Product nameRecombinant Human PSAP protein
See all PSAP proteins and peptides
Protein lengthFull length protein
SourceHEK 293 cells
Amino Acid Sequence
SequenceASGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCD ICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYL PVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDM TEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRT NSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEI CALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVY CEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTY GSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKK LVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIE ILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNA VEHCKRHVWNKLHHHHHH
Molecular weight58 kDa including tags
Amino acids17 to 524
TagsHis tag C-Terminus
Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included. Includes an N-terminal linker (extra amino acids AS).
Our Abpromise guarantee covers the use of ab203534 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Endotoxin level< 1.000 Eu/µg
Purity> 95 % SDS-PAGE.
Assessed by densitometry. Purifed using Ni-NTA chromatography.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -80°C.
Constituents: 99% Phosphate Buffer, 0.44% Sodium chloride
Lyophilized from a 0.4 µM filtered solution.
ReconstitutionAdd deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a week.
- 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 188.8.131.52) and galactosylceramide by beta-galactosylceramidase (EC 184.108.40.206). 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 220.127.116.11), GM1 gangliosides by beta-galactosidase (EC 18.104.22.168) and globotriaosylceramide by alpha-galactosidase A (EC 22.214.171.124). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 126.96.36.199).
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 ab203534.
Lane 1: Reduced and boiled sample, 2.5 μg/lane
Lane 2: Non-reduced and non-boiled sample, 2.5 μg/lane
The ~66KDa band corresponds to whole PSAP 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.
ab203534 has not yet been referenced specifically in any publications.