Recombinant Mouse Lysosomal Acid Glucosylceramidase (GBA)

Name: Recombinant Mouse Lysosomal Acid Glucosylceramidase (GBA)
Brand: Beta LifeScience
SKU: BLC-07407P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Lysosomal Acid Glucosylceramidase (GBA) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17439
Target Symbol	GBA
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	AQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRMELSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPTQKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLPEEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLGFTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEAAKYVHGIAVHWYMDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVTGWTDWNLALNPEGGPNWVRNFVDSPIIVDIPKDAFYKQPMFYHLGHFSKFIPEGSQRVALVASESTDLETVALLRPDGSAVVVVLNRSSEDVPLTISDPDLGFLETVSPGYSIHTYLWRRQ
Expression Range	20-515aa
Protein Length	Full Length of Mature Protein
Mol. Weight	55.6 kDa
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	Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose. Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation. Also plays a role in cholesterol metabolism. May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol. The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction. Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide. Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol.
Subcellular Location	Lysosome membrane; Peripheral membrane protein; Lumenal side.
Protein Families	Glycosyl hydrolase 30 family
Database References	KEGG: mmu:14466 STRING: 10090.ENSMUSP00000076589 UniGene: PMID: 29173981 The data support the contention that prolonged antagonism of glucosylceramide synthase (GCS)in the central nervous system (CNS)can affect alpha-synuclein processing and improve behavioral outcomes. Hence, inhibition of GCS represents a disease-modifying therapeutic strategy for GBA-related synucleinopathies and conceivably for certain forms of sporadic disease PMID: 28223512 These results indicate that Gba1 deficiency enhances neuronal vulnerability to neurodegenerative processes triggered by increased alpha-synuclein expression. PMID: 28969384 This study demonstrated that the gba1 deficiency mice showed gene regulation expression of the type I interferon. PMID: 27175482 Rab7 accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR impairment, we anticipate that strategies to restore GCase activity in the brains of both sporadic patients with PD and those with GBA1 mutations will improve autophagy lysosomal pathway, preventing the accumulation of a-synuclein and spread of pathology. PMID: 27378698 heterozygosity for a Gaucher disease-associated mutation in glucocerebrosidase interferes with alpha-synuclein degradation and contributes to its accumulation PMID: 25351739 Data indicate that ABC transporter A family member 12 knockout (Abca12(-/-)) epidermis had 5-fold more beta-glucocerebrosidase (GCase) protein, and a 5-fold increase in GCase activity. PMID: 24293640 These results demonstrate, for the first time, a novel function of GBA1 as a beta-ChlGlc-synthesizing enzyme. PMID: 24211208 Substrate compositional variation with tissue/region and Gba1 mutations in mouse models--implications for Gaucher disease. PMID: 23520473 GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples. PMID: 22659419 results not only point to a fundamental role for GBA in immune regulation but also suggest that GBA mutations in GD may cause widespread immune dysregulation through the accumulation of substrates PMID: 22665763 This study suggested that several leads connecting GBA1 mutations with alpha-synuclein misprocessing have emerged as potential targets for the treatment of GBA1-related synucleinopathies. PMID: 22327140 IFG stabilizes GCase in tissues and serum and can reduce visceral substrates in vivo. PMID: 22167193 Mutations in GBA1 can cause Parkinson disease-like alpha-synuclein pathology; rescuing brain glucocerebrosidase activity might represent a therapeutic strategy for GBA1-associated synucleinopathies. PMID: 21730160 evidence for the involvement of deletion of the GBA1 gene in multiple cell lineages in nonneuronopathic type 1 Gaucher disease PMID: 20962279 The saposin C deficient mice backcrossed to point mutated GCase mimics the central nervous system phenotype and biochemistry of some type 3 (neuronopathic) variants of Gaucher disease. PMID: 20047948 isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase PMID: 20148966 Saposin C has multiple roles in glycosphingolipid catabolism and functions in Central Nervous System independent of its role as an stabilizer of GCase. PMID: 20015957 mRNA shows generalized low level expression early in gestation with gradual appearance of differential expression appearing around gestational age E14 and significantly increasing at term and into adulthood. PMID: 11749048 Results indicate that glucocerebrosidase deficiency, even in the absence of large amounts of sphingolipid storage, can trigger an inflammatory reaction. PMID: 11994410 data indicate that saposin C is required for acid beta-glucosidase resistance to proteolytic degradation in the cell PMID: 12813057

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.