Render Target: STATIC
Render Timestamp: 2024-11-21T13:40:24.376Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:28:21.971
Product last modified at: 2024-11-12T12:45:15.374Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

ApoE Antibody #68587

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY M R
    SENSITIVITY Endogenous
    MW (kDa) 35
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    ApoE Antibody recognizes endogenous levels of total ApoE protein.

    Species Reactivity:

    Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp26 of mouse ApoE protein. Antibodies are purified by peptide affinity chromatography.

    Background

    Apolipoproteins are plasma lipoproteins that function as transporters of lipids and cholesterol in the circulatory system. Chylomicrons are a fundamental class of apolipoproteins containing very low-density lipoproteins (VLDL), intermediate-density lipoproteins (IDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) (1,2).
    Human ApoE has three isoforms: ApoE2, ApoE3, and ApoE4. These three isoforms differ in the combination of cysteine and arginine residues located at positions 130 and 176. The ApoE4 isoform contains arginine at both locations (3). Arginine 130 in ApoE4 allows for interaction between carboxy- and amino-terminal domains through orientation of arginine 61, leading to a preference for binding lower density lipoproteins, where ApoE2 and ApoE3 show preference for binding HDL. Mouse ApoE contains similar sequence to human ApoE4, with arginine present at equivalent positions to 130 and 176. However, the mouse sequence lacks arginine at critical position 61, which allows it to behave similarly to human ApoE3, including preferential binding to HDL (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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