Allen JP, Litten RZ, Anton RF, Cross GM: Carbohydrate-deficient transferrin as a measure of immoderate drinking: Remaining issues. Alcohol Clin Exp Res 18,799-812 (1994). Anton RF, Moak DH: Carbohydrate-deficient transferrin and -glutamyltransferase as markers of heavy alcohol consumption. Alcohol Clin Exp Res 18/3,747-754 (1994). Anton R, Bean P: Two methods for measuring carbohydrate-deficient transferrin in inpatient alcoholics and healthy controls compared. Clin Chem 40/3,364-368 (1994). Arndt T, Gressner AM, Kropf J: Labordiagnostik und Kontrolle des Alkoholabusus. Med Welt 45,247-257 (1994). Behrens U, Worner TM, Braly LF et al: Carbohydrate-deficient Transferrin, a Marker for Chronic Alcohol Consumption in Different Ethnic Populations. Alcohol Clin Exp Res 12,427-432 (1988). Behrens UJ, Worner TM, Lieber CS: Changes in Carbohydrate-Deficient Transferrin levels after alcohol withdrawal. Alcohol Clin Exp Res 12,539-542 (1988). Bell H, Tallaksen C, Sjahem T, Weberg R et al: Serum ...
Carbohydrate-deficient transferrin (CDT) is a laboratory test used to help detect heavy ethanol consumption. Transferrin is a serum protein that carries iron through the bloodstream to the bone marrow, where red blood cells are manufactured, as well as to the liver and spleen. Structurally, transferrin is a polypeptide with two N-linked polysaccharide chains. These polysaccharide chains are branched with sialic acid residues. Sialic acid is a monosaccharide carbohydrate. Various forms of transferrin exist, with differing levels of sialylation. The most common form is tetrasialotransferrin, with four sialic acid chains. In persons who consume significant quantities of alcohol (usually more than 4 or 5 alcoholic beverages a day for two weeks or more), the proportion of transferrin with zero, one, or two sialic acid chains is increased. These are referred to as carbohydrate-deficient transferrins. These carbohydrate-deficient transferrins can be measured in the bloodstream, and are an important ...
1. According to the Fletcher-Huehns hypothesis there exists a functional difference between the two iron-binding sites of transferrin.. 2. The aim of the study presented was to evaluate this hypothesis in a homogeneous system, with human bone marrow cells and pure human monoferric transferrins A and B.. 3. For this reason normal human bone marrow cells were incubated with human monoferric transferrin. The monoferric transferrins A and B were obtained by selective labelling at different pH of apotransferrin followed by preparative isoelectric focusing in granulated gels. The uptake of iron by the cell suspensions from monoferric transferrins A and B was equal.. 4. In a heterogeneous but more active system for the removal of iron from human transferrin in vitro the two human monoferric transferrins did not show any significant functional differences.. 5. No support for the Fletcher-Huehns hypothesis could be obtained. ...
The paper describes a study of 58 consecutive male soldiers under 30 years old admitted to an alcohol treatment unit in London, and 51 age- and gender-matched controls to compare the efficacy of isoelectric focusing, a non-quantitative measure of carbohydrate deficient transferrin (CDT), with other markers of alcohol misuse. The Severity of Alcohol Dependence Questionnaire, the Michigan Alcohol Screening Test and the CAGE questions were all more sensitive in detecting alcohol misusers than the laboratory markers measured. At standard cut-off levels, the laboratory markers yielded low sensitivities even in those subjects who admitted to drinking over 80 g alcohol daily for at least 3 weeks immediately prior to the study. CDT was the most sensitive (31%), followed by mean cell volume (14%) and gamma glutamyl transferase (11%). The questionnaires and laboratory markers had good specificities.. ...
An increased plasma transferrin level is often seen in patients suffering from iron deficiency anemia, during pregnancy, and with the use of oral contraceptives, reflecting an increase in transferrin protein expression. When plasma transferrin levels rise, there is a reciprocal decrease in percent transferrin iron saturation, and a corresponding increase in total iron binding capacity in iron deficient states[14] A decreased plasma transferrin can occur in iron overload diseases and protein malnutrition. An absence of transferrin results from a rare genetic disorder known as atransferrinemia, a condition characterized by anemia and hemosiderosis in the heart and liver that leads to heart failure and many other complications. Transferrin and its receptor have been shown to diminish tumour cells when the receptor is used to attract antibodies.[9] ...
