All of the antibodies listed have been evaluated with clinical samples.

Rabbit monoclonal antibody clones for procalcitonin (PCT)

Procalcitonin (PCT) is a peptide precursor of the hormone calcitonin, the latter being involved with calcium homeostasis. The level of procalcitonin in the blood stream of healthy individuals is below the limit of detection (0.01 µg/L) of clinical assays1, but rises to as high as 100 µg/L in a response to a proinflammatory stimulus, especially of bacterial origin.

The procalcitonin test has been approved by the U.S. Food and Drug Administration (FDA) in 2005 for use in conjunction with other laboratory findings and clinical assessments to assist in the risk assessment of critically ill people for progression to severe sepsis and septic shock, and the use of procalcitonin test has been steadily increasing in recent years.

Procalcitonin levels may be useful to distinguish bacterial infections from nonbacterial infections. Trials from 2008 and 2009 have shown that they may help guide therapy and reduce antibiotic use, which can help save on cost of antibiotic prescriptions and drug resistance2, 3

AvantGen has generated a compatible pair of high affinity rabbit monoclonal antibodies against human PCT. These clones are suitable for high sensitivity PCT assay development.

Catalog No Antigen Clone Application Data Sheet
DA-2001 PCT G11 WB, ELISA Download PDF Request Quote
DA-2002 PCT G12 WB, ELISA Download PDF Request Quote

1. Dandona, P, et al., Procalcitonin increase after endotoxin injection in normal subjects. J. Clin. Endocrinol. Metab. 1994; 79, (6): 1605–8.
2. Schuetz, P., et al.,  Effect of procalcitonin-based guidelines vs standard guidelines on antibiotic use in lower respiratory tract infections: the ProHOSP randomized controlled trial. JAMA. 2009;302(10):1059-66.
3.  Briel M, et al.,  Procalcitonin-guided antibiotic use vs a standard approach for acute respiratory tract infections in primary care. Arch Intern Med. 2008;168(18):2000-7; discussion 2007-8.

Rabbit monoclonal antibodies for NT-proBNP

Brain-type naturiuretic peptide (BNP) is a polypeptide synthesized as pre-proBNP which is cleaved to proBNP(aa1-108), then cleaved by furin to subsequently be secreted as the biologically active BNP(aa77-108) and the inactive N-terminal BNP(aa1-76, NT-proBNP).

Both BNP and NT-proBNP levels in the blood are used for screening and diagnosis of acute congestive heart failure (CHF) and may be useful to establish prognosis in heart failure, as both fragmentsare typically higher in patients with poor prognosis.While the plasma concentrations of both BNP and NT-proBNP are also typically increased in patients with asymptomatic or symptomatic left ventricular dysfunction, the BNP peptide hormone has a short half life and the NT-proBNP fragment serves as a better biomarker1,2. Elevated NT-proBNP levels are associated with left ventricular dysfunction, heart failure and myocardial ischemia2-4.

AvantGen has generated a compatible pair of rabbit monoclonal antibodies against the NT-proBNP with higher affinities than other commercially available antibody clones, with a corresponding increase in assay sensitivity. These clones are suitable for high sensitivity NT-proBNP assay development.

Catalog No Antigen Clone Application Data Sheet
DA-2003 NT-proBNP S3A10 WB, ELISA Download PDF Request Quote
DA-2004 NT-proBNP S3H8 WB, ELISA Download PDF Request Quote

1. Yeo, KT et al., Multicenter evaluation of the Roche NT-proBNP assay and comparison to the Biosite Triage BNP assay. ClinChimActa.2003; 338(1-2):107-15.
2. Hall, C., NT-ProBNP: the mechanism behind the marker.J Card Fail, 2005; 11(5 Suppl): p. S81-3.
3. deLemos, JA., et al. The prognostic value of B-type natriuretic peptide in patients with acute coronary syndromes.N Engl J Med. 2001;345:1014 –1021.
4. Costello-Boerrigter, LC.,et al.,Amino-terminal pro-B-type natriuretic peptide and B-type natriuretic peptide in the general community: determinants and detection of left ventricular dysfunction. J AmColl Cardiol, 2006; 47(2): p. 345-53.
5. Wang, TJ.,et al., Multiple biomarkers for the prediction of first major cardiovascular events and death. N Engl J Med. 2006; 355(25):2631-9.

Rabbit monoclonal antibodies for Strep-A

Group A Streptococcus is a bacterium that can cause a wide range of infections. People may also carry group A streptococci (GAS) in the throat or on the skin and have no symptoms of illness. Most GAS infections are relatively mild illnesses such as “strep throat,” or impetigo (a skin infection). However, these bacteria can also cause severe and even life-threatening diseases.

AvantGen has developed rabbit monoclonal antibodies that recognizes all Strep A strains with high affinity tested to date (ATCC:10782, 11434 12344, 12386, 14289 and 49399; CDC: 410, 482, 496, 633, 634, 635, 721, 754, and 799) and do not recognize Strep B, C, F or G. These antibodies are therefore suitable for diagnostic kit development. These antibodies have been shown to outperform rabbit polyclonal antibodies in the similar assays.

