Specification
Description | Recombinant protein from the full-length sequence of homo sapiens glucosidase, beta, acid (GBA), transcript variant 1 (NM_000157). |
Organism | Homo sapiens (Human) |
Expression Host | Human Cells |
Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
Purity | Greater than 90% by SDS-PAGE gel |
Uniprot ID | P04062 |
Entry Name | GLCM_HUMAN |
Gene Names | GBA GC GLUC |
Alternative Gene Names | GC GLUC |
Alternative Protein Names | Lysosomal acid glucosylceramidase (Lysosomal acid GCase) (EC 3.2.1.45) (Acid beta-glucosidase) (Alglucerase) (Beta-glucocerebrosidase) (Beta-GC) (Cholesterol glucosyltransferase) (SGTase) (EC 2.4.1.-) (Cholesteryl-beta-glucosidase) (EC 3.2.1.-) (D-glucosyl-N-acylsphingosine glucohydrolase) (Imiglucerase) |
Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
Length | 536 |
Molecular Weight(Da) | 59716 |
Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ |
Background
Function | FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose (PubMed:9201993, PubMed:24211208, PubMed:15916907). Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Also plays a role in cholesterol metabolism (PubMed:24211208, PubMed:26724485). May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol (PubMed:24211208, PubMed:26724485). The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide (PubMed:26724485). Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol (PubMed:24211208, PubMed:26724485). {ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:27378698, ECO:0000269|PubMed:9201993}. |
Pathway | Steroid metabolism; cholesterol metabolism. Sphingolipid metabolism. |
Protein Families | Glycosyl hydrolase 30 family |
Tissue Specificity |
QC Data
Note | Please contact us for QC Data |
Product Image (Reference Only) | ![]() |