbit mAb. Mouse Anti-Rabbit IgG (Conformation Specific) (L27A9) mAb (HRP Conjugate) #5127 was used as a secondary antibody.
Transcription factor EB (TFEB) is a member of the Myc-related, bHLH leucine-zipper family of transcription factors that drives the expression of a network of genes known as the Coordinated Lysosomal Expression and Regulation (CLEAR) network (1,2). TFEB specifically recognizes and binds regulatory sequences within the CLEAR box (GTCACGTGAC) of lysosomal and autophagy genes, resulting in the up-regulated expression of genes involved in lysosome biogenesis and function, and regulation of autophagy (1,2). TFEB is activated in response to nutrient deprivation, stimulating translocation to the nucleus where it forms homo- or heterooligomers with other members of the microphthalmia transcription factor (MiTF) subfamily and resulting in up-regulation of autophagosomes and lysosomes (3-5). Recently, it has been shown that TFEB is a component of mammalian target of rapamycin (mTOR) complex 1 (mTORC1), which regulates the phosphorylation and nuclear translocation of TFEB in response to cellular starvation and stress (6-9). During normal growth conditions, TFEB is phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation promotes association of TFEB with 14-3-3 family proteins and retention in the cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it increases transcription of CLEAR and autophagy genes (10). TFEB has also been shown to be activated in a nutrient-dependent manner by p42 MAP kinase (Erk2). TFEB is phosphorylated at Ser142 by Erk2 in response to nutrient deprivation, resulting in nuclear localization and activation, and indicating that pathways other than mTOR contribute to nutrient sensing via TFEB (3).
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