Catalog No Antigen Clone Application Data Sheet
DA-2005 Strep A S3H2 Lateral flow, ELISA Download PDF Request Quote
DA-2006 Strep A S3C79 Lateral flow, ELISA Download PDF Request Quote

Rabbit and human monoclonal antibody clones for GPBB

Glycogen phosphorylase BB (GPBB) is another potential candidate for clinical diagnosis of myocardial ischemia within the first 1-3 hours after chest-pain onset. GP is bound to glycogen in the sarcoplasmic reticulum and catalyzes the first step of glycogenolysis after activation, which involves the separation of glucose-1-phosphate from glycogen. Three GP isoenzymes are present in human tissue and are named according to the tissue of their initial description: GPLL (liver), GPMM (muscle) and GPBB (brain). In addition to its occurrence in brain, GPBB is also found in high concentrations in heart muscle. During myocardial ischemia, activation of GPBB results in an increase in glycogen degradation. Thus, GPBB is released from glycogen and then enters the bloodstream. Initial research has shown higher sensitivity of GPBB within the first 4 h following chest-pain onset in comparison to other cardiac markers. In addition, GPBB seems to indicate necrotic cell damage and, in particular, ischemic processes, e.g., as observed with unstable angina pectoris (UAP). Therefore, GPBB may serve as another candidate marker to provide earlier diagnosis in AMI1-4.

AvantGen’s anti-GPBB antibody clones are highly specific and show no cross-reactivity to GPLL and GPMM and are suitable for sensitive GPBB assay development.

Catalog No Antigen Clone Application Data Sheet
DA-2007 GPBB E9B10 ELISA Download PDF Request Quote
DA-2008 GPBB F5B11 ELISA Download PDF Request Quote

1. Peetz, D., et al.,Glycogen phosphorylase BB in acute coronary syndromes.ClinChem Lab Med, 2005; 43(12): p. 1351-8.
2. Entman, ML., et al.,Association of glycogenolysis with cardiac sarcoplasmic reticulum: II. Effect of glycogen depletion, deoxycholatesolubilization and cardiac ischemia: evidence for a phorphorylasekinase membrane complex.J Mol Cell Cardiol, 1977; 9(7): p. 515-28.
3. Krause, EG.,et al.,Glycogen phosphorylaseisoenzyme BB in diagnosis of myocardial ischaemic injury and infarction.Mol Cell Biochem, 1996; 160-161: p. 289-95.
4. Bozkurt S., et al., The diagnostic and prognostic value of first hour glycogen phosphorylaseisoenzyme BB level in acute coronary syndrome. Cardiol J. 2011;18(5):496-502.

Human monoclonal antibodies for PAPP-A

Pregnancy-associated plasma protein A (PAPP-A) is a 200 kDa metalloproteinase specific for insulin-like growth factor 4 (IGF-4) that forms a homodomer of 400 kDa in active form.  In the serum of pregnant women it exists as a heterotetramer with pro-eosinophil basic protein (proEBP; 2:2 ratio of PAPP-A to proEBP) with the proEBP maintaining the metalloproteinase in an inactive form1-2.  More recently, PAPP-A has been shown to be a promising marker for unstable atherosclerotic plaques with potential as a prognostic indicator for elevated risk in patients with cardiovascular disease3-5. With the recent development of highly specific antibodies for the dimeric form of PAPP-A, it has been demonstrated that it is the dimeric form of PAPP-A that becomes elevated in the serum of patients with cardiovascular disease, not the form complexed with proEBP6,7.

AvantGenhas developed compatible high affinity human monoclonal antibodies that specifically identify the PAPP-A subunit relevant to cardiovascular disease for diagnostic purposes and show no cross-reactivity to either proEBP or related metalloproteinases such as PAPP-A2 or MMP-9.

Catalog No Antigen Clone Application Data Sheet
DA-2009 PAPP-A A1 ELISA Download PDF Request Quote
DA-2010 PAPP-A C1 ELISA Download PDF Request Quote

1. Lawrence, JB.,et al., The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A. Proc. Natl. Acad. Sci U. S. A. 1999; 96, 3149–3153.
2.  Oxvig, C., et al., Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein. J. Biol. Chem. 1993; 268,12243–12246.
3. Bayes-Genis A., et al., Pregnancy-associated plasma protein A as a marker of acute coronary syndromes. N Engl J Med. 2001; 345(14):1022-9.
4. Iversen, KK., et al., CLARICOR Trial Group.Pregnancy associated plasma protein-A as a marker for myocardial  infarction and death in patients with stable coronary artery disease: a prognostic study within the CLARICOR Trial. Atherosclerosis. 2011;214(1):203-8.
5. Qin QP.,et al., Molecular distinction of circulating pregnancy-associated plasma protein A in myocardial infarction and pregnancy. Clin Chem. 2005; 51(1):75-83.
6. Kavsak, PA, et al., PAPP-A as a marker of increased long-term risk in patients with chest pain. ClinBiochem. 2009; 42(10-11):1012-8.
7. Lund, J., et al., Free vs total pregnancy-associated plasma protein A (PAPP-A) as a predictor of 1-year outcome in patients presenting with non-ST-elevation acute coronary syndrome. Clin Chem. 2010; 56(7):1158-65.

Fatty acid binding proteins (FABPs)

Fatty acid binding proteins (FABPs) are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-type. They form 14-15 kDa proteins and are thought to participate in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. They may also be responsible in the modulation of cell growth and proliferation.

Human heart-type fatty acid binding protein (H-FABP) also known as mammary-derived growth inhibitor is a cytoplasmic protein encoded by the human FABP3 gene.1-2

H-FABP is released from cardiac myocytes following an ischemic episode and is a sensitive biomarker for myocardial infarction (MI). 3-5  H-FABP can be detected in the blood within one to three hours of MI. H-FABP is 20 times more specific to cardiac muscle than myoglobin,6 it is found at 10-fold lower levels in skeletal muscle than heart muscle and the amounts in the kidney, liver and small intestine are even lower again.7-8

Studies showed that measuring H-FABP in combination with troponin increased the diagnostic accuracy and with a negative predictive value of 98% could be used to identify those not suffering from MI at the early time point of 3–6 hours post chest pain onset. The effectiveness of using the combination of H-FABP with troponin to diagnose MI within 6 hours is well reported.9-11

Catalog No Antigen Clone Application Data Sheet
DA-2011 FABP A10 ELISA Download PDF Request Quote
DA-2012 FABP E10 ELISA Download PDF Request Quote

1. Phelan CM, Larsson C, Baird S, Futreal PA, Ruttledge MH, Morgan K, Tonin P, Hung H, Korneluk RG, Pollak MN, Narod SA (May 1996). “The human mammary-derived growth inhibitor (MDGI) gene: genomic structure and mutation analysis in human breast tumors”. Genomics 34 (1): 63–8.

2  “Entrez Gene: FABP3 fatty acid binding protein 3, muscle and heart (mammary-derived growth inhibitor)”.

3. Kleine AH, Glatz JF, Van Nieuwenhoven FA, Van der Vusse GJ (Oct 1992). “Release of heart fatty acid-binding protein into plasma after acute myocardial infarction in man”. Molecular and Cellular Biochemistry 116 (1-2): 155–62.

4  Tanaka T, Hirota Y, Sohmiya K, Nishimura S, Kawamura K (Apr 1991). “Serum and urinary human heart fatty acid-binding protein in acute myocardial infarction”. Clinical Biochemistry 24 (2): 195–201.

5.  Watanabe K, Wakabayashi H, Veerkamp JH, Ono T, Suzuki T (May 1993). “Immunohistochemical distribution of heart-type fatty acid-binding protein immunoreactivity in normal human tissues and in acute myocardial infarct”. The Journal of Pathology 170 (1): 59–65

6. Glatz JF, van Bilsen M, Paulussen RJ, Veerkamp JH, van der Vusse GJ, Reneman RS (Jul 1988). “Release of fatty acid-binding protein from isolated rat heart subjected to ischemia and reperfusion or to the calcium paradox”. Biochimica Et Biophysica Acta 961 (1): 148–52.

7 Ghani F, Wu AH, Graff L, Petry C, Armstrong G, Prigent F, Brown M (May 2000). “Role of heart-type fatty acid-binding protein in early detection of acute myocardial infarction”. Clinical Chemistry 46 (5): 718–9. PMID 10794758.

8.  Pelsers MM, Hermens WT, Glatz JF (Feb 2005). “Fatty acid-binding proteins as plasma markers of tissue injury”. Clinica Chimica Acta; International Journal of Clinical Chemistry 352 (1-2): 15–35

9. Azzazy HM, Pelsers MM, Christenson RH (Jan 2006). “Unbound free fatty acids and heart-type fatty acid-binding protein: diagnostic assays and clinical applications”. Clinical Chemistry 52 (1): 19–29.

10. McCann CJ, Glover BM, Menown IB, Moore MJ, McEneny J, Owens CG, Smith B, Sharpe PC, Young IS, Adgey JA (Dec 2008). “Novel biomarkers in early diagnosis of acute myocardial infarction compared with cardiac troponin T”. European Heart Journal 29 (23): 2843–50.

11. Li CJ, Li JQ, Liang XF, Li XX, Cui JG, Yang ZJ, Guo Q, Cao KJ, Huang J (Mar 2010). “Point-of-care test of heart-type fatty acid-binding protein for the diagnosis of early acute myocardial infarction”. Acta Pharmacologica Sinica 31 (3): 307–12.