Recombinant Human Proactivator Polypeptide (PSAP) Protein (GST)

Name: Recombinant Human Proactivator Polypeptide (PSAP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04400P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Proactivator Polypeptide (PSAP) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07602
Target Symbol	PSAP
Synonyms	A1 activator; Cerebroside sulfate activator; Co-beta-glucosidase; Component C; CSAct; Dispersin; GLBA; Glucosylceramidase activator; Proactivator polypeptide; Proactivator polypeptide precursor; Prosaposin (sphingolipid activator protein 1); prosaposin (variant Gaucher disease and variant metachromatic leukodystrophy); Prosaposin; Protein A; Protein C; PSAP; SAP 1; SAP 2; SAP-1; SAP-2; SAP_HUMAN; SAP1; Saposin A; Saposin B; Saposin B Val; Saposin C; Saposin D; Saposin-D; Saposins; Sgp1; Sphingolipid activator protein 1; Sphingolipid activator protein 2; Sulfated glycoprotein 1; Sulfatide/GM1 activator
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	SDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGT
Expression Range	311-391aa
Protein Length	Partial
Mol. Weight	36.1kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). 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 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.; Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.; 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.
Subcellular Location	Lysosome.; [Prosaposin]: Secreted.
Database References	HGNC: 9498 OMIM: 176801 KEGG: hsa:5660 STRING: 9606.ENSP00000378394 UniGene: PMID: 28541286 Both PSAP reduction and overexpression lead to significantly elevated extracellular progranulin (PGRN) levels. Intriguingly, PSAP knockdown increases PGRN monomers, whereas PSAP overexpression increases PGRN oligomers, partly through a protein-protein interaction. PMID: 27356620 Study demonstrated that the binding of CST3 and PSAP decreased the inhibitory effects of CST3 on proteinase in vitro. The co-localization of both proteins was detected in cultured cells and in Bunina body-containing motor neurons from patients with amyotrophic lateral sclerosis, suggesting that they might be involved in the process of Bunina body formation. PMID: 29249381 This report documents the successful use of plasma lysoSLs profiling in the PSAP deficiency diagnosis, as a reliable and informative tool to obtain a preliminary information in infantile cases with complex traits displaying severe neurological signs and visceral involvement. PMID: 26831127 an extensive review of all the PSAP-causative variants published in the literature to date, accounting for a total of 10 PSAP allele types (review) PMID: 26462614 Our findings suggest a novel pharmacological approach to Sap C deficiency directed to treat major secondary pathological aspects in this disorder. PMID: 25926625 PSAP is a secreted biomarker. PMID: 26341737 Data suggested that the abundance of Psap in sperm sample may be a sensitive endpoint to predict PCB exposure. PMID: 26045750 Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin. PMID: 26370502 findings support a lung metastasis-promoting function of the miR-23b/27b/24 cluster of miRNAs, which functions in part through the direct inhibition of PSAP in breast cancer PMID: 24966325 Of the 2575 proteins identified, proteins upregulated in gallbladder cancer included several lysosomal proteins such as prosaposin, cathepsin Z and cathepsin H. PMID: 24657443 Saposin C protects glucocerebrosidase against alpha-synuclein inhibition. PMID: 24070323 Urine of patients with early prostate cancer contains lower levels of light chain fragments of inter-alpha-trypsin inhibitor and prosaposin fragment or saposin B. PMID: 23417432 These findings suggested that prosaposin might enhance estrogen receptor alpha-mediated signaling axis and play a role in breast cancer development and progression. PMID: 22738294 PSAP is a novel TFPI-2-interacting protein and that the binding sites are the KD2 of TFPI-2 and the C-terminus of PSAP. PMID: 21943334 novel esophageal squamous cell carcinoma marker PSAP was identified by mass spectrometry and immunohistochemical analysis PMID: 21743296 PSAP is a target gene of the BACH1 transcription factor according to ChIP-seq analysis in HEK 293 cells. PMID: 21555518 saposin C caused stimulation of androgen receptor expression and activity by associations with Src kinases PMID: 21328455 