The single-banding components of bovine transferrin from animals homozygous for the four transferrin variants found in the U.K. were isolated. Sedimentation equilibrium ultracentrifugation and sodium dodecyl sulphate-polyacrylamide-gel electrophoresis showed that the bands of a single variant have molecular weights of 77500 and 73300 respectively. The different bands of a single variant and single bands of different variants show no evidence of size heterogeneity or of low-molecular-weight peptides being split off after reduction in 6m-guanidine hydrochloride. The two slower bands of a single variant, which both contain 2 molecules of sialic acid/molecule of protein, have the same molecular weight and amino acid composition, and give identical peptide maps, although differences in composition and peptide maps occur between the different variants. The results support the concept that bovine transferrin is essentially a single polypeptide chain, but they do not explain differences in ...
Abstract. The relationship between plasma iron, transferrin saturation, and plasma iron turnover was studied in 53 normal subjects whose transferrin saturation
CDT blood testing can be used to screen for alcohol abuse (heavy alcohol consumption). The protein transferrin carries iron to parts of the body, heavy consumption of alcohol can increase transferrin. High CDT levels can reduce if alcohol consumption is lowered and will generally return to normal after time. This priva
Transferrin receptor 2 (TfR2) is a homolog of transferrin receptor 1 (TfR1), the receptor responsible for the uptake of iron-loaded transferrin (holo-Tf) into cells.The half-life of the chimera increased 2.7-fold in cells exposed to Human Holo Transferrin holo-Tf like the endogenous TfR2 in HepG2 cells. Like TfR2 and unlike TfR1, the levels of the chimera did not respond to intracellular iron content. These results suggest that although holo-Tf binding to the ectodomain is necessary, the cytoplasmic domain of TfR2 is largely responsible for its stabilization by holo-Tf ...
The effect of iron on the exocytosis of transferrin by K562 cells was studied by first allowing the cells to endocytose apotransferrin or diferric transferrin. Subsequent release of the apotransferrin was very rapid with a t 1/2 of 3.01 min, compared with 5.5 min for diferric transferrin. Release of apotransferrin was slowed by the weak base methylamine, t 1/2 8.0 min, but the effect of this agent was substantially greater when iron-transferrin was used, t 1/2 18.65 min, suggesting that methylamine affects both iron removal and receptor recycling. Release of iron-transferrin could be accelerated to a rate comparable with that of apotransferrin by addition of the permeant iron-chelator desferrioxamine. The difference in the rates of release of different forms of the protein could be explained by the re-endocytosis of the iron-rich protein, a process detected by the accelerated release of transferrin when the cells were washed in medium at pH 5.5 containing an iron-chelator or treated with a ...
Apo Transferrin vs Human transferrin - posted in Cell Biology Products: Greetings, What is the difference between apo-transferrin and human transferrin? I got their definition of apo-transferrin is free from iron binding while transferrin based on Sigma product is already half-saturated with iron. Once saturated with iron, i.e forming holo-transferrin it will bring iron into cell by receptor binding of the cell. I am confused why Sigma need to have two different products which in th...
Mycobacterium tuberculosis (M.tb), which requires iron for survival, acquires this element by synthesizing iron-binding molecules known as siderophores and by recruiting a host iron-transport protein, transferrin, to the phagosome. The siderophores extract iron from transferrin and transport it into the bacterium. Here we describe an additional mechanism for iron acquisition, consisting of an M.tb protein that drives transport of human holo-transferrin into M.tb cells. The pathogenic strain M.tb H37Rv expresses several proteins that can bind human holo-transferrin. One of these proteins is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH, Rv1436), which is present on the surface of M.tb and its relative Mycobacterium smegmatis. Overexpression of GAPDH results in increased transferrin binding to M.tb cells and iron uptake. Human transferrin is internalized across the mycobacterial cell wall in a GAPDH-dependent manner within infected macrophages ...
