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Western blot analysis of LCB1 on a rat kidney lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-LCB1 antibody.
BD Transduction Laboratories™ Purified Mouse Anti-LCB1
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/pharmingen/protocols/Western_Blotting.shtml
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.
Companion Products
Sphingolipid biosynthesis is initiated by condensation of L-serine with palmitoyl coenzyme A, a reaction catalyzed by serine palmitoyltransferase (SPT). SPT is the rate-determining enzyme in the sphingolipid pathway. This enzyme is a key component for regulating cellular sphingolipid content. Initially identified in SPT-deficient S. cerevisiae strains, LCB1 and LCB2 homologs have been identified and characterized in mouse, human, and CHO cell lines. The mammalian LCB1 protein has 35% amino acid identity with yeast LCB1, while the mammalian LCB2 protein has 43% amino acid identity with yeast LCB2. Both LCB1 and LCB2 are transmembrane proteins containing protein localization sites, predicting they are membrane-bound enzymes enriched in the endoplasmic reticulum. In mouse tissue, LCB1 and LCB2 are expressed ubiquitously, with the highest levels detected in kidney and brain. Transfection of SPT-defective CHO mutant strains with LCB1-expressing plasmid restores both SPT activity and de novo sphingolipid synthesis to wild type levels. Thus, LCB1 may be an essential component of SPT activity during mammalian sphingolipid biosynthesis.
Development References (2)
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Hanada K, Hara T, Nishijima M, Kuge O, Dickson RC, Nagiec MM. A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis. J Biol Chem. 1997; 272(51):32108-32114. (Biology). View Reference
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Weiss B, Stoffel W. Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997; 249(1):239-247. (Biology). View Reference
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