[H06] HRP-conjugated Goat Anti-Human Apolipoprotein B-100, Academy Bio-medical Company, Inc.

[H06] HRP-conjugated Goat Anti-Human Apolipoprotein B-100


Academy Bio-Medical Company, Inc.

  • $252.00

Host Species: Goat
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: Human Apolipoprotein B100
Purification: Affinity purified
Form: Freeze dried powder
Buffer: 50 mM PBS, 0.1 M NaCl, and 0.01% Thiomersal, pH 7.4.
Specificity Specifically binds to human apo B-100. Dilution for immunoblot and ELISA range: 1,000 to 8,000.
Use: The antibody can be used for detection of apo B-100 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: 10 mg / ml Bovine Serum Albumin.


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.



ApoB exists in human plasma in two isoforms, ApoB-48 (Chen et al., 1987) and Apo B-100 (Wei et al., 1985, Yang et al., 1986a; 1989a,b; 1990; Chen et al., 1986; Yang et al., 1990, Yang and Pownall, 1992). Apo B-100 is the major physiological ligand for the LDL receptor. Apo B-100 is a large monomeric protein, containing 4536 amino acids (m.w. 515 kDa, Yang et al., 1986b).

Apo B-100 is synthesized in the liver and is required for the assembly of VLDL. It is found in LDL and VLDL after the removal of the Apo A, E and C. Apo B-48 is present in chylomicrons and their remnants. It is essential for the intestinal absorption of dietary lipids. Apo B levels correlate with the risk of coronary disease.

The Apo B protein is directly involved in the retention of LDL with the arterial wall (Olofsson and Boren, 2012). Apo B-48 is synthesized in the small intestine. It comprises approximately half of the N-terminal region of ApoB-100 and is the result of posttranscriptional mRNA editing by a stop codon in the intestine not found in the liver.

Chen, S., G. Habib, C. Yang, Z. Gu, B. Lee, S. Weng, S. Cai, J. Deslypere, M. Rosseneu, and Al. Et. "Apolipoprotein B-48 Is the Product of a Messenger RNA with an Organ-specific In-frame Stop Codon." Science 238 (1987): 363- 66.

Olofsson, S.-O., and J. Boren. "Apolipoprotein B Secretory Regulation by Degradation." Arteriosclerosis, Thrombosis, and Vascular Biology 32 (2012): 1334-338.

Wei, C. F., S. H. Chen, C. Y. Yang, Y. L. Marcel, R. W. Milne, W. H. Li, J. T. Sparrow, A. M. Gotto, and L. Chan. "Molecular Cloning and Expression of Partial cDNAs and Deduced Amino Acid Sequence of a Carboxyl-terminal Fragment of Human Apolipoprotein B-100." Proceedings of the National Academy of Sciences 82 (1985): 7265- 269.

Yang, Chao-Yuh, and Pownall, H.J. "In Structure and Function of Plasma Apolipoproteins." Structure and Function of Apolipoproteins. Boca Raton, Fla.: CRC, 1992.

Yang, Chao-Yuh, T. W. Kim, S. A. Weng, B. R. Lee, M. L. Yang, and A. M. Gotto. "Isolation and Characterization of Sulfhydryl and Disulfide Peptides of Human Apolipoprotein B-100." Proceedings of the National Academy of Sciences 87 (1990): 5523-527.

Yang, Chao-Yuh, Z. W. Gu, S. A. Weng, T. W. Kim, S. H. Chen, H. J. Pownall, P. M. Sharp, S. W. Liu, W. H. Li, and A. M. Gotto. "Structure of Apolipoprotein B-100 of Human Low Density Lipoproteins." Arteriosclerosis, Thrombosis, and Vascular Biology 9 (1989a): 96-108.

Yang, Chao-Yuh, Zi-Wei Gu, Lawrence Chan, Henry J. Pownall, and Antonio M. Gotto. "Structure and Functional Domains of Human Apolipoprotein B-100: A Strategy to Elucidate the Structure Information of a Large Protein." Methods in Protein Sequence Analysis (1989b): 466-74.

Yang, Chao-Yuh, San-Hwan Chen, Sandra H. Gianturco, William A. Bradley, James T. Sparrow, Masako Tanimura, Wen-Hsiung Li, Doris A. Sparrow, Hans Deloof, Maryvonne Rosseneu, Fu-Shin Lee, Zi-Wei Gu, Antonio M. Gotto, and Lawrence Chan. "Sequence, Structure, Receptor-binding Domains and Internal Repeats of Human Apolipoprotein B-100." Nature 323 (1986a): 738-42.



[H06] 2013 Virella, Gabriel; Colglazier, Joan; Chassereau, Charlyne; Hunt, Kelly J.; Baker, Nathaniel L.; Lopes-Virella, Maria F. (2013): Immunoassay of modified forms of human low density lipoprotein in isolated circulating immune complexes. In Journal of immunoassay & immunochemistry 34 (1), pp. 61–74. DOI: 10.1080/15321819.2012.683500.
[H06] 2009 Gillard, Baiba K.; Lin, Hu-Yu Alice; Massey, John B.; Pownall, Henry J. (2009): Apolipoproteins A-I, A-II and E are independently distributed among intracellular and newly secreted HDL of human hepatoma cells. In Biochimica et biophysica acta 1791 (12), pp. 1125–1132. DOI: 10.1016/j.bbalip.2009.07.004.
[H06] 2006 Judge, Adam D.; Bola, Gurneet; Lee, Amy C. H.; MacLachlan, Ian (2006): Design of noninflammatory synthetic siRNA mediating potent gene silencing in vivo. In Molecular therapy : the journal of the American Society of Gene Therapy 13 (3), pp. 494–505. DOI: 10.1016/j.ymthe.2005.11.002.
[H06] 2004 Soutschek, Jürgen; Akinc, Akin; Bramlage, Birgit; Charisse, Klaus; Constien, Rainer; Donoghue, Mary et al. (2004): Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs. In Nature 432 (7014), pp. 173–178. DOI: 10.1038/nature03121.

We Also Recommend