Sphingosine-1-phosphate lyase1 Active human, recombinant, expressed in baculovirus infected insect c

Stock Code: 3592615
Manufacturer Part No: SRP0191-10UG
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Application

Useful for the study of biochemical function.

Biochem/physiol Actions

SGPL1 (sphingosine-1-phosphate lyase 1) enzyme is involved in the synthesis of long-chain aliphatic aldehydes which occurs during several metabolic processes, such as peroxisomal ?-oxidation of 3-methyl-branched fatty acids and 2-hydroxy long-chain fatty acids, microsomal oxidation of long-chain alcohols, prenylated protein degradation in the lysosomes, microsomal degradation of phosphorylated sphingoid bases, attack of plasmalogens by myeloperoxidase (MPO)-derived hypochlorous acid, and degradation of (lyso)plasmalogens in the microsomes.s This protein shows reduced expression in OSCC (oral squamous cell carcinoma), colon and prostate cancers, and this is associated with poor prognosis.

General description

SGPL1 (sphingosine-1-phosphate lyase 1) is an ER (endoplasmic reticulum) enzyme which shows a wide level of tissue expression. This protein is composed of putative 568 amino acids, and has a molecular weight of 63.5kDa. This enzyme is a member of the pyridoxal 5?-phosphate-dependent carbon-carbon lyases, which form a subclass of aldehyde lyases. It is a type III membrane protein, also known as type I membrane protein which lacks a cleavable N-terminal signal sequence. The single transmembrane segment is in proximity to the N-terminal which faces the ER lumen. The catalytic region faces the cytoplasm.

Physical form

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 10% glycerol, 3 mM DTT, 0.5 mM pyridoxal 5′ phosphate monohydrate.

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

ManufacturerSIGMA-ALDRICH
Formaqueous solution
Assay≥70% (SDS-PAGE)

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