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C1 inhibitor function using contact-phase proteases as target: evaluation of an innovative assay.

Controlling prekallikrein activation by C1 inhibitor (C1Inh) represents the most essential mechanism for angioedema patient protection. C1Inh function in the plasma is usually measured based on the residual activity of the C1s protease not involved in the pathological process. We have hereby proposed an alternative enzymatic measurement of C1Inh function based on contact-phase activation and correlation with angioedema diagnostic requirements.

2966 related Products with: C1 inhibitor function using contact-phase proteases as target: evaluation of an innovative assay.

Active human antiplasmin Mouse Anti-Insulin-Like G Mouse anti-chick type I c Mouse anti-chick type I c Mouse anti-bovine type I Mouse anti-bovine type I Mouse anti-porcine type I Mouse anti-porcine type I Mouse anti-human type I c Mouse anti-mouse type I c Mouse anti-mouse type I c Rat anti-chick type I col

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Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma.

A simple mass spectrometric approach for the discovery and validation of biomarkers in human plasma was developed by targeting nonglycosylated tryptic peptides adjacent to glycosylation sites in an N-linked glycoprotein, one of the most important biomarkers for early detection, prognoses, and disease therapies. The discovery and validation of novel biomarkers requires complex sample pretreatment steps, such as depletion of highly abundant proteins, enrichment of desired proteins, or the development of new antibodies. The current study exploited the steric hindrance of glycan units in N-linked glycoproteins, which significantly affects the efficiency of proteolytic digestion if an enzymatically active amino acid is adjacent to the N-linked glycosylation site. Proteolytic digestion then results in quantitatively different peptide products in accordance with the degree of glycosylation. The effect of glycan steric hindrance on tryptic digestion was first demonstrated using alpha-1-acid glycoprotein (AGP) as a model compound versus deglycosylated alpha-1-acid glycoprotein. Second, nonglycosylated tryptic peptide biomarkers, which generally show much higher sensitivity in mass spectrometric analyses than their glycosylated counterparts, were quantified in human hepatocellular carcinoma plasma using a label-free method with no need for N-linked glycoprotein enrichment. Finally, the method was validated using a multiple reaction monitoring analysis, demonstrating that the newly discovered nonglycosylated tryptic peptide targets were present at different levels in normal and hepatocellular carcinoma plasmas. The area under the receiver operating characteristic curve generated through analyses of nonglycosylated tryptic peptide from vitronectin precursor protein was 0.978, the highest observed in a group of patients with hepatocellular carcinoma. This work provides a targeted means of discovering and validating nonglycosylated tryptic peptides as biomarkers in human plasma, without the need for complex enrichment processes or expensive antibody preparations.

1285 related Products with: Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma.

Lipoproteins, Human Plasm Human interleukin 2(IL-2) Prolactin-Inducible Prote Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Bone Morphogenetic Protei Growth Differentiation Fa CELLKINES Natural Human I Human Interleukin-4 IL-4 Human Interleukin-6 IL-6 Human Interleukin-7 IL-7 Human Interleukin-2 IL-2

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Changes in high molecular weight kininogen levels during and after cardiopulmonary bypass surgery measured using a chromogenic peptide substrate assay.

High molecular weight kininogen (HK) is a co-factor in the blood-contact activation system. A chromogenic peptide substrate assay for HK (HKcs) has been developed in which test plasmas are mixed with diluted HK-deficient plasma and incubated with a soluble contact system activator that activates prekallikrein and factor XII. Calcium chloride, a synthetic thrombin inhibitor and a chromogenic peptide substrate for activated factor X (FXa) are then added. The FXa generated cleaves the FXa substrate releasing p-nitroanaline, which is measured photometrically. Test plasma HK values were calculated from a standard curve generated using a pooled normal plasma. Acceptable intra-assay and inter-assay precision values were obtained and levels of HK up to 200% were measurable. The assay measured HK in plasmas deficient in factor XII, prekallikrein and factor XI, was not affected by antiphospholipid antibodies and gave an acceptable correlation (r = 0.95) when normal plasmas and mixtures of HK-deficient and normal pooled plasma, calculated to give HK levels of 25 and 50%, were compared using HKcs and a HK one-stage clotting assay. The HKcs was used to measure HK levels in seven patients undergoing cardiopulmonary bypass (CPB). HK levels fell significantly during CPB (P = 0.0014) and were significantly higher (P = 0.016) 6 days after CPB, suggesting that HK may be a positive acute-phase reacting protein.

