LPL Human
Lipoprotein Lipase Human Recombinant
Cat. No.
BT5501
Source
Escherichia Coli.
Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Appearance
Purity
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.
Product Specs
Introduction
Lipoprotein lipase (LPL) is an enzyme responsible for breaking down triglycerides in the bloodstream. It is primarily found in tissues like the heart, muscles, and adipose tissue. LPL functions as a dimer, playing a crucial role in both triglyceride hydrolysis and facilitating receptor-mediated lipoprotein uptake. Genetic mutations affecting LPL can lead to various lipid metabolism disorders. Severe mutations can cause LPL deficiency, resulting in Type I hyperlipoproteinemia. Additionally, LPL contributes to atherosclerosis development by promoting monocyte adhesion to endothelial cells, stimulating TNF secretion, and inducing vascular smooth muscle cell proliferation.
Description
This recombinant human LPL protein, expressed in E. coli, has a molecular weight of 51.61 kDa. It consists of 458 amino acids corresponding to the human LPL sequence, with a 10-amino acid His tag attached to the N-terminus.
Formulation
The LPL protein was filtered through a 0.4 μm filter and subsequently lyophilized at a concentration of 0.5 mg/ml in 50 mM acetate buffer with a pH of 4.
Solubility
To create a working stock solution of around 0.5 mg/ml, add 0.1 M acetate buffer (pH 4) to the lyophilized pellet and allow it to dissolve completely. For use at a higher pH, dilute the solution with the appropriate buffer to a concentration of 10 μg/ml. The solubility of this antigen is limited at higher concentrations. Note that this product is not sterile. Prior to cell culture use, filter it through a sterile filter of appropriate pore size.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize repeated freeze-thaw cycles. Reconstituted protein remains stable at 4°C for a limited period and shows no significant changes for up to two weeks when stored at 4°C.
Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHAS ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA QEHYPVSAGY TKLVGQDVAR FINWMEEEFN YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCSSKEAF EKGLCLSCRK NRCNNLGYEI SKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESETH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW SDWWSSPGFA IQKIRVKAGE TQKKVIFCSR EKVSHLQKGK APAVFVKCHD KSLNKKSG.
Product Science Overview
Structure and Function
Recombinant Human Lipoprotein Lipase
Applications
Recombinant LPL is used in various research applications, including:
- Biochemical Studies: To understand the enzyme’s kinetics and mechanism of action.
- Drug Development: As a target for developing therapies for lipid disorders.
- Diagnostic Tools: In assays to measure lipase activity in biological samples.
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