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Key Specifications Table
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, Porcine, Sh, Mi, Bab, R, B, Fe, Ch, Gp | DB, ELISA, FC, ICC, IH(P), IP, INHIB, WB | M | Purified | Monoclonal Antibody |
| Description | |
|---|---|
| Catalogue Number | MABS1350 |
| Description | Anti-Lipoprotein Lipase Antibody, clone 5D2 |
| Alternate Names |
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| Background Information | Lipoprotein lipase (EC 3.1.1.34; UniProt P06858; also known as LPL) is encoded by the LPL gene (Gene ID 280843) in bovine species. Lipoprotein lipase (LPL) catalyzes the hydrolysis of triglycerides in plasma lipoproteins. LPL is produced by adipocytes and myocytes and secreted into the interstitial spaces, where it is bound by GPIHBP1 (a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells) and shuttled to the luminal face of capillaries. The GPIHBP1 LPL complex is crucial for the binding of triglyceride-rich lipoproteins (TRLs) to endothelial cells and the subsequent lipolytic processing of TRLs. TRLs bind only the LPL-GPIHBP1 complex, but not GPIHBP1 alone, on the cell surface. A deficiency of either protein results in severe hypertriglyceridemia (chylomicronemia) and impaired delivery of lipid nutrients to parenchymal cells. Enzymatically active LPL appears to be a non-covalently linked homodimer with a head-to-tail subunit orientation that rapidly dissociates into inactive monomers. However, evidence for enzymatically active monomeric human LPL has also been presented. LPL is produced with a signal peptide sequence (a.a. 1-27), the removal of which yields the mature 448-amino acid (a.a. 28-475) enzyme containing a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain (a.a. 341-464) and a heparin-binding domain (a.a. 346-441). |
| Product Information | |
|---|---|
| Format | Purified |
| Presentation | Purified mouse IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide. |
| Quality Level | MQ100 |
| Applications | |
|---|---|
| Application | Detect Lipoprotein lipase using this mouse monoclonal Anti-Lipoprotein Lipase, clone 5D2 Antibody, Cat. No. MABS1350, validated for use in Dot Blot, ELISA, Flow Cytometry, Immunocytochemistry, Immunohistochemistry (Paraffin), Immunoprecipitation, Inhibition assay, and Western Blotting. |
| Key Applications |
|
| Application Notes | Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected lipoprotein lipase/LPL in human pancreatic cancer and normal bladder tissue sections. Western Blotting Analysis: A representative lot detected recombinant wild-type human LPL, as well as the S447X polymorphic form of LPL missing the last two amino acids at the C-terminal end (Turlo, K., et al. (2014). Biochim. Biophys. Acta. 1841(7):963-969). Western Blotting Analysis: Representative lots detected purified bovine, chicken, guinea pig, human, and rat LPL (Chang, S.F., et al. (1998). J. Lipid Res. 39(12):2350-2359; Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). Flow Cytometry Analysis: A representative lot detected surface LPL immunoreactivity among B-CLL patients peripheral blood CD19+ leukemic cells (Heintel, D., et al. (2005). Leukemia. 19(7):1216-1223). Immunocytometry Analysis: A representative lot detected more intense intracellular LPL immunoreactivity in B-CLL patients-derived CD19+ leukemic cells with unmutated Ig heavy chain variable region (IGVH) genes than those with mutated IGVH by fluorescent immunocytochemistry staining of 3.7% formaldehyde-fixed, 0.1% Triton X-100-permeabilized cells (Heintel, D., et al. (2005). Leukemia. 