Saposin B(Sap B) is not a limiting factor of the coupled Sap B-arylsulfatase A reaction in mouse kidney cells even if sulfatide has accumulated to unphysiologically high levels PMID: 19224915 The biological properties of cells from four recently described Gaucher disease patients carrying mutations in the Sap C domain of the PSAP gene have been characterized. PMID: 20484222 PSAP is involved in prostate cancer invasion. PMID: 20132547 reconstruction of the order of internal duplications that gave rise to the four saposins by using phylogenetic tools PMID: 11734895 procathepsin D interacts with prosaposin in human breast and ovarian cancer cells. PMID: 12083803 crystal structure reveals a dimeric shell for lipid binding PMID: 12518053 data indicate that saposin C is required for acid beta-glucosidase resistance to proteolytic degradation in the cell PMID: 12813057 The structure of saposin C compared to other saposin-fold family members provides an explanation for function variability of this protein family. PMID: 14674747 model proposed in which saposin C exposes lipid antigens from intralysosomal membranes for loading onto CD1b PMID: 14716313 There might be a potential pleuripotent regulatory function for prosaposin in prostate cancer. PMID: 15305334 Amplification and overexpression of PSAP was studied in prostatic neoplasms. PMID: 16080200 determination of crystal structure of human saposins A and C to 2.0 Angstroms and 2.4 Angstroms, respectively and both reveal the compact, monomeric saposin fold PMID: 16823039 FSAP (Factor VII-activating protease) can cleave and inactivate PDGF-BB (platelet-derived growth factor-BB) and thereby inhibits VSMC (vascular smooth-muscle cell) proliferation. PMID: 17300216 saposin B may facilitate lipid binding to CD1d molecules throughout the endocytic pathway PMID: 17372201 an unglycosylated Sap-B variant, Asn215His, which causes a fatal sphingolipid storage disease, lost the ability to extract membrane lipids at acidic pH in the presence of BMP PMID: 17561962 Expression of saposin C-originated saposin C may upregulate AR gene expression and activate the androgen receptor transcriptional function in an androgen-independent manner in prostate cancer cells. PMID: 17712477 These data for the first time demonstrate that not only saposin C or PSAP regulates AR expression/activity, but also function as an androgen-regulated gene in prostate stromal cells. PMID: 18481277 findings point to the role of lipid rafts in the prosaposin-triggered signalling pathway, thus supporting a role for this factor as a new component of the multimolecular signalling complex involved in the neurotrophic response. PMID: 18761669 two new patients with PSAP gene defects; one, with pSap-d, who had a severe neurovisceral dystrophy and died as a neonate, and the other with SapB-d, who presented with a metachromatic leukodystrophy-like disorder but had normal arylsulfatase activity PMID: 19267410 Report the up-regulation of prosaposin in the senescent fibroblasts and endothelial cells. PMID: 19471889 Prosaposin functions in a paracrine and endocrine fashion by stimulating the expression of thrombospondin-1 (Tsp-1) in fibroblasts present in both primary tumors and distant organs, doing so in a p53-dependent manner. PMID: 19581582 Saposin C or its precursor (PSAP) function as an androgen-agonist and upregulate androgen receptor and prostate-specific antigen expression/activity in androgen-responsive prostate cancer cells LNCaP, TRAMP-C1 and -C2., and CWR 22RV1. PMID: 17044040 Prosaposin is an androgen-target gene and its expression in androgen-responsive prostate cancer cells can be upregulated by male hormones. PMID: 17171640 Cloning of prosaposin gene from androgen-independent (AI) prostate cancer (PCa) cells and it genomic amplification in human metastatic AI PCa cell lines and punch biopsy samples of prostate cancer xenografts and lymph node metastases. PMID: 16080200 Saposin C stimulates prostate cancer and stromal cells growth and invasion and uPA/uPAR expression, and activates p42/44 and SAPK/JNK signaling pathways of MAPK. PMID: 15897971 Prosaposin and/or saposin C via modulation of caspases expression/activity and/or PI3K/Akt signaling pathway act as a survival and anti-apoptotic factor for prostate cancer cells. PMID: 15548330

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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