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Cerebral array ii

Product Method Size Catalog Price Quantity
Cerebral array ii B A T (evidence investigatorâ„¢) 54 biochips EV3637 $8545.76
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INTENDED USE

The Evidence Investigator Cerebral Array II is to be used for the in-vitro simultaneous quantitative detection of multiple related cerebral immunoassays (in parallel) from a single patient sample.

The Evidence Investigator Cerebral Array II is for research use only and not for diagnostic procedures.

CLINICAL SIGNIFICANCE

In developed countries cerebrovascular disease, is one of the major public health problems, with stroke being the third leading cause of death in the United States and the leading cause of major adult disability. Determination of the type of stroke is very important and can be crucial to rational treatment and pdiction of outcome. Cerebrovascular disease is a complex condition and currently there are a number of diagnostic procedures. Many of these procedures are time-consuming and not always feasible(1-3).

The cerebral arrays have been specially designed for research that is required to determine the pathological processes that pcede the onset of stroke, development of diagnostic markers specific for each of the different types of stroke and also development of tests for the pdiction of outcome and likelihood of further stroke episodes.

PRINCIPLE

Evidence Investigator Biochip Array Technology is used to perform simultaneous quantitative detection of multiple analytes from a single patient sample. The core technology is the Randox Biochip, a (9 mm(2)) solid substrate containing an array of discrete test regions of immobilized antibodies specific to different cerebral markers.

A chemiluminescent immunoassay is employed. The light signal generated from each of the test regions on the biochip is detected using a CCD camera and state-of-the-art digital imaging technology.

The light signal generated from each of the test regions on the biochip is detected using digital imaging technology and compared to that from a stored calibration curve. From this the concentration is calculated.

Several different immunoassay based multi-analyte panels have been developed for use on Evidence Investigator . The Cerebral Array II Panel will quantitatively test for Neuron Specific Enolase, Neutrophil Gelatinase-associated Lipocalin, Soluble Tumor Necrosis Factor Receptor I, D-Dimer, Thrombomodulin and C-reactive protein simultaneously.

REFERENCES

1. Frizzell J.P. (2005) Acute stroke: pathophysiology, diagnosis, and treatment. AACN Clin Issues. 16(4): 421-40.

2. Foerch C., Otto B., Singer O.C., Neumann-Haefelin T., Yan B., Berkefeld J., Steinmetz H. and Sitzer M. (2004) Serum S100B pdicts a malignant course of infarction in patients with acute middle cerebral artery occlusion. Stroke. 35(9): 2160-4.

3. Missler U., Wiesmann M., Friedrich C. and Kaps M. (1997) S-100 Protein and Neuron-Specific Snolase Concentrations in Blood as Indicators of Infarction Volume and Prognosis in Acute Ischemic Stroke. Stroke. 28(10): 1956-60.

4. Primus FJ, Kelley EA, Hansen HJ, Goldenberg DM. "Sandwich"-Type Immunoassay of Carcinoembryonic Antigen in Patients Receiving Murine Monoclonal Antibodies for Diagnosis and Therapy. Clin Chem 1988;35:261.

5. Hansen HJ, Solving the Problem of Antibody Interference in Commercial "Sandwich"-Type Immunoassay of Carcinoembryonic Antigen. Clin Chem 1989;35:146.

6. Schroff RW, Foon KA, Beatty SM, Oldham RK, Morgan AC Jr. Human Anti-Mouse Immunoglobulin Responses in Patients Receiving Monoclonal Antibody Therapy. Cancer Res 1985;45:879.

7. Boscato LM, Stuart MC. Heterophilic Antibodies: A Problem for all Immunoassays. Clin Chem 1998;34:27.

 

Neuron Specific Enolase (NSE) Assay

INTENDED USE

The Evidence Investigator NSE assay has been designed for the quantitative measurement of NSE in human plasma samples.

