PSAP recombinant protein

Recombinant Human PSAP protein

Cat. Num. AAA1561889

• Gene Names: PSAP; GLBA; SAP1
• Purity: >90% as determined by SDS-PAGE
• Synonyms: PSAP; Recombinant Human PSAP protein; Prosaposin; Proactivator polypeptide; A1 activator; Co-beta-glucosidase; Glucosylceramidase activator; Sphingolipid activator protein 2; SAP-2; PSAP recombinant protein

• Host: E Coli
• Purity/Purification: >90% as determined by SDS-PAGE
• Form/Format: Lyophilized. Lyophilized from PBS pH 7.4, 0.2% NLS, 5% Trehalose, 5% Mannose, 1mM EDTA.

• Species: Homo sapiens (Human)
• Protein Construction: A DNA sequence encoding the human PSAP (Gly17-Asn524) was fused with His tag
• Reconstitution: Reconstitute in sterile water for a stock solution.
• Preparation and Storage: Store at 2 to 8 degree C for one week. Store at -20 to -80 degree C for twelve months from the date of receipt. Use a manual defrost freezer and avoid repeated freeze thaw cycles.; In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.

Related Product Information for PSAP recombinant protein

SH2 domain-containing protein 1A (SH2D1A/SAP) is a 128 amino acid protein, containing a single Src homology 2 (SH2) domain, flanked by 5 amino acids at the N-terminus and 25 amino acids at the C-terminus. The absence of a catalytic domain and the presence of an SH2 domain suggest that SH2D1A regulates one or more signal transduction pathways. SH2D1A interacts with signaling lymphocytic activation molecule (SLAM), which is a transmembrane protein expressed on the surface of activated T and B cells. SH2D1A (SAP) interacts via its SH2 domain with a motif (TIYXXV) present in the cytoplasmic tail of the cell-surface receptors, including CD15/SLAM, CD84, CD229/Ly-9, and CD244/2B4. SH2D1A was expressed in EBV-carrying, tumor phenotype representative (type I), but not in EBV-carrying lymphoblastoid cell line (LCL)-like (type III) or EBV-negative Burkitt lymphoma (BL) lines. It has been supposed to be related to the X-linked lymphoproliferative disease which is also known as Duncan's disease or Purtilo syndrome.

Product Categories/Family for PSAP recombinant protein

Protein

NCBI and Uniprot Product Information

• NCBI GI #: 110224476
• NCBI GeneID: 5660
• NCBI Accession #: NP_001035930.1
• NCBI GenBank Nucleotide #: NM_001042465.1
• UniProt Accession #: P07602; P07292; P15793; P78538; P78541; P78546; P78547; P78558; Q53Y86; Q6IBQ6; Q92739; Q92740
• Molecular Weight: 58,113 Da
• NCBI Official Full Name: proactivator polypeptide isoform b preproprotein
• NCBI Official Synonym Full Names: prosaposin
• NCBI Official Symbol: PSAP
• NCBI Official Synonym Symbols: GLBA; SAP1
• NCBI Protein Information: proactivator polypeptide; sphingolipid activator protein-1
• UniProt Protein Name: Proactivator polypeptide
• Protein Family: Prosaposin
• UniProt Gene Name: PSAP
• UniProt Synonym Gene Names: GLBA; SAP1; CSAct; SAP-1; SAP-2
• UniProt Entry Name: SAP_HUMAN

NCBI Description

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]

Uniprot Description

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; extracellular space; lysosomal lumen; mitochondrion; intracellular membrane-bound organelle; lysosomal membrane; nucleolus; integral to membrane; extracellular region

Molecular Function: protein binding; enzyme activator activity; lipid binding

Biological Process: positive regulation of catalytic activity; platelet activation; regulation of lipid metabolic process; platelet degranulation; sphingolipid 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