[F07] FITC-conjugated Goat Anti-Human Apolipoprotein CI, Academy Bio-medical Company, Inc.

[F07] FITC-conjugated Goat Anti-Human Apolipoprotein CI

31F-G1a

Academy Bio-Medical Company, Inc.

  • $309.00


Host Species: Goat
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: Human Apolipoprotein CI
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 CI. Molar F/P ratio is 3.0. The investigator should determine working dilutions.

Use: The antibody can be used for detection of apo CI 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

ApoCI contains 57 amino acid residues and the m.w. is 6.6 kDa (Jackson et al., 1974).

ApoCI has been found to activate LCAT (Liu and Subbaiah 1993). Apo CI is an inhibitor of lipoprotein binding to the LDL receptor, LDL receptor-related protein, and VLDL receptor. Apo CI is also an inhibitor of the plasma cholesteryl ester transfer protein and of fatty acid uptake into tissues (Shachter, 2001). This inhibition role can potentially regulate several lipase enzymes (Poensgen, 1990, Conde-Knape et al., 2002; Berbee et al., 2005.)

Berbee J.F., C.C. van der Hoogt, D. Sundararaman, L.M. Havekes, and P.C. Rensen. “Severe hypertriglyceridemia in human APOC1 transgenic mice is caused by apoC-I-induced inhibition of LPL.” J. Lipid. Res. 46 (2005) 297-306.

Conde-Knape K., A. Bensadoun, J.H. Sobel. J.S. Cohn, and N.S. Shachter. “Overexpression of apoC-I in apoE-null mice: severe hypertriglyceridemia due to inhibition of hepatic lipase” J. Lipid Res. 43 (2002): 2136-2145.

Jackson R.L., J. T. Sparrow, H. N. Baker, J.D. Morrisett, O. D. Taunton, and A. M. Jr. Gotto. “The primary structure of apolipoprotein-serine.” J. Biol. Chem. 249.16 (1974): 5308-13.

Liu, M. and P.V. Subbaiah. “Activation of plasma lysolecithin acyltransferase reaction by apolipoproteins A-I, C-I and E.” Biochim. Biophys. Acta. 1168 (1993): 144-152.

Poensgen, J., “Apolipoprotein C-1 inhibits the hydrolysis by phospholipase A2 of phospholipids in liposomes and cell membranes” Biochim. Biophys. Acta. 1042 (1990): 188-192.

Shachter, Neil S., “Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism” Current Opinion in Lipidology 12(3): 297-304.

 


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