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Purified Mouse Anti-LCB1
Product Details
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BD Transduction Laboratories™
Rat (QC Testing), Human, Mouse (Tested in Development)
Mouse IgG1
Mouse LCB1 aa. 121-238
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
53 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Western blot:  Please refer to

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to for technical protocols.
  3. 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.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
611305 Rev. 1
Antibody Details
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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.

611305 Rev. 1
Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
611305 Rev.1
Citations & References
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Development References (2)

  1. 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
  2. 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
611305 Rev. 1

Please refer to Support Documents for Quality Certificates

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.