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Cerebral array i

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Cerebral array i B A T (evidence investigatorâ„¢) 54 biochips EV3573 $7538.95
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Intended Use

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

The Evidence Investigator Cerebral Array I is for research use only and not for use in diagnosis.

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 prediction 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 precede the onset of stroke, development of diagnostic markers specific for each of the different types of stroke and also development of tests for the prediction 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 solid substrate containing an array of discrete test regions of immobilized antibodies specific to different cerebral markers. A sandwich chemiluminescent immunoassay is employed. Increased levels of cerebral markers in a sample will lead to increased binding of antibody labeled with horseradish peroxidase (HRP) and thus an increase in the chemiluminescence signal emitted. The light signal generated from each of the test regions on the biochip is detected using state-of-the-art digital imaging technology and compared to that from a stored calibration curve. The concentration of analyte present in the sample is then calculated from the calibration curve.

Several different immunoassay based multi-analyte panels have been developed for use on Evidence Investigator. The Cerebral Array I will quantitatively test for brain derived neurotrophic factor (BDNF), heart type fatty acid binding protein (FABP), glial fibrillary acidic protein (GFAP) and interleukin-6 (IL6) 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 predicts 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.

 

Brain Derived Neurotrophic Factor (BDNF) Assay

Intended Use

The Evidence Investigator BDNF assay has been designed for the quantitative measurement of BDNF in human plasma, serum and CSF samples.

This assay is for research use only.

Clinical Significance

BDNF is one of the neurotrophins, which are a family of growth factors that are expressed in the mammalian nervous system. BDNF is synthesized as a 32 kDa precursor, which is cleaved to form the mature BDNF, a 14 kDa non-glycosylated polypeptide (1). In vitro studies have shown that the uncleaved BDNF may be released extracellularly and that it could be biologically active (1,2). The primary structure of BDNF is the same for a number of species that have been examined (3). BDNF is widely distributed throughout the central nervous system with a number of different cell types known to express it (1). A large number of functions have been attributed to BDNF (2-6). It is recognized as playing an important role in the survival, differentiation and outgrowth of select peripheral and central neurons during development and in adulthood (1,2,6). It is thought that BDNF has a beneficial role in the brain after injury and limits neurodegenerative damage (2,4,5). As there is a significant difference in the levels of BDNF detected in serum and plasma it is thought that BDNF is present in platelet granules and is released upon platelet activation (3).

Principle

The Evidence Investigator BDNF assay is a sandwich chemiluminescent assay for the detection of BDNF in human plasma, serum and CSF.

REFERENCES

1. Mowla S.J., Farhadi H.F., Pareek S., Atwal J.K., Morris S.J., Seidah N.G. and Murphy R.A. (2001) Biosynthesis and Post-translational Processing of the Precursor to Brain-derived Neurotrophic Factor. J. Biol. Chem. 276(16): 12660-6.

2. Hashimoto K., Shimizu E. and Iyo M. (2004) Critical role of brain-derived neurotrophic factor in mood disorders. Brain Res Brain Res Rev. 45(2): 104-114.

3. Radka S.F., Holst P.A., Fritsche M. and Altar C.A. (1996) Presence of brain-derived neurotrophic factor in brain and human and rat but not mouse serum detected by a sensitive and specific immunoassay. Brain Res. 709(1): 122-301.

4. Wu D. (2005) Neuroprotection in Experimental Stroke with Targeted Neurotrophins. NeuroRx. 2(1): 120-8.

5. Binder D.K. and Scharfman H.E. (2004) Brain-derived Neurotrophic Factor. Growth Factors. 22(3): 123-31.

6. Kalb R. (2005) The protean actions of neurotrophins and their receptors on the life and death of neurons. Trends Neurosci. 28(1): 5-11.

 

Heart Type Fatty Acid Binding Protein (FABP) Assay

Intended Use

The Evidence Investigator FABP assay has been designed for the quantitative measurement of heart type FABP (hFABP) in human plasma , serum and CSF samples.

This assay is for research use only.

Clinical Significance

The fatty acid binding proteins (FABPs) are a family of small (15 kDa) cytoplasmic, non-enzymatic proteins that are involved in lipid homeostasis by intracellular buffering and transport of long-chain fatty acids (1-3). Members of the FABP family of proteins have 126 to 137 amino acid residues and show between 20 to 70% sequence homology. They have been detected in virtually all tissue types but are abundantly expressed in tissues with an active fatty acid metabolism like heart and liver and are released rapidly into the circulation from damaged cells. There are nine FABP members that have mostly been named after the tissue from which they were first isolated (1,3). They have a stable intracellular half-life of 2-3 days with distinct types showing a characteristic pattern of tissue distribution. hFABP is one of the main types of FABP and has been found to be an early and sensitive marker of cardiac injury (1).

