Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
CREB-H (D10D8) Rabbit mAb recognizes endogenous levels of total and cleaved CREB-H proteins.
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu93 of human CREB-H protein.
CREB-H belongs to the bZIP transmembrane transcription factor family that activates transcription by binding to cAMP responsive elements (1,2). CREB-H interacts with ATF-6 and binds to conserved elements in the APR genes to synergistically activate transcription (2-4). Evidence suggests that CREB-H is activated by cleavage upon ER stress, inflammatory stimuli (2-5), and metabolic stress (5,6). Known chemical activators of ER stress, such as tunicamycin and thapsigargin, have been shown to induce cleavage of the full-length 75 kDa from of CREB-H, releasing the 50 kDa N-terminal fragment, which translocates to the nucleus (1-4). Upon ER stress, the transmembrane domain of CREB-H is cleaved by Golgi proteases, which allows subsequent translocation to the nucleus. Liberated nuclear CREB-H plays a crucial role in the acute systemic inflammatory response by activating transcription of genes that encode serum amyloid P-component (SAP) and C-reactive protein (CRP) (2,3). Recent studies suggest that activated CREB-H functions as a crucial metabolic regulator of hepatic lipogenesis, fatty acid (FA) oxidation, and lipolysis (5,6). Metabolic stress inducers, such as saturated fatty acids, insulin, and atherogenic high-fat diets have been shown to activate CREB-H in the liver (5-7).
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