Transferrin is a glycoprotein with a molecular weight of approximately 80 kd. Its single polypeptide chain is formed into two lobes and it is able to bind two ferric (Fe III) ions per protein molecule. Horse serum transferrin, like the transferrins of most vertebrate species, exhibits extensive genetic polymorphism. Transferrin is one of several protein systems used for blood-typing horses. During routine blood typing a new band (designated*) was found. This variant originated from a thoroughbred stallion which was of considerable value as a sire and so it was of interest to characterize this new transferrin variant. Thoroughbred horses carry genes for only six of the fourteen known transferrin isoforms; D, Fl, F2, H2, 0 and R. The aim of this project was to characterize, by classical amino acid sequence analysis, the transferrin variant and the parental variants D and Fl, from one of which must have arisen. All three variant forms (D, Fl and*) were purified. Tryptic digests of the variants were ...
The complexation of Cm(iii) with human serum transferrin was investigated in a pH range from 3.5 to 11.0 using time-resolved laser fluorescence spectroscopy (TRLFS). At pH [greater-than-or-equal] 7.4 Cm(iii) is incorporated at the Fe(iii) binding site of transferrin whereas at lower pH a partially bound Cm(iii) transferrin species is formed. At physiological temperature (310 K) at pH 7.4{,} about 70% of the partially bound and 30% of the incorporated Cm(iii) transferrin species are present in solution. The Cm(iii) results obtained by TRLFS are in very good agreement with Am(iii) EXAFS results{,} confirming the incorporation of Am(iii) at the Fe(iii) binding site at pH 8.5 ...
Hi Ashley, I am not an expert on transferrin, but I hope I can answer your question to your satisfaction. Ferric iron (Fe3+) is found under conditions of neutral or alkaline pH, while ferrous iron (Fe2+) is found under acidic pH. This in itself would suggest that transferrin would mostly only come into contact with ferric iron in the body. Anyway, transferrin binds to a number of different metals, but its highest affinity is for ferric iron. It does not bind at all to ferrous iron. This would explain the colour change / absorbance when mixed with Fe3+, but no change when transferrin is mixed with Fe2+. In terms of the bicarbonate versus carbonate question, I can see the problem, because a lot of people are lazy and do not distinguish between the two. I looked up a research article that definitively said that transferrin binds to bicarbonate (aka hydrogen carbonate) but not carbonate. Hope this helps! - Karin ...
UNC-51 overexpression can inhibit the transferrin endocytosis in the transfected COS-7 cells. We think that this inhibition of transferrin endocytosis should be caused by UNC-51-dependent...
TY - JOUR. T1 - Guinea pig and human red cell hemolysates release iron from transferrin. AU - Pollack, Simeon. AU - Weaver, J.. PY - 1985. Y1 - 1985. N2 - Despite a binding constant of 1022 L/mol-1, iron is released from transferrin in the reticulocyte. The mechanism of this release is unclear. It has been suggested that iron is released from transferrin in endocytic vesicles that have been acidified. But the carboxy-terminal iron in transferrin is acid stable at the pH apparently achieved in the endocytic vesicle, and is, nevertheless, released. We found that red cell hemolysates, at neutral pH, will release iron from transferrin. With molecular sieve chromatography, the activity is seen to consist of high and low molecular weight components. The activity of both components is susceptible to destruction by phosphatases. The releasing activity of hemolysates can account for about 25% of the iron uptake of a reticulocyte at pH 7; at pH 5.5 (the purported pH of the endocytic vesicle), the ...