2506 related Products with: Changes in high molecular weight kininogen levels during and after cardiopulmonary bypass surgery measured using a chromogenic peptide substrate assay.

Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu EnzyChrom™ Kinase Assay MarkerGene™ Cellular Se Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu Amplite™ Fluorimetric H Amplite™ Intracellular Amplite™ Fluorimetric P Amplite™ Fluorimetric A

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Contact activation factors in plasma from women on estrogen replacement therapy after ovariohysterectomy.

The plasma levels of factor XII, prekallikrein, factor XI, and high molecular weight kininogen were studied in women with bilateral oophorectomy and hysterectomy who received hormone replacement therapy with a 2 mg daily dose of estradiol valerate. Also plasminogen activator activity was investigated. The observations made provide support for the assumption that the low doses of estrogen used in hormone replacement therapy do not significantly affect the levels of contact activation or fibrinolytic factors in plasma. Plasma obtained from young, healthy women was used as a standard reference material. Significantly higher levels of factor XII and prekallikrein were registered in functional tests in the ectomized women than in the reference material, an increase not observed in the immunological assays. These observations are discussed in light of recently published data from our laboratory on an increase in the measured level of factor XII obtained upon the removal of IgG before assay. Also a marked increase in urokinase activity was registered in the ectomized women. The high levels of factor XII, prekallikrein, and urokinase, as compared with the reference material, seemed to be age dependent, being also observed in a group of naturally postmenopausal women.

1880 related Products with: Contact activation factors in plasma from women on estrogen replacement therapy after ovariohysterectomy.

Contact Factors: Human Fa Stat3 Activation Inhibito EtBr Destaining Bag Kit A Lipoproteins, Human Plasm Rabbit Anti-FGF3 Oncogene Human interleukin 2(IL-2) Bovine prolactin-induced Transcription factors: O Plasma Proteins: Corn Try Contact Factors: Human al Contact Factors: Human Fa Contact Factors: Human Fa

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Cleavage of plasma high molecular weight kininogen in surgical ICU patients.

To characterize kininogens in plasma from surgical patients in the intensive care unit (ICU).

2146 related Products with: Cleavage of plasma high molecular weight kininogen in surgical ICU patients.

Plasma Proteins: Two Chai Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma Anti RAGE (Receptor for A Lipoproteins, Human Plasm Lipoproteins, Human Plasm

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Plasma activity of contact coagulation factors in patients with IgA nephritis.

Intraglomerular coagulation, initiated by the local activation of contact coagulation factors, has been suggested as one possible factor causing glomerular injury in IgA nephritis. The plasma activity of factor XII, prekallikrein and high molecular weight (HMW) kininogen were measured in 24 patients with biopsy-proven IgA nephritis and in 123 normal controls, using an activated partial thromboplastin time assay with the appropriate factor-deficient plasma as substrate. IgA patients had significantly lower plasma activity of factor XII (45.5% +/- 28.3% against 80.7% +/- 31.8%; mean +/- standard deviation, P < 0.001), prekallikrein (37.7% +/- 24.5% against 119.8% +/- 37.7%; P < 0.001) and HMW kininogen (72.8% +/- 37.8% against 119.1% +/- 42.8%; P < 0.001) when compared with controls. In the IgA patients, there was no significant correlation between factor XII, prekallikrein and HMW kininogen activity and 24-hour total urinary protein excretion, suggesting that the reduced plasma activity was not due to increased urinary loss of the coagulation factors. One possible explanation for these results is that the intrinsic coagulation pathway is activated in patients with IgA nephritis.

1431 related Products with: Plasma activity of contact coagulation factors in patients with IgA nephritis.

Contact Factors: Human Fa Contact Factors: Human co Contact Factors: Human co ANTI ACTIVATED X FACTOR A Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri Alkaline Phospatase (ALP) Lipoproteins, Human Plasm Human interleukin 2(IL-2) Human Helicobacter pylori Bovine prolactin-induced ELISA kit CLGI,Collagenas

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