CLINICAL SIGNIFICANCE

Neuron specific enolase is an isoenzyme of enolase, which is a dimeric glycolytic enzyme that converts 2 phosphoglycerate to phosphoenolpyruvate. There are three distinct subunits α, β and γ, with the γγ isoenzyme shown to exist in high concentrations only in cells of neuroendocrine or neuronal origin. NSE is the γγ isoenzyme of enolase and is a highly soluble cytoplasmic protein(1) of approximately 80 kDa(2), that after tissue damage is readily released into the CSF and blood(1,2). It has been shown to be a valuable tumor marker of neuroendocrine origin, particularly in small cell lung cancer and in neuroblastoma(3,4). There have been a number of studies measuring NSE levels in stroke and brain injury patients, and it has been reported that blood NSE is elevated in stroke(2,5-8). A recent review of all suitable studies involving NSE and stroke patients found that the serum level of NSE was higher in stroke patients than controls, and that it seemed to correlate with the volume of infarcted tissue(9).

PRINCIPLE

The Evidence Investigator NSE assay is a sandwich chemiluminescent assay for the detection of NSE in human plasma.

References

1. Cunningham R.T., Watt M., Winder J., McKinstry S., Lawson J.T., Johnston C.F., Hawkins S.A. and Buchanan K.D. (1996) Serum neurone-specific enolase as an indicator of stroke volume. Eur. J. Clin. Invest. 26(4): 298-303.

2. Oh S.H., Lee J.G., Na S.J., Park J.H., Choi Y.C. and Kim W.J. (2003) pdiction of Early Clinical Severity and Extent of Neuronal Damage in Anterior-Circulation Infarction Using the Initial Serum Neuron-Specific Enolase Level. Arch. Neurol. 60(1): 37-41.

3. Koyama R. (1995) [Gamma-enolase (gamma-eno)]. Nippon Rinsho. 53(5): 1277-81.

4. Martens P., Raabe A. and Johnsson P. (1998) Serum S-100 and Neuron-Specific Enolase for pdiction of Regaining Consciousness after Global Cerebral Ischemia. Stroke. 29(11): 2363-2366.

5. Cunningham R.T., Young I.S., Winder J., O'Kane M.J., McKinstry S., Johnston C.F., Dolan O.M., Hawkins S.A. and Buchanan K.D. (1991) Serum neurone specific enolase (NSE) levels as an indicator of neuronal damage in patients with cerebral infarction. Eur. J. Clin. Invest. 21(5): 497-500.

6. Fassbender K., Schmidt R., Schreiner A., Fatar M., Muhlhauser F., Daffertshofer M. and Hennerici M.J. (1997) Leakage of brain-originated proteins in peripheral blood: temporal profile and diagnostic value in early ischemic stroke. Neurol. Sci. 148(1): 101-105.

7. Missler U., Wiesmann M., Friedrich C. and Kaps M. (1997) S-100 Protein and Neuron-Specific Enolase Concentrations in Blood as Indicators of Infarction Volume and Prognosis in Acute Ischemic Stroke. Stroke. 28(10): 1956-1960.

8. Herrmann M. and Ehrenreich H. (2003) Brain derived proteins as markers of acute stroke: Their relation to pathophysiology, outcome pdiction and neuroprotective drug monitoring. Restor. Neurol. Neurosci. 21(3-4): 177-190.

9. Anand N. and Stead LG. (2005) Neuron-Specific Enolase as a Marker for Acute Ischemic Stroke: A Systematic Review. Cerebrovasc. Dis. 20(4): 213-9.

10. Pelinka L. E. (2004) Serum markers of severe traumatic brain injury: Are they useful? Indian J. Crit. Care Med. 8: 190-193.

 

Neutrophil Gelatinase-Associated Lipocalin (NGAL) Assay

INTENDED USE

The Evidence Investigator NGAL assay has been designed for the quantitative measurement of NGAL in human plasma samples.

CLINICAL SIGNIFICANCE

NGAL is a 25 kDa protein that is a member of the lipocalin family(1), and is secreted from specific granules of human neutrophils upon activation of the cells(2). Some of the synonyms of NGAL are human neutrophil lipocalin HNL, N-formyl peptide binding protein and 25 kDa α2-microglobulin-related protein(3). The lipocalin family has more than 25 members(4), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core(1,4). The lipocalins also have a tendency to associate with other proteins and as its name suggests NGAL has been found to associate with gelatinase(1). However, it has been shown that NGAL exists mainly in forms not associated with gelatinase, namely as the monomeric and homodimeric forms(1). The lipocalins seem to be able to bind several different ligands rather than being specific for one(4). The function of NGAL is not well known but is thought to be important during the inflammatory response (1-4). NGAL levels have been measured in a number of conditions and elevated levels of NGAL have been found to distinguish acute bacterial and viral infections with a high degree of accuracy and specificity(3). It has also been shown to be elevated in patients with acute severe peritonitis, cystic fibrosis, and in a number of other conditions(3). NGAL levels have been measured in relation to stroke and it has been shown that NGAL is elevated in plasma after stroke in the acute stage(5) and that it remains elevated for some time afterwards(6). As elevated NGAL is considered a marker of neutrophil activation, it is not a specific marker for brain damage associated with stroke(3).

PRINCIPLE

The Evidence Investigator NGAL assay is a sandwich chemiluminescent assay for the detection of NGAL in human plasma.

References

1. Kjeldsen L., Bainton D.F., Sengelov H. and Borregaard N. (1994) Identification of Neutrophil Gelatinase-Associated Lipocalin as a Novel Matrix Protein of Specific Granules in Human Neutrophils. Blood. 83(3): 799-807.

2. Falke P., Elneihoum A.M. and Ohlsson K. (2000) Leukocyte Activation: Relation to Cardiovascular Mortality after Cerebrovascular Ischemia. Cerebrovasc. Dis. 10(2): 97-101.

3. Xu S. and Venge P. (2000) Lipocalins as biochemical markers of disease. Biochim. Biophys. Acta. 1482(1-2): 298-307.

4. Kjeldsen L., Koch C., Arnljots K. and Borregaard N. (1996) Characterization of two ELISAs for NGAL, a newly described lipocalin in human neutrophils. Immunol. Methods. 198(2): 155-164.

5. Elneihoum A.M., Falke P., Axelsson L., Lundberg E., Lindgarde F. and Ohlsson K. (1996) Leukocyte Activation Detected by Increased Plasma Levels of Inflammatory Mediators in Patients With Ischemic Cerebrovascular Diseases. Stroke. 27: 1734-1738.

6. Anwaar I., Gottsater A., Ohlsson K., MattiassonI. and Lindgarde F. (1998) Increasing Levels of Leukocyte-Derived Inflammatory Mediators in Plasma and cAMP in Platelets during Follow-Up after Acute Cerebral Ischemia. Cerebrovasc. Dis. 8(6): 310-317.

 

Soluble Tumor Necrosis Factor Receptor I (TNFRI) Assay

INTENDED USE

The Evidence Investigator TNFRI assay has been designed for the quantitative measurement of sTNFRI in human plasma samples.

CLINICAL SIGNIFICANCE

sTNFRI is the soluble form of the tumor necrosis factor receptor I (p55, p60, CD120a, TNFRSF1A) found in serum, urine and other body fluids which repsents the extracellular portion of the membrane associated receptor(1). The membrane associated receptor is one of two specific, high affinity cell surface receptors (TNFRI p55 and TNFRII p75) that function as transducing elements, providing the intracellular signal for cell responses to tumor necrosis factor (TNF)(2). TNFRI has a molecular mass of 55 kDa(1) and is involved in interleukin-2 receptor induction, anti-viral activities, growth stimulation, HLA antigens expssion and endothelial cells adhesion. Shedding of the soluble receptor is induced by various ways, such as TNF itself, other cytokines and agents and cell to cell contact. It is thought that the shedding process is probably tissue and cytokine specific(2).

Elevated levels have been found in serum and plasma in various infectious, inflammatory, autoimmune, malignant and neoplastic diseases(3,4). It has been reported that the levels were higher in patients with acute ischemic cerebrovascular disease than in normal control subjects, and that higher plasma levels of sTNFRI could be a significant pdictor of cardiovascular mortality after cerebrovascular ischemia(3-6).

PRINCIPLE

The Evidence Investigator TNFRI assay is a sandwich chemiluminescent assay for the detection of sTNFRI in human plasma.

REFERENCES

1. Carpentier I., Coornaert B. and Beyaert R. (2004) Function and Regulation of Tumor Necrosis Factor Receptor Type 2. Curr Med Chem. 11(16): 2205-12.

2. Aderka D. (1996) The Potential Biological and Clinical Significance of the Soluble Tumor Necrosis Factor Receptors. Cytokine Growth Factor Rev. 7(3): 231-40.

3. Elneihoum A.M., Falke P., Axelsson L., Lundberg E., Lindgarde F. and Ohlsson K. (1996) Leukocyte Activation Detected by Increased Plasma Levels of Inflammatory Mediators in Patients with Ischemic Cerebrovascular Diseases. Stroke. 27: 1734-1738.

4. Elkind M.S., Cheng J., Boden-Albala B., Rundek T., Thomas J., Chen H., Rabbani L.E. and Sacco R.L. (2002) Tumor Necrosis Factor Receptor Levels Are Associated With Carotid Atherosclerosis. Stroke. 33(1): 31-7.

5. Anwaar I., Gottsater A., Ohlsson K., MattiassonI. and Lindgarde F. (1998) Increasing Levels of Leukocyte-Derived Inflammatory Mediators in Plasma and cAMP in Platelets during Follow-Up after Acute Cerebral Ischemia. Cerebrovasc. Dis. 8(6): 310-7.

6. Falke P., Elneihoum A.M. and Ohlsson K. (2000) Leukocyte Activation: Relation to Cardiovascular Mortality after Cerebrovascular Ischemia. Cerebrovasc. Dis. 10(2): 97-101.

 

D-dimer (DDMER) Assay

INTENDED USE

The Evidence Investigator DDMER assay has been designed for the quantitative measurement of D-dimer in human plasma samples.

CLINICAL SIGNIFICANCE

D-dimer is a product of fibrinolysis and is formed when cross-linked fibrin is degraded by plasmin. During clot formation fibrinogen is transformed into fibrin by thrombin at sites of vascular injury. The fibrin is then stabilized by cross-links to form an insoluble fibrin clot. The fibrinolytic system removes the formed clot by proteolytically degrading the fibrin. Plasmin cleaves the fibrin to produce smaller degradation products, typically containing two D domains (D-dimer). Therefore D-dimer is not merely a single substance but exists as a complex variety of cross-linked fibrin derivatives, with a range of molecular weights(1,2). D-dimer is considered to be a marker of plasmin activity, and fibrinolysis(3). It has been reported that elevations in plasma D-dimer concentration is dependent on the type of stroke and if elevated, the levels correlate with the degree of damage and neurological outcome(3-8). As D-dimer is a marker of fibrinolysis activation it is not specific for stroke, and can be elevated in other disease states, and conditions(3).

PRINCIPLE

The Evidence Investigator DDMER assay is a sandwich chemiluminescent assay for the detection of D-dimer in human plasma.

REFERENCES

1. Keeling D.M., Mackie I.J., Moody A. and Watson H.G. The Haemostasis and Thrombosis Task Force of the British Committee for Standards in Haematology. (2004) The diagnosis of deep vein thrombosis in symptomatic outpatients and the potential for clinical assessment and D-dimer assays to reduce the need for diagnostic imaging. Br. J. Haematol. 124(1): 15-25.

2. Haapaniemi E., Soinne L., Syrjala M., Kaste M. and Tatlisumak T. (2004) Serial changes in fibrinolysis and coagulation activation markers in acute and convalescent phase of ischemic stroke. Acta Neurol. Scand. 110(4): 242-247.

3. Ince B., Bayram C., Harmanci H. and Ulutin T. (1999) Hemostatic Markers in Ischemic Stroke of Undetermined Etiology. Thromb Res. 96(3): 169-74.

4. Kataoka S., Hirose G., Hori A., Shirakawa T. and Saigan T.J. (2000) Activation of thrombosis and fibrinolysis following brain infarction. Neurol. Sci. 181(1-2): 82-88.

5. Ono N., Koyama T., Suehiro A., Oku K., Fujikake K. and Kakishita E. (1991) Clinical Significance of New Coagulation and Fibrinolytic Markers in Ischemic Stroke Patients. Stroke. 22(11): 1369-1373.

6. Berge E., Friis P. and Sandset P.M. (2001) Hemostatic Activation in Acute Ischemic Stroke. Thromb. Res. 101(2): 13-21.

7. Altes A., Abellan M.T., Mateo J., Avila A., Marti-Vilalta J.L. and Fontcuberta J. (1995) Hemostatic Disturbances in Acute Ischemic Stroke: a Study of 86 Patients. Acta Haematol. 94(1): 10-15.

8. Fon E.A., Mackey A., Cote R., Wolfson C., McIlraith D.M., Leclerc J. and Bourque F. (1994) Hemostatic Markers in Acute Transient Ischemic Attacks. Stroke. 25(2): 282-286

 

C-Reactive Protein (CRP) Assay

INTENDED USE

The Evidence Investigator CRP assay has been designed for the quantitative measurement of CRP in human plasma samples.

CLINICAL SIGNIFICANCE

CRP is composed of 5 identical, non-covalently bonded subunits and belongs to the pentraxins, a family of pentameric proteins. Each subunit consists of 206 amino acids with the total molecular weight of CRP approximately 120 kDa. It is an acute phase reactant that is synthesized in the liver, with its synthesis controlled by cytokines especially IL-6(1-4). The serum CRP concentration may increase up to 1000 fold with infection, trauma, surgery, and other acute inflammatory events within 24 to 48 hours(3-5). It has a half-life of approximately 19 hours and is the most consistently increased and fastest acting acute phase protein(4). Traditionally serum CRP has been used clinically for diagnosis of various infections and inflammatory processes(1,4). Chronic inflammation plays a major role in the development and progression of atherosclerosis and it has been demonstrated that increases in CRP concentrations within the reference interval are associated with future coronary artery disease, cerebrovascular disease and peripheral arterial disease(1,4-6).

High sensitivity CRP assays have been used to measure the CRP variability within the reference range as traditional CRP methods lack sensitivity (4,6). In a recent AHA Conference proceedings report on markers of inflammation and cardiovascular disease hsCRP cut-off points were recommended for risk assessment. Low risk was <1.0 mg/L, average risk was 1.0 to 3.0 mg/L, and high risk was >3.0 mg/L. It was recommended that if the CRP concentration was >10 mg/L then the test should be repeated and the person examined for sources of infection or inflammation(3).

PRINCIPLE

The Evidence Investigator CRP assay is a sandwich chemiluminescent assay for the detection of CRP in human plasma.

REFERENCES

1. Roberts W.L., Moulton L., Law T.C., Farrow G., Cooper-Anderson M., Savory J. and Rifai N. (2001) Evaluation of Nine Automated High-Sensitivity C-Reactive Protein Methods: Implications for Clinical and Epidemiological Applications. Part 2. Clin. Chem. 47(3): 418-25.

2. Roberts W.L. (2004) CDC/AHA Workshop on Markers of Inflammation and Cardiovascular Disease: Application to Clinical and Public Health Practice: Laboratory Tests Available to Assess Inflammation - Performance and Standardization A. Background Paper. Circulation. 110(25): e572-6.

3. Myers G.L., Rifai N., Tracy R.P., Roberts W.L., Alexander R.W., Biasucci L.M., Catravas J.D., Cole T.G., Cooper G.R., Khan B.V., Kimberly M.M., Stein E.A., Taubert K.A., Warnick G.R. and Waymack P.P. (2004) CDC/AHA Workshop on Markers of Inflammation and Cardiovascular Disease: Application to Clinical and Public Health Practice: Report From the Laboratory Science Discussion Group. Circulation. 110(25): e545-9.

4. Ledue T.B and Rifai N. (2003) panalytic and Analytic Sources of Variations in C-Reactive Protein Measurement: Implications for Cardiovascular Disease Risk Assessment. Clin. Chem. 49(8): 1258-71.

5. Cao J.J., Thach C., Manolio T.A., Psaty B.M., Kuller L.H., Chaves P.H., Polak J.F., Sutton-Tyrrell K., Herrington D.M., Price T.R. and Cushman M. (2003) C-Reactive Protein, Carotid Intima-Media Thickness, and Incidence of Ischemic Stroke in the Elderly: The Cardiovascular Health Study. Circulation. 108(2): 166-70.

6. Roberts W.L., Sedrick R., Moulton L., Spencer A. and Rifai N. (2000) Evaluation of Four Automated High-Sensitivity C-Reactive Protein Methods: Implications for Clinical and Epidemiological Applications. Clin. Chem. 46(4): 461-8.