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Buy our Natural Human Transferrin protein. Ab91435 is a full length protein produced in Nativesyntheticaly and has been validated in WB, SDS-PAGE. Abcam…
TY - JOUR. T1 - Transferrin and the transferrin receptor for the targeted delivery of therapeutic agents to the brain and cancer cells. AU - Dufès, Christine. AU - Al Robaian, Majed. AU - Somani, Sukrut. PY - 2013/5/7. Y1 - 2013/5/7. N2 - The potential use of many promising novel drugs is limited by their inability to specifically reach their site of action after intravenous administration, without secondary effects on healthy tissues. In order to remediate this problem, the protein transferrin (Tf) has been extensively studied as a targeting molecule for the transport of drug and gene delivery systems to the brain and cancer cells. A wide range of delivery approaches have been developed to target the Tf receptor and they have already improved the specific delivery of Tf-bearing therapeutic agents to their site of action. This review provides a summary of the numerous delivery strategies used to target the Tf receptor and focuses on recent therapeutic advances.. AB - The potential use of many ...
Hereditary hemochromatosis (HH) is a prevalent genetic disorder that results in the daily excess absorption of dietary iron. If untreated this disease leads to systemic organ failure and death. HH is caused by mutations to the gene coding for a protein called HFE, a type I transmembrane glycoprotein with a demonstrated role in regulating cellular iron homeostasis. HFE binds to the cell-surface receptor transferrin receptor (TfR), a dimeric type II transmembrane glycoprotein responsible for iron uptake into most mammalian cell types. TfR binds iron-loaded transferrin (Fe-Tf) from the blood and transports it to acidic recycling endosomes where iron is released from Fe-Tf in a TfR-facilitated process. Iron-free transferrin (apo-Tf) remains bound to TfR and is recycled to the cell surface, where apo-Tf rapidly dissociates from TfR upon exposure to the basic pH of blood. HFE and Fe-Tf can bind simultaneously to TfR to form a ternary complex, but HFE binding to TfR lowers the apparent affinity of the ...
We sought to examine the relationship between elevated transferrin saturation (TS) and measures of health status (telomere length and patient-reported health-related quality of life) to assess whether elevated TS is associated with negative patient outcomes beyond increased risk for morbidity and mortality, using a cross-sectional analysis of the Hemochromatosis and Iron Overload Screening Study supplemented with assays for leukocyte telomere length in adults ≥25 years old (n = 669). Among individuals with elevated TS (≥45 % for women and ≥50 % for men), who also had a usual source of care, only 5.2 % reported ever being told by a doctor that they had an elevated iron condition. In a fully adjusted general linear regression model controlling for demographic characteristics as well as health conditions associated with iron overload, elevated TS versus non-elevated TS was associated with worse general health status (60.4 vs. 63.8, P , 0.05), mental health status (76.5 vs. 82.2, P , 0.0001) ...
Background and Methods The involvement of iron in the risk for, and complications of, type 2 diabetes has generated substantial interest over the past 15 years, initially sparked by an association with raised serum ferritin, and the observation that people with iron overload diseases frequently develop diabetes. Considerable advances have since been made in understanding the effect glucose has on molecules, cells, and tissues; and the role that oxidative stress plays in the development of the pathologies of long-term diabetes. Poorly liganded iron is potentially both a contributor to, and consequence of, these complications. In vitro experiments with glucose-incubated transferrin by earlier workers have demonstrated loss of function with increasing glycation, leading to the suggestion that the failure of this key iron-binding protein may contribute to diabetic pathology, via the presence of redox active non-transferrin-bound iron (NTBI). In vitro glycated transferrin is examined here by ...
Test results may vary depending on your age, gender, health history, the method used for the test, and other things. Your test results may not mean you have a problem. Ask your healthcare provider what your test results mean for you. Results are given in milligrams per deciliter (mg/dL). The normal range for transferrin is 170 to 370 mg/dl. If you have a higher amount, you may have iron-deficiency anemia. If you have a lower level, you may have another problem, such as liver disease and hemolytic anemia. Transferrin may also be measured using a value called total iron-binding capacity (TIBC). Results are given in micrograms per deciliter (mcg/dL). Normal values are 300 to 360 mcg/dL. A higher level means that you may have iron-deficiency anemia. Another measurement, called transferrin saturation, checks how many places on your transferrin that can hold iron are actually doing so. Normal values are 20% to 50%. In severe cases of iron-deficiency and anemia, this number may fall below 10%. Many ...
