Product nameRecombinant Human PSAP protein
See all PSAP proteins and peptides
Purity> 95 % Densitometry.
ab167924 was purifed using Ni-NTA chromatography.
Endotoxin level< 1.000 Eu/µg
Expression systemHEK 293 cells
Protein lengthFull length protein
SequenceASGPVLGLKE CTRGSAVWCQ NVKTASDCGA VKHCLQTVWN KPTVKSLPCD ICKDVVTAAG DMLKDNATEE EILVYLEKTC DWLPKPNMSA SCKEIVDSYL PVILDIIKGE MSRPGEVCSA LNLCESLQKH LAELNHQKQL ESNKIPELDM TEVVAPFMAN IPLLLYPQDG PRSKPQPKDN GDVCQDCIQM VTDIQTAVRT NSTFVQALVE HVKEECDRLG PGMADICKNY ISQYSEIAIQ MMMHMQPKEI CALVGFCDEV KEMPMQTLVP AKVASKNVIP ALELVEPIKK HEVPAKSDVY CEVCEFLVKE VTKLIDNNKT EKEILDAFDK MCSKLPKSLS EECQEVVDTY GSSILSILLE EVSPELVCSM LHLCSGTRLP ALTVHVTQPK DGGFCEVCKK LVGYLDRNLE KNSTKQEILA ALEKGCSFLP DPYQKQCDQF VAEYEPVLIE ILVEVMDPSF VCLKIGACPS AHKPLLGTEK CIWGPSYWCQ NTETAAQCNA VEHCKRHVWN KLHHHHHH
Predicted molecular weight58 kDa including tags
Amino acids17 to 524
TagsHis tag C-Terminus
Our Abpromise guarantee covers the use of ab167924 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -80°C.
Constituents: 99% Phosphate Buffer, 0.43% Sodium chloride
ReconstitutionAdd 200µl of deionized water to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage.
Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
- A1 activator
- Cerebroside sulfate activator
FunctionThe lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymic proteins: the sphingolipids activator proteins (coproteins).
Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 184.108.40.206) and galactosylceramide by beta-galactosylceramidase (EC 220.127.116.11). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.
Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 18.104.22.168), GM1 gangliosides by beta-galactosidase (EC 22.214.171.124) and globotriaosylceramide by alpha-galactosidase A (EC 126.96.36.199). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 188.8.131.52).
Involvement in diseaseDefects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:611721]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.
Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:249900]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis.
Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:610539]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.
Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:611722]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.
Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).
Sequence similaritiesContains 2 saposin A-type domains.
Contains 4 saposin B-type domains.
modificationsThis precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.
N-linked glycans show a high degree of microheterogeneity.
The one residue extended Saposin-B-Val is only found in 5% of the chains.
- Information by UniProt
12% SDS-PAGE analysis of ab167924
Lane 1: reduced and boiled sample, 2.5μg/lane
Lane 2: non-reduced and non-boiled sample, 2.5μg/lane
The ~66 kDa band corresponds to whole PSAP (prosaposin) molecule that consists of four saposin units. The individual saposins naturally cleave off the prosaposin which results in ~15, ~35 and ~50 kDa fragments of mono-, di- and trisaposins, respectively.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab167924 has not yet been referenced specifically in any publications.