19(7):1216-1223). ELISA Analysis: A representative lot detected human LPL by ELISA. Human LPL peptide a.a. 384-395, but not a.a. 396-410, effectively blocked clone 5D2 immunoreactivity (Chang, S.F., et al. (1998). J. Lipid Res. 39(12):2350-2359). ELISA Analysis: A representative lot was used as both the capture and the detection antibody (HRP-conjugated) in sandwich ELISA. Treatment of purified human plasma LPL by heat (45°C for 60 min) or guanidine hydrochloride (60 min) decreased the ELISA immunoreactivity due to dimer dissociation (Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). Dot Blot Analysis: A representative lot detected human LPL by dot blot. Human LPL peptide a.a. 384-395, but not a.a. 396-410, effectively blocked clone 5D2 immunoreactivity (Chang, S.F., et al. (1998). J. Lipid Res. 39(12):2350-2359). Dot Blot Analysis: A representative lot detected baboon, bovine, mink, pig, sheep, LPL peptides representing region equivalent to human LPL a.a. 398-410, as well as cat, baboon, bovine, chicken, guinea pig, mink, pig, rat, sheep, LPL peptides representing region equivalent to human LPL a.a. 384-395. No reactivity toward murine peptides was observed (Chang, S.F., et al. (1998). J. Lipid Res. 39(12):2350-2359). Immunoprecipitation Analysis: A representative lot immunoprecipitated more LPL from post-heparin than pre-heparin human plasma. The highly homologous hepatic lipase (HL) was not immunoprecipitate by clone 5D2 (Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). Inhibits Activity/Function: A representative lot inhibited bovine milk LPL-mediated HCV binding to CHO cells in an HSPG-dependent, but LPL receptor-independent manner (Andréo, U., et al. (2007). Cell Microbiol. 9(10):2445-2456). Inhibits Activity/Function: A representative lot inhibited bovine milk LPL-mediated chylomicrons binding to CHO cells in an LPL receptor-independent manner (Kobayashi, J., et al. (2001). Ann. Clin. Biochem 38(Pt 2):124-128). Inhibits Activity/Function: A representative lot prevented human plasma LDL from binding immobilized bovine LPL dimer (Hussain, M.M., et al. (2000). J. Biol. Chem. 275(38):29324-29330). Inhibits Activity/Function: Clone 5D2 specifically inhibited the enzymatic activity of LPL, but not that of the homologous hepatic lipase (HL) (Babirak, S.B., et al. (1989). Atherosclerosis 9(3):326-334). Note: It is not recommended to probe LPL by Western blotting using whole plasma samples due to the large amount of albumin that co-migrates with LPL during electrophoresis. Affinity isolation of LPL from blood samples by immobilized heparin, clone 5D2, or other LPL antibodies is recommended prior to Western blotting analysis (Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). |
| Biological Information | |
|---|---|
| Immunogen | Purified bovine milk LPL. |
| Clone | 5D2 |
| Concentration | Please refer to lot specific datasheet. |
| Host | Mouse |
| Specificity | Clone 5D2 specifically reacts with LPL, but not the highly homologous hepatic lipase (HL) (Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). |
| Isotype | IgG1κ |
| Species Reactivity |
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| Species Reactivity Note | Baboon, Bovine, Chicken, Feline, Guinea pig, Human, Mink, Porcine, Rat, Sheep. Not Mouse. |
| Antibody Type | Monoclonal Antibody |
| Entrez Gene Number |
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| Gene Symbol |
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| Purification Method | Protein G purified. |
| UniProt Number |
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| Molecular Weight | 50.55/53.38 kDa (bovine mature/proLPL) and 50.39/53.16 kDa (human mature/proLPL) calculated. ~56 kDa observed (Chang, S.F., et al. (1998). J. Lipid Res. 39(12):2350-2359; Peterson, J., et al. (1992). J. Lipid Res. 33(8):1165-1170). |
| Product Usage Statements | |
|---|---|
| Quality Assurance | Evaluated by Immunohistochemistry in human placenta tissue. Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected lipoprotein lipase/LPL in human placenta tissue sections. |
| Usage Statement |
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| Storage and Shipping Information | |
|---|---|
| Storage Conditions | Stable for 1 year at 2-8°C from date of receipt. |
| Packaging Information | |
|---|---|
| Material Size | 100 μg |