Recombinant Human SMPDL3B protein (GST tag N-Terminus)
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Recombinant Human SMPDL3B protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 373 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
ASML3B, ASMLPD, SMPDL3B, Acid sphingomyelinase-like phosphodiesterase 3b, ASM-like phosphodiesterase 3b
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SMPDL3B protein (GST tag N-Terminus) (AB162135)
ab162135 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SMPDL3B regulates various cellular processes such as apoptosis proliferation and differentiation by controlling ceramide levels. It does not typically function as part of a larger protein complex but interacts with membrane components to exert its enzymatic activity. SMPDL3B modulates signal transduction pathways that are sensitive to changes in membrane lipid composition influencing cellular responses to stress and immune signals.
Pathways
SMPDL3B is involved in the sphingolipid metabolism pathway and the cholesterol metabolism pathway. It interacts with other sphingolipid enzymes like acid ceramidase which further regulates ceramide levels. SMPDL3B affects the activation of signaling proteins like protein kinase C which links it to various cellular responses. Changes in sphingolipid metabolism can influence pathways linked to cell survival and inflammation.
Specifications
Form
Liquid
General info
Function
Lipid-modulating phosphodiesterase (PubMed : 26095358). Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling (By similarity). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown (PubMed : 26095358). Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (By similarity).
Sequence similarities
Belongs to the acid sphingomyelinase family.
Post-translational modifications
N-glycosylated.
Target data
Product promise
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