Plasma hFABP has also been reported to be a valid biomarker for the early diagnose of stroke (2). Studies of the tissue distribution of brain type FABP (bFABP) and hFABP in segments of brain suggest that serum hFABP could be used with serum bFABP in a ratio to diagnose stroke, which may also be able to locate the area of brain injury (3). In another study hFABP and bFABP concentrations showed peak values 2 to 3 hours after stroke onset and remained elevated up to 120 hours after stroke onset. In this study hFABP, unlike bFABP, concentrations were significantly associated with the severity of the neurological deficit and functional outcome (4). As hFABP can be used as a biomarker for other tissue damage it cannot be regarded as specific for stroke (1,4).

Principle

The Evidence Investigator FABP assay is a sandwich chemiluminescent assay for the detection of hFABP in human plasma, serum and CSF.

REFERENCES

1. Pelsers M.M., Hermens W.T. and Glatz J.F. (2005) Fatty acid-binding proteins as plasma markers of tissue injury. Clin. Chim. Acta. 352(1-2): 15-35.

2. Zimmermann-Ivol C.G., Burkhard P.R., Le Floch-Rohr J., Allard L., Hochstrasser D.F. and Sanchez J.C. (2004) Fatty Acid Binding Protein as a Serum Marker for the Early Diagnosis of Stroke: a pilot study. Mol. Cell Proteomics. 3(1): 66-72.

3. Pelsers M.M., Hanhoff T., Van der Voort D., Arts B., Peters M., Ponds R., Honig A., Rudzinski W., Spener F., de Kruijk J.R., Twijnstra A., Hermens W.T., Menheere P.P. and Glatz J.F. (2004) Brain- and Heart-Type Fatty Acid-Binding Proteins in the Brain: Tissue Distribution and Clinical Utility. Clin. Chem. 50(9): 1568-1575.

4. Wunderlich M.T., Hanhoff T., Goertler M., Spener F., Glatz J.F., Wallesch C.W. and Pelsers M.M. (2005) Release of brain-type and heart-type fatty acid-binding proteins in serum after acute ischemic stroke. J Neurol. 252(6): 718-24.

 

Glial Fibrillary Acidic Protein (GFAP) Assay

Intended Use

The Evidence Investigator GFAP assay has been designed for the quantitative measurement of GFAP in human plasma, serum and CSF samples.

This assay is for research use only.

Clinical Significance

GFAP is the major intermediate filament protein in human astrocytes. It is a non-soluble acidic protein and belongs to the class-III intermediate filament proteins (1,2). Cytoskeletal GFAP is tightly packed into polymers and after break-up of the polymer a soluble fragment of approximately 41 kDa is released (2). It is expressed almost exclusively by astrocytes, which suggests that it could be a very specific marker for astrocyte damage (1,3). Researchers interested in serum markers absolutely specific for central nervous system considered GFAP a high priority candidate (1,3-5). In a small number of studies GFAP levels have been measured in CSF in neurological disorders (2,3,6). A number of studies have measured the levels of GFAP in blood and have found it to be significantly elevated following stroke onset (1,3,4,6). Studies have indicated that the release pattern of GFAP may be dependent on subtype of stroke and therefore may allow insight into the underlying pathophysiology of stroke (3-7).

Principle

The Evidence Investigator GFAP assay is a sandwich chemiluminescent assay for the detection of GFAP in human plasma, serum and CSF.

REFERENCES

1. van Geel W.J.A., de Reus H.P.M., Nijzing H., Verbeek M.M., Vos P.E. and Lamers K.J.B. (2002) Measurement of glial fibrillary acidic protein in blood: an analytical method. Clinica Chimica Acta. 326(1-2): 151-154.

2. Petzold A., Keir G., Green A.J.E., Giovannoni G. and Thompson E.J.J. (2004) An ELISA for glial fibrillary acidic protein. Immunol. Methods. 287(1-2): 169-177.

3. Herrmann M., Vos P., Wunderlich M.T., de Bruijn C.H.M.M. and Lamers K.J.B. (2000) Release of Glial Tissue-Specific Proteins After Acute Stroke. A Comparative Analysis of Serum Concentrations of Protein S-100B and Glial Fibrillary Acidic Protein. Stroke. 31: 2670-2677.

4. Missler U., Wiesmann M., Wittmann G., Magerkurth O. and Hagenström H. (1999) Measurement of Glial Fibrillary Acidic Protein in Human Blood: Analytical Method and Preliminary Clinical Results. Clin. Chem. 1999 138-141.

