Specification
| Description | Recombinant protein from the full-length sequence of homo sapiens lipoprotein lipase (LPL) (NM_000237). |
| 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 | P06858 |
| Entry Name | LIPL_HUMAN |
| Gene Names | LPL LIPD |
| Alternative Gene Names | LIPD |
| Alternative Protein Names | Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) |
| 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 | 475 |
| Molecular Weight(Da) | 53162 |
| Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG |
Background
| Function | FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619, PubMed:11342582, PubMed:27578112). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:7592706, PubMed:12032167). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232). {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8675619}. |
| Pathway | |
| Protein Families | AB hydrolase superfamily, Lipase family |
| Tissue Specificity | Detected in blood plasma (PubMed:2340307, PubMed:11893776, PubMed:12641539). Detected in milk (at protein level) (PubMed:2340307). {ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:2340307}. |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |