Human SMPD1 Protein 2242

$375.00 – $1,250.00

Summary

Expression: Baculovirus-Insect Cells
Active: Yes (catalytic)
Amino Acid Range: Met1-Pro628

SKU: 2242parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_000534.3
express system	Baculovirus-Insect Cells
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Sphingomyelin phosphodiesterase 1 (SMPD1) converts sphingomyelin into ceramide and phosphocholine; hence, loss of SMPD1 function causes abnormal accumulation of sphingomyelin in lysosomes, which results in the lipid-storage disorder Niemann-Pick disease (types A and B). SMPD1 activity is dependent on zinc, which is coordinated at the active site of the enzyme.
molecular weight	The protein has a predicted MW of 66.53 kDa. Due to glycosylation, the protein migrates to 67-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human SMPD1 Protein 2242

protein

Size and concentration 100, 500µg and liquid
Form Liquid
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped with dry ice.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Sphingomyelin phosphodiesterase 1 (SMPD1) converts sphingomyelin into ceramide and phosphocholine; hence, loss of SMPD1 function causes abnormal accumulation of sphingomyelin in lysosomes, which results in the lipid-storage disorder Niemann-Pick disease (types A and B). SMPD1 activity is dependent on zinc, which is coordinated at the active site of the enzyme.
Protein names Sphingomyelin phosphodiesterase (EC 3.1.4.12) (EC 3.1.4.3) (Acid sphingomyelinase) (aSMase) [Cleaved into: Sphingomyelin phosphodiesterase, processed form]
Protein family Acid sphingomyelinase family
Mass 69936Da
Function Converts sphingomyelin to ceramide (PubMed:12563314, PubMed:1840600, PubMed:18815062, PubMed:25339683, PubMed:25920558, PubMed:27659707, PubMed:33163980). Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly (PubMed:20807762, PubMed:21098024, PubMed:9660788). However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form (PubMed:12563314, PubMed:20530211, PubMed:20807762, PubMed:22573858, PubMed:9393854). {ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:1840600, ECO:0000269\|PubMed:18815062, ECO:0000269\|PubMed:20530211, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:21098024, ECO:0000269\|PubMed:22573858, ECO:0000269\|PubMed:25339683, ECO:0000269\|PubMed:25920558, ECO:0000269\|PubMed:27659707, ECO:0000269\|PubMed:33163980, ECO:0000269\|PubMed:9393854, ECO:0000269\|PubMed:9660788, ECO:0000305}.; In the lysosomes, converts sphingomyelin to ceramide (PubMed:20807762, PubMed:21098024). Plays an important role in the export of cholesterol from the intraendolysosomal membranes (PubMed:25339683). Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol (PubMed:25339683). Modulates stress-induced apoptosis through the production of ceramide (PubMed:8706124). {ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:21098024, ECO:0000269\|PubMed:25339683, ECO:0000269\|PubMed:8706124}.; When secreted, modulates cell signaling with its ability to reorganize the plasma membrane by converting sphingomyelin to ceramide (PubMed:12563314, PubMed:17303575, PubMed:20807762). Secreted form is increased in response to stress and inflammatory mediators such as IL1B, IFNG or TNF as well as upon infection with bacteria and viruses (PubMed:12563314, PubMed:20807762, PubMed:9393854). Produces the release of ceramide in the outer leaflet of the plasma membrane playing a central role in host defense (PubMed:12563314, PubMed:20807762, PubMed:9393854). Ceramide reorganizes these rafts into larger signaling platforms that are required to internalize P. aeruginosa, induce apoptosis and regulate the cytokine response in infected cells (PubMed:12563314). In wounded cells, the lysosomal form is released extracellularly in the presence of Ca(2+) and promotes endocytosis and plasma membrane repair (PubMed:20530211). {ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:17303575, ECO:0000269\|PubMed:20530211, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:9393854}.; [Sphingomyelin phosphodiesterase, processed form]: This form is generated following cleavage by CASP7 in the extracellular milieu in response to bacterial infection (PubMed:21157428). It shows increased ability to convert sphingomyelin to ceramide and promotes plasma membrane repair (By similarity). Plasma membrane repair by ceramide counteracts the action of gasdermin-D (GSDMD) perforin (PRF1) pores that are formed in response to bacterial infection (By similarity). {ECO:0000250\|UniProtKB:Q04519, ECO:0000269\|PubMed:21157428}.; (Microbial infection) Secretion is activated by bacteria such as P. aeruginos, N. gonorrhoeae and others, this activation results in the release of ceramide in the outer leaflet of the plasma membrane which facilitates the infection. {ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:9393854, ECO:0000305\|PubMed:31155842}.; (Microbial infection) Secretion is activated by human coronaviruses SARS-CoV and SARS-CoV-2 as well as Zaire ebolavirus, this activation results in the release