The transferrin receptor is a type II transmembrane protein. It is a homo-dimer consisting of two identical monomers joined by two disulfide bindings at cystein residues 89 and 92 in the extracellular domain just outside the cell membrane (Jing and Trowbridge 1987). The monomer is a glycoprotein with molecular mass 90 kDa consisting of 780 amino residues. The protein have three domains: one 61-residue amino-terminal cytoplasmic region, a 28-residue transmembrane region and a 671-residue extracellular carboxyl-terminus (McClelland et al 1984, Schneider et al 1984). Each ectodomain can bind one molecule of transferrin and thus the transferrin receptor can bind two molecules of transferrin carrying in total four Fe3+. The ectodomain consists of three regions, each contributing to and critical for the transferrin binding (Lawrence et al 1999). The structure of the ectodomain has striking similarities to the membranebound carboxy peptidase II (Lawrence et al 1999), suggesting that they have evolved ...
Busch, B., 1969: Studies on serum transferrin types of German Black Pied cattle (DDR). 3. Relationships between serum transferrin types and milk performance traits
As a screening test for iron deficiency or chronic total-body iron overload (such as hemochromatosis), an overnight fasting sample is best. If checking for acute iron poisoning, a diagnostic baseline sample taken at any time prior to treatment is optimal. Screening programs to detect iron overload much more frequently identify cases of iron deficiency (low iron)...a situation which demands diagnostic work up without any undue delay (there may be a serious & manageable reason)! An iron profile screen for serum iron and total iron-binding capacity (TIBC...STS serum transferrin saturation) gives a result that reflects the percentage iron saturation of the iron-binding sites on the transferrin protein (iron carrier protein). A percentage saturation ,55% is cause to look further for iron overload. This is a much more specific screening test than serum ferritin (many other causes of elevated ferritin especially are a non-fasting sample & also other liver disease, inflammation, recent multiple ...
transferrin - MedHelps transferrin Center for Information, Symptoms, Resources, Treatments and Tools for transferrin. Find transferrin information, treatments for transferrin and transferrin symptoms.
|strong|Sheep anti Human transferrin antibody|/strong| recognizes human transferrin, also known as beta-1 metal-binding globulin siderophilin or serotransferrin. Transferrin is 647 amino acid ~7…
Product is the lyophilized powder of human transferrin and buffer salts. ransferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains. The N-terminal and C-terminal domains of this protein are globular moieties of about 330 amino acids. Each of these domains is divided into two sub-domains, with the iron- and anion-binding sites found within the intersubdomain cleft. The binding cleft opens with iron release and closes with iron binding. Transferrin binds iron with an association constant of approximately 1022 M-1. Ferric iron couples to transferrin only in the presence of an anion (usually carbonate) that serves as a bridging ligand between metal and protein, excluding water from the two coordination sites. Without the anion cofactor, iron binding to transferrin is negligible. In the presence of anions, ferric transferrin is resistant to all but the most potent chelators. The remaining four coordination sites are provided by the transferrin protein - a histidine ...
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Study finds extreme levels of Transferrin Saturation Ratio reflecting blood iron levels linked to increased risk of death. A new study led by researchers at the Graduate Entry Medical School (GEMS), University of Limerick (UL) has found that people with low levels and very high levels of a commonly measured laboratory test, the "transferrin saturation ratio" are at an increased risk of death. The test is a measure of the amount of available iron in the bloodstream with low levels generally reflecting a state of iron deficiency and high levels suggesting a relative excess.. The study found that subjects with extremely low transferrin saturation levels (less that 17.5%) were at a 45% higher risk of death. On the other hand, the risk of death was also significantly higher for subjects with very high levels of transferrin saturation above 31.3 %.. According to primary author, Professor Austin Stack, Foundation Chair of Medicine at University of Limerick Graduate Entry Medical School, and Consultant ...
