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Overview

  • Product nameLCAT protein (Tagged-His Tag)See all LCAT proteins and peptides ...
  • Protein descriptionRecombinant fragment, corresponding to amino acids 49-440 (392 aa) of Human LCAT with a N terminal His tag; predicted MWt 45kDa: Uniprot ID = P04180.
  • Expression hostE. coli
  • Properties

  • Purification notesPurity level >85%
    This protein was expressed as an N-terminal His-tag fusion protein using Escherichia coli, and purified using Immobilized Metal Ion Affinity Chromatography. In some cases, smaller protein fragments may be present in addition to the intended expression product as a result of premature termination during translation in E. coli and subsequent co-purification via the His-tag. In some cases purified proteins run at a molecular weight different to the theoretically calculated molecular weight. This may be as a result of unequally distributed charges in the amino acid sequence. Alternatively, dimerisation of the expression product can occur under oxygen limitation during expression/cultivation.
  • FormLyophilised:Reconstitution with 133 µl aqua dest.
  • Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
  • Storage bufferPreservative: None
    Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5
  • Concentration information loading...
  • Additional notesProtein Identity confirmed by Mass Spectrometry (MS/MS) (acquired on initial reference batch)
  • Sequence notesVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDL NMFLPLGVDCWIDN TRVVYNRSSGLVSNAPGVQIRVPG FGKTYSVEYLDSSKLAGYLHTLVQNLVNNG YVRDETVR AAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGH SLGCLH LLYFLLRQPQAWKDRFIDGFISLGAPWGGSIK PMLVLASGDNQGIPIMSSIKLK EEQRITTTSPWMFPSR MAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMW LQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYT DPVGVLYEDGDDTV ATRSTELCGLWQGRQPQPVHLLPL HGIQHLNMVFSNLTLEHINAILLGAYRQGP PASPTASP EPPPPE
  • Research Areas
  • Applications

    Our Abpromise guarantee covers the use of ab91931 in the following tested applications.

    The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

    Application Notes
    SDS-PAGE
    MS
  • Application notesMS: Use at an assay dependent dilution.
    SDS-PAGE: Use at an assay dependent dilution.


    Not yet tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.
  • Protein info

    • Alternative names
        LCATLCAT_HUMANLecithin cholesterol acyltransferase
        Lecithin-cholesterol acyltransferasePhosphatidylcholine sterol acyltransferasePhosphatidylcholine-sterol acyltransferasePhospholipid cholesterol acyltransferasePhospholipid-cholesterol acyltransferase
      see all
  • FunctionCentral enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms.
  • Tissue specificityExpressed mainly in brain, liver and testes. Secreted into plasma and cerebral spinal fluid. In liver, expressed in HEPG2 hepatocytes.
  • Involvement in diseaseDefects in LCAT are the cause of lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]; also called Norum disease. LCATD is a disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: familial LCAT deficiency and fish-eye disease. Familial LCAT deficiency is associated with a complete absence of alpha and beta LCAT activities and results in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure.
    Defects in LCAT are a cause of fish-eye disease (FED) [MIM:136120]; also known as dyslipoproteinemic corneal dystrophy or alpha-LCAT deficiency. FED is due to a partial LCAT deficiency that affects only alpha-LCAT activity. It is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye').
  • Sequence similaritiesBelongs to the AB hydrolase superfamily. Lipase family.
  • Post-translational
    modifications
    O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures. N-glycosylated sites contain sialylated triantennary and/or biantennary complex structures.
  • Cellular localizationSecreted. Secreted into blood plasma. Produced in astrocytes and secreted into cerebral spinal fluid.
  • Target information above from: UniProt accession P04180 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    LCAT protein (Tagged-His Tag) images

    • The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images colored control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.

    References for LCAT protein (Tagged-His Tag) (ab91931)

    ab91931 has not yet been referenced specifically in any publications.

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