of ceramide in the outer leaflet of the plasma membrane which facilitates the infection. {ECO:0000269\|PubMed:22573858, ECO:0000269\|PubMed:33163980}.; [Isoform 2]: Lacks residues that bind the cofactor Zn(2+) and has no enzyme activity. {ECO:0000269\|PubMed:1840600, ECO:0000305}.; [Isoform 3]: Lacks residues that bind the cofactor Zn(2+) and has no enzyme activity. {ECO:0000269\|PubMed:1840600, ECO:0000305}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:15877209, ECO:0000269\|PubMed:1718266, ECO:0000269\|PubMed:1840600, ECO:0000269\|PubMed:18815062, ECO:0000269\|PubMed:22573858, ECO:0000269\|PubMed:25339683, ECO:0000269\|PubMed:26084044, ECO:0000269\|PubMed:27349982, ECO:0000269\|PubMed:33163980, ECO:0000269\|PubMed:8702487, ECO:0000269\|PubMed:8706124}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000269\|PubMed:25339683, ECO:0000305\|PubMed:12563314, ECO:0000305\|PubMed:1840600, ECO:0000305\|PubMed:22573858, ECO:0000305\|PubMed:33163980, ECO:0000305\|PubMed:8706124}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-octadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:54284, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72961, ChEBI:CHEBI:83358, ChEBI:CHEBI:295975; Evidence={ECO:0000269\|PubMed:25339683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54285; Evidence={ECO:0000269\|PubMed:25339683}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-dihexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:45304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:82929, ChEBI:CHEBI:295975; Evidence={ECO:0000269\|PubMed:25339683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45305; Evidence={ECO:0000305\|PubMed:25339683}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; Evidence={ECO:0000269\|PubMed:25339683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605; Evidence={ECO:0000305\|PubMed:25339683}; CATALYTIC ACTIVITY: [Sphingomyelin phosphodiesterase, processed form]: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269\|PubMed:21157428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000305\|PubMed:21157428};
Subellular location Lysosome {ECO:0000269\|PubMed:16787399, ECO:0000269\|PubMed:18815062, ECO:0000269\|PubMed:20530211, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:27659707, ECO:0000269\|PubMed:9660788}. Lipid droplet {ECO:0000269\|PubMed:25339683}. Secreted {ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:16787399, ECO:0000269\|PubMed:17303575, ECO:0000269\|PubMed:20530211, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:22573858, ECO:0000269\|PubMed:27659707, ECO:0000269\|PubMed:8702487, ECO:0000269\|PubMed:9030779, ECO:0000269\|PubMed:9660788}. Note=The secreted form is induced in a time- and dose-dependent by IL1B and TNF as well as stress and viral infection. This increase of the secreted form seems to be due to exocytosis of the lysosomal form and is Ca(2+)-dependent (PubMed:20530211, PubMed:20807762, PubMed:22573858). Secretion is dependent of phosphorylation at Ser-510 (PubMed:17303575). Secretion is induced by inflammatory mediators such as IL1B, IFNG or TNF as well as infection with bacteria and viruses (PubMed:12563314, PubMed:20807762). {ECO:0000269\|PubMed:12563314, ECO:0000269\|PubMed:17303575, ECO:0000269\|PubMed:20530211, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:22573858}.; [Sphingomyelin phosphodiesterase, processed form]: Secreted, extracellular space {ECO:0000250\|UniProtKB:Q04519}. Note=This form is generated following cleavage by CASP7. {ECO:0000250\|UniProtKB:Q04519}.
Structure Monomer. Interacts with SORT1; the interaction is required for SMPD1 targeting to lysosomes (PubMed:16787399). {ECO:0000269\|PubMed:16787399, ECO:0000269\|PubMed:27349982}.
Post-translational modification Proteolytically processed (PubMed:21098024, PubMed:9030779). Mature lysosomal form arises from C-terminal proteolytic processing of pro-sphingomyelin phosphodiesterase (PubMed:21098024). {ECO:0000269\|PubMed:21098024, ECO:0000269\|PubMed:9030779}.; [Sphingomyelin phosphodiesterase, processed form]: This form is generated following cleavage by CASP7 in the extracellular milieu (PubMed:21157428). It shows increased activity (By similarity). {ECO:0000250\|UniProtKB:Q04519, ECO:0000269\|PubMed:21157428}.; Both lysosomal and secreted forms are glycosylated but they show a differential pattern of glycosylation. {ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:9030779}.; Phosphorylated at Ser-510 by PRKCD upon stress stimuli. Phosphorylation is required for secretion. {ECO:0000269\|PubMed:17303575, ECO:0000269\|PubMed:20807762, ECO:0000269\|PubMed:9030779}.
Target Relevance information above includes information from UniProt accession: P17405
The UniProt Consortium

Data

Measured by its ability to cleave 2-N-Hexadecanoylamino-4-nitrophenylphosphorylcholine (HNPPC). The specific activity is > 1500 pmol/min/µg, as measured under the described conditions.

The purity of Human SMPD1 is greater than 95% as determined by SEC-HPLC.

Human SMPD1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.