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Western blot analysis of MTP on a mouse liver lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-MTP antibody.
BD Transduction Laboratories™ Purified Mouse Anti-MTP
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/support/resources/cell_biology/index.jsp
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The microsomal triglyceride transfer protein (MTP) catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between membranes within the lumen of microsomes in hepatocytes and enterocytes. MTP forms a heterodimer with the 58 kDa protein disulfide isomerase. PDI catalyzes the isomerization of intramolecular disulfide bridges, thereby allowing them to generate their most thermodynamically stable configuration within proteins. MTP is mutated in abetalipoproteinemia, which results from defects in apolipoprotein-B (apoB)-containing lipoproteins. A lack of MTP expression prevents secretion of apoB from mammalian cells, leading to intracellular degradation. In the C-terminal region, MTP has structural homology to apoB and the lamprey lipovitellin protein. This region contains a membrane binding helix (Helix A), and a triglyceride binding helix (Helix B). Mutations in Helix B cause abetalipoproteinemia. In addition, inhibitors of MTP activity may be important therapeutics for lowering atherogenic lipoprotein levels. Thus, MTP is a microsomal protein that is required for transport of lipids between membranes in liver and small intestines.
Development References (6)
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Chen Z, Newberry EP, Norris JY, et al. ApoB100 is required for increased VLDL-triglyceride secretion by microsomal triglyceride transfer protein in ob/ob mice. J Lipid Res. 2008; 49(9):2013-2022. (Clone-specific: Western blot). View Reference
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Morral N, Edenberg HJ, Witting SR, Altomonte J, Chu T, Brown M. Effects of glucose metabolism on the regulation of genes of fatty acid synthesis and triglyceride secretion in the liver. J Lipid Res. 2007; 48(7):1499-1510. (Clone-specific: Western blot). View Reference
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Nakamuta M, Chang BH, Hoogeveen R, Li WH, Chan L. Mouse microsomal triglyceride transfer protein large subunit: cDNA cloning, tissue-specific expression and chromosomal localization. Genomics. 1996; 33(2):313-316. (Biology). View Reference
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Qin B, Anderson RA, Adeli K. Tumor necrosis factor-alpha directly stimulates the overproduction of hepatic apolipoprotein B100-containing VLDL via impairment of hepatic insulin signaling. Am J Physiol Gastrointest Liver Physiol. 2008; 294(5):G1120-1129. (Clone-specific: Western blot). View Reference
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Read J, Anderson TA, Ritchie PJ. A mechanism of membrane neutral lipid acquisition by the microsomal triglyceride transfer protein. J Biol Chem. 1999; 275(39):30372-30377. (Biology). View Reference
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Wetterau JR, Gregg RE, Harrity TW. An MTP inhibitor that normalizes atherogenic lipoprotein levels in WHHL rabbits. Science. 1998; 282(5389):751-754. (Biology). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.