Overview

Description

  • NatureRecombinant
  • SourceHEK 293 cells
  • Amino Acid Sequence
    • AccessionP04180
    • SpeciesHuman
    • SequenceHVDYKDDDDKPAGFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLE AKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNR SS GLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGY VRDE TVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHS LGCLHL LYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQ GIPIMSSI KLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRD FQRFFADLHF EEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTY IYDHGFPYTDPV GVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLH GIQHLNMVFSNLTL EHINAILLGAYRQGPPASPTASPEPPPPE
    • Molecular weight49 kDa including tags
    • Amino acids25 to 440
    • TagsDDDDK tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab104359 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • FormLyophilised
  • Additional notesPlease filter the product by an appropriate sterile filter before using it in the cell culture.
    Store lyophilized protein at –20°C. Lyophilized protein remains stable until the expiry date when stored at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -80°C.

    Preservative: None
    Constituents: 50mM Sodium chloride, 20mM Tris, pH 7.5

  • ReconstitutionAdd deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile!

General Info

  • Alternative names
    • LCAT
    • LCAT_HUMAN
    • Lecithin cholesterol acyltransferase
    • Lecithin-cholesterol acyltransferase
    • Phosphatidylcholine sterol acyltransferase
    • Phosphatidylcholine-sterol acyltransferase
    • Phospholipid cholesterol acyltransferase
    • Phospholipid-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.
  • Information by UniProt

Recombinant Human LCAT protein images

  • 14% SDS-PAGE showing ab104359 at approximately 48.5kDa:
    Lane 1: M.W. marker – 14, 21, 31, 45, 66, 97 kDa
    Lane 2: reduced and boiled sample, 5µg/lane.
    Lane 3: non-reduced and non-boiled sample, 5µg/lane.

References for Recombinant Human LCAT protein (ab104359)

ab104359 has not yet been referenced specifically in any publications.

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