protein

Recombinant Human Prosaposin

MBS145818

0.002 mg

140 USD

Recombinant Protein

Recombinant Human Prosaposin

[Prosaposin]

[Prosaposin; Proactivator polypeptide; PSAP; GLBA; SAP1]

[prosaposin isoform b preproprotein; Prosaposin; prosaposin; proactivator polypeptide; sphingolipid activator protein-1; prosaposin; Proactivator polypeptideCleaved into the following 5 chains:Saposin-AAlternative name(s):Protein A]

[PSAP]

[PSAP; PSAP; GLBA; SAP1; GLBA; SAP1; CSAct; SAP-1; SAP-2]

SAP_HUMAN

AS GPVLGLKE 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 .

Greater than 95.0% as determined by SDS-PAGE.

Filtered (0.4 um) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4

Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time .

Source: HEK 293. Physical Appearance: Filtered White lyophilized (freeze-dried) powder.

Solubility: It is recommended to add 200 ul deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PSAP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins

PSAP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-524) containing a total of 518 amino acids, having a molecular mass of 57.7kDa (calculated), though it migrates at approximately 65kDa on SDS PAGE, the PSAP is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and a 6 a.a His tag at C-Terminus.The Human PSAP is purified by proprietary chromatographic techniques.

110224476

NP_001035930.1

NM_001042465.1

P07602

Class A/1 (Rhodopsin-like Receptors) Pathway (106357); Defective ACTH Causes Obesity And Pro-opiomelanocortinin Deficiency (POMCD) Pathway (1127664); Disease Pathway (530764); GPCR Ligand Binding Pathway (161020); Glycosphingolipid Metabolism Pathway (530751); Hemostasis Pathway (106028); Lysosome Pathway (99052); Lysosome Pathway (96865); Metabolic Disorders Of Biological Oxidation Enzymes Pathway (1127637); Metabolism Pathway (477135)

This gene encodes a highly conserved glycoprotein which is a precursor for 4 cleavage products: saposins A, B, C, and D. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Mutations in this gene have been associated with Gaucher disease, Tay-Sachs disease, and metachromatic leukodystrophy. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]

PSAP: The 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). Defects in PSAP are the cause of combined saposin deficiency (CSAPD); 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). 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). 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). AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease. Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis). 3 isoforms of the human protein are produced by alternative splicing. Chromosomal Location of Human Ortholog: 10q21-q22. Cellular Component: nucleoplasm; Golgi apparatus; lysosomal lumen; extracellular space; mitochondrion; intracellular membrane-bound organelle; lysosomal membrane; integral to membrane; extracellular region; nucleolus. Molecular Function: protein binding; enzyme activator activity; lipid binding. Biological Process: positive regulation of catalytic activity; platelet activation; sphingolipid metabolic process; platelet degranulation; regulation of lipid metabolic process; regulation of MAPKKK cascade; glycosphingolipid metabolic process; lipid transport; blood coagulation. Disease: Gaucher Disease, Atypical, Due To Saposin C Deficiency; Metachromatic Leukodystrophy Due To Saposin B Deficiency; Krabbe Disease, Atypical, Due To Saposin A Deficiency; Combined Saposin Deficiency

0.002 mg

140 USD

0.01 mg

205

1 mg

5015