|Application ||WB, E|
|Calculated MW||58113 Da|
|Antigen Region||285-314 aa|
|Other Names||Prosaposin, Proactivator polypeptide, Saposin-A, Protein A, Saposin-B-Val, Saposin-B, Cerebroside sulfate activator, CSAct, Dispersin, Sphingolipid activator protein 1, SAP-1, Sulfatide/GM1 activator, Saposin-C, A1 activator, Co-beta-glucosidase, Glucosylceramidase activator, Sphingolipid activator protein 2, SAP-2, Saposin-D, Component C, Protein C, PSAP, GLBA, SAP1|
|Target/Specificity||This SAP antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 285-314 amino acids from the Central region of human SAP.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SAP Antibody (Center E300) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 18.104.22.168) and galactosylceramide by beta-galactosylceramidase (EC 22.214.171.124). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 126.96.36.199). Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.|
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Provided below are standard protocols that you may find useful for product applications.
PSAP is 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.
Gunia,S., Virchows Arch. 454 (5), 573-579 (2009)
Kuchar,L., Am. J. Med. Genet. A 149A (4), 613-621 (2009)
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