5. Pelinka L.E., Kroepfl A., Schmidhammer R., Krenn M., Buchinger W., Redl H. and Raabe A. (2004) Glial Fibrillary Acidic Protein in Serum After Traumatic Brain Injury and Multiple Trauma. J. Trauma. 57(5): 1006-1012.

6. Lamers K.J., Vos P., Verbeek M.M., Rosmalen F., van Geel W.J. and van Engelen B.G. (2003) Protein S-100B, neuron-specific enolase (NSE), myelin basic protein (MBP) and glial fibrillary acidic protein (GFAP) in cerebrospinal fluid (CSF) and blood of neurological patients. Brain Res. Bull. 61(3): 261-4.

7. Herrmann M. and Ehrenreich H. (2003) Brain derived proteins as markers of acute stroke: their relation to pathophysiology, outcome prediction and neuroprotective drug monitoring. Restor. Neurol. Neurosci. 21(3-4): 177-90.

 

Interleukin-6 (IL6) Assay

Intended Use

The Evidence Investigator IL6 assay has been designed for the quantitative measurement of IL6 in human plasma, serum and CSF samples.

This assay is for research use only.

Clinical Significance

IL6 is a pleiotrophic cytokine that is involved in the regulation of a number of important biological processes. It is produced by both lymphoid and non lymphoid cells and is a glycoprotein of 212 amino acids including a signal peptide of 28 amino acids. IL6 is a key mediator of the acute phase response and possesses anti-inflammatory and neurotrophic properties. It has also been shown to have a protective role in several cytokine mediated pathologies (1-2). Stroke can trigger an acute-phase response and elevated levels of acute phase response proteins have been found in stroke patients (3). It has been reported that IL6 is more significantly elevated in CSF than serum following stroke, and it has been proposed that astrocytes are the major IL6 expressing cells in injured brain (2-4). IL6 concentrations rise after stroke onset and results from studies indicate a role for IL6 in the regulation of the inflammatory response in stroke although the mechanism seems to be complex (3,5). It has been reported that the IL6 level correlates with parameters of brain damage in intracerebral hemorrhage and volume of brain lesion in ischemic stroke (3,6,7). Serum elevations of IL6 can be associated with many other proinflammatory conditions so elevations of serum IL6 are not specific for stroke (2,4-7).

Principle

The Evidence Investigator IL6 assay is a competitive chemiluminescent assay for the detection of IL6 in human plasma, serum and CSF.

REFERENCES

1. Hirano T. (1998) Interleukin 6. In The Cytokine Handbook, 3rd ed. Thomson A. (ed) Academic Press, San Diego. pp 197-228.

2. Terreni L. and De Simoni M.G. (1998) Role of the Brain in Interleukin-6 Modulation. Neuroimmunomodulation. 5(3-4): 214-9.

3. Tarkowski E., Rosengren L., Blomstrand C., Wikkelsö C., Jensen C., Ekholm S. and Tarkowski A. (1995) Early Intrathecal Production of Interleukin-6 Predicts the Size of Brain Lesion in Stroke. Stroke. 26: 1393-1398.

4. Kim H.M., Shin H.Y., Jeong H.J., An H.J., Kim N.S., Chae H.J., Kim H.R., Song H.J., Kim K.Y., Baek S.H., Cho K.H., Moon B.S. and Lee Y.M.J. (2000) Reduced IL-2 But Elevated IL-4, IL-6, and IgE Serum Levels in Patients with Cerebral Infarction During the Acute Stage. Mol. Neurosci. 14(3): 191-6.

5. Dziedzic T., Bartus S., Klimkowicz A., Motyl M., Slowik A. and Szczudlik A. (2002) Intracerebral Hemorrhage Triggers Interleukin-6 and Interleukin-10 release in Blood. Stroke. 33(9): 2334-5.

6. Acalovschi D., Wiest T., Hartmann M., Farahmi M., Mansmann U., Auffarth G.U., Grau A.J., Green F.R., Grond-Ginsbach C. and Schwaninger M. (2003) Multiple Levels of Regulation of the Interleukin-6 System in Stroke. Stroke. 34(8): 1864-9.

7. Smith C.J., Emsley H.C., Gavin C.M., Georgiou R.F., Vail A., Barberan E.M., del Zoppo G.J., Hallenbeck J.M., Rothwell N.J., Hopkins S.J. and Tyrrell P.J. (2004) Peak plasma interleukin-6 and other peripheral markers of inflammation in the first week of ischemic stroke correlate with brain infarct volume, stroke severity and long-term outcome. BMC Neurol. 4: 2.

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