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).
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).
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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