Application

Anti-Lipoprotein Lipase/LPL Antibody, clone 4-1a is an antibody against Lipoprotein Lipase/LPL for use in Immunohistochemistry (Paraffin), Western Blotting, ELISA, Immunocytochemistry, Immunofluorescence.

Research CategorySignaling

Research Sub CategoryLipid Metabolism & Weight Regulation

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected lipoprotein lipase/LPL immunoreactivity in human pancreas, human skeletal muscle, and rat heart tissue sections.
Western Blotting Analysis: A representative lot detected human plasma lipoprotein lipase (LPL) and bovine milk LPL by Western blotting. Clone 4-1a exhibited much reduced binding to murine or chicken LPL, and failed to detect human hepatic lipase (hHL) (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).
Western Blotting Analysis: A representative lot detected recombinant wild-type human LPL (rhLPL), as well as rhLPL with mutated Gln3 & Arg4. Clone 4-1a failed to react with rhLPL with mutated Ile8 or Asp9, nor rhLPL with either a.a. 5-15 or aa.16-25 deletion (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).
ELISA Analysis: A representative lot was employed as the capture antibody for the detection of human LPL by sandwich ELISA, using biotinylated clone 5D2 as the detcting antibody (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).
Immunocytochemistry Analysis: A representative lot detected the binding of human LPL to CHO and CHL cells transfected to express surface GPIHBP1, but not to mock transfected cells or cells transfected to express GPIHBP1 C65S mutant. Clone 4-1a does not compete against triglyceride-rich lipoproteins (TRLs) for binding the LPL-GPIHBP1 complex on cell surface (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).
Immunofluorescence Analysis: A representative lot detected hLPL immunoreactivity associated with GPIHBP1 on capillary endothelial cells in OCT-embedded, methanol/acetone-fixed frozen skeletal muscle sections from mice expressing muscle-specific human LPL transgene. Much lower immunoreactivity of the endogenous mLPL was detected in skeletal muscle sections from non-transgenic mice (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).
Note: Clone 4-1a exhibits much weaker affinity toward rat & murine LPL when compared with human LPL. Higher amount of sample loading (in Western blotting and ELISA) and/or high sensitivity detection method (e.g. HRP polymer or fluorescence detection in Western blotting and immunohistochemistry) is recommended when using this clone for detecting rat & murine LPL.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Lipoprotein lipase (EC 3.1.1.34; UniProt P06858; also known as hLPL, LPL) is encoded by the LPL (also known as LIPD) gene (Gene ID 4023) in human. 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. 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).

Immunogen

Purified human plasma lipoprotein lipase/LPL.

Epitope: Near the N-terminus of mature LPL.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein G Purified

Purified mouse monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Format: Purified

Quality

Evaluated by Immunohistochemistry in mouse heart tissue.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected lipoprotein lipase/LPL immunoreactivity in mouse heart tissue sections.

Specificity

Clone 4-1a binds human and bovine LPL, as well as GPIHBP1-bound LPL, but not human hepatic lipase. Clone 4-1a does not inhibit LPL catalytic activity or LPL heparin interaction, nor does clone 4-1a compete against triglyceride-rich lipoproteins (LRLs) for bining GPIHBP1-LPL complex (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

53.16 kDa (ProLPL) and 50.39 (Mature LPL) calculated. ~56 kDa observed (Bensadoun, A., et al. (2014). Biochim. Biophys. Acta. 1841(7):970-976).