[F09] FITC-conjugated Goat Anti-Human Apolipoprotein CIII, Academy Bio-medical Company, Inc.

[F09] FITC-conjugated Goat Anti-Human Apolipoprotein CIII

33F-G2a

Academy Bio-Medical Company, Inc.

  • $309.00


Host Species: Goat
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: Human Apolipoprotein CIII
Purification: Affinity purified
Buffer: 75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity

Specifically binds to human apo CIII. Molar F/P ratio is 3.6. The investigator should determine working dilutions.

Use: The antibody can be used for detection of apo CIII in plasma and lipoproteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.
Storage: -20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.
Form: Freeze dried powder
Stabilizer: 5 mg / ml Bovine Serum Albumin.

Reconstitution

and Storage:

Freeze-dried product should be stored refrigerated until opened. After opening, restore to suggested ml volume with distilled water. If it is not completely clear after standing for 1-2 hours at room temperature, centrifuge the product. It is stable for several weeks at 4°C as an undiluted liquid. Do not use for more than one day after dilution. For extended storage after reconstitution, we suggest aliquot to avoid repeated freezing and thawing; or the addition of an equal volume of glycerol to make a final glycerol concentration of 50%, followed by storage at -20°C. The concentration of protein and buffer salts will decrease to one-half of the original after the addition of glycerol.

 

*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.

 

Importance

Apo CIII contains 79 amino acid residues. The m.w. is 8.7 kDa (Brewer et al., 1974).

It may inhibit the activation of lipoprotein lipase by apo CIII. Apo CIII is a constituent of both apoB- and apoAI-containing lipoproteins in the circulation. Apo CIII plays a pivotal role in regulating the plasma metabolism of VLDL, IDL, and LDL, primarily by inhibiting receptor-mediated uptake of these lipoproteins by the liver (Sehayek and Eisenberg 1991, Aalto-Setala et al., 1992, Zheng et al., 2007)

Brewer, H. B., R. Shulman, P. Herbert, R. Ronan, and K. Wehrly. “The complete amino acid sequence of alanine apolipoprotein (apoC-3), and apolipoprotein from human plasma very low density lipoproteins.” J Biol Chem 249.15 (1974):4975-84.

Sehayek , E. , and S. Eisenberg . “Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-dependent cellular metabolism of human triglyceride-rich lipoproteins through the low density lipoprotein receptor pathway.” J. Biol. Chem. 266 (1991) : 18259 – 18267 .

Aalto-Setala , K., E. A. Fisher , X. Chen , T. Chajek-Shaul , T. Hayek , R. Zechner , A. Walsh , R. Ramakrishnan , H. N. Ginsberg , and J. L. Breslow . “ Mechanism of hypertriglyceridemia in human apolipoprotein (apo) CIII transgenic mice. Diminished very low density lipoprotein fractional catabolic rate associated with increased apo CIII and reduced apo E on the particles.” J. Clin. Invest. 90 (1992): 1889 – 1900.

Zheng , C. , C. Khoo , K. Ikewaki , and F. M. Sacks . “ Rapid turnover of apolipoprotein C-III-containing triglyceride-rich lipoproteins contributing to the formation of LDL subfractions.” J. Lipid Res. 48 (2007): 1190 -203.

 


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