Abstract. Objective. To evaluate whether levels of iron status markers (haemoglobin, serum transferrin saturation, serum ferritin) in pregnant women, measured in the beginning of the second trimester, could be used to predict levels later in pregnancy, pre partum and post partum.. Design. Randomized, double-blind, placebo-controlled parallel study.. Setting. The Birth Clinic at the Department of Obstetrics, Herning Hospital, Herning, Denmark.. Subjects. One hundred and twenty healthy pregnant women between 14 and 18 weeks of gestation.. Interventions. Sixty-three women were allocated to treatment with tablets containing 66 mg ferrous iron (as fumarate) daily, and 57 women to treatment with placebo.. Main outcome measures. Haemoglobin, serum transferrin saturation, and serum ferritin were measured every 4th week during gestation, prior to delivery, and 1 and 8 weeks post partum.. Results. Correlation matrices during pregnancy and post partum were calculated for each iron status marker separately ...
Transferrin (Tf) is a multifunctional, iron binding protein found in both vertebrates and invertebrates. Although transferrin has been suggested to play a role in innate immunity, its immunological function during infection has not been characterized. In this study, we identified and characterized Bombyx mori transferrin (BmTf). The promoter region of BmTf has numerous putative NF-κB binding sites, suggesting its possible function in innate immunity. Analysis of BmTf gene expression shows that it is highly inducible in response to a wide variety of pathogens including bacteria, fungus, and viruses. Recombinant BmTf protein produced in a baculovirus system exhibits iron binding capacity and antibacterial activity against various Gram-positive and -negative bacteria. Taken together, our results indicate that BmTf is an inducible immune effector molecule that may play an important role in pathogen clearance of insect innate immunity. © 2009 Elsevier Ltd. All rights reserved ...
Transferrin: The Iron Carrier , Transferrin: The Iron Carrier , کتابخانه دیجیتال دانشگاه علوم پزشکی اصفهان
The cardiomyopathy of idiopathic or acquired haemochromatosis suggests that the heart may be especially sensitive to toxic effects of excess iron (Sullivan 1990). The features of inherited iron overload include cardiac problems (arrhythmias and heart failure), and/or cirrhosis of the liver, diabetes, arthritis and skin pigmentation. Since haemochromatosis can be easily treated by phlebotomy once diagnosed, this condition is considered a preventable form of heart disease amongst other equally important health risks. Not only homozygosity for the HFE C282Y mutation, but also the heterozygous state is associated with increased serum iron parameters (Rossi et al. 2001). Individuals with serum transferrin saturation levels above 55% carry an increased all-cause mortality risk especially when combined with high red meat intake (Mainous et al. 2004a,b). Coronary heart disease rates rise sharply from age 20 onwards in males, who begin accumulating excess iron from late adolescence. Healthy women, on the ...
Transferrin is a single polypeptide chain glycoprotein belonging to iron binding family of proteins. It has a molecular weight of 81,5 kDa (porcine). It is synthesised in the liver and consists of two domains each having a high affinity reversible binding site for Fe3+. The iron is transported in blood and interstitial fluids to sites of use and disposal. Iron/transferrin is essential in haemoglobin synthesis and for certain types of cell division. Serum concentration rises in iron deficiency and pregnancy and falls in iron overload, infection and inflammatory conditions ...
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We read with great interest the article by Park et al. (1) in Diabetes Care. The results they report in middle-aged Korean men are very similar to ours published in 2007 in Diabetes Care for both sexes from the DESIR (Data from an Epidemiological Study on the Insulin Resistance Syndrome) prospective study in a Caucasian population (2). In our article, we showed that high baseline ferritin levels (above the higher tertile) were associated with a higher risk of incident International Diabetes Federation-defined metabolic syndrome in men and in menopausal women over a 6-year follow-up. Moreover, we found that high transferrin levels were also associated with this risk, either alone or in combination with ferritin. The parameters most consistently associated with baseline ferritin and transferrin were triglyceride and insulin levels. In another article (3), we described an association of both ferritin and transferrin with an increase in glucose levels during a 3-year follow-up in DESIR.. The results ...
the control group. All the examinees had their blood sampled intravenously in order for full blood count results and parameters of iron metabolism to be determined. Also, ELISA method was used for establishing the level of hepcidin in the serum. The research showed that the concentration of hepticin is statistically lower in children and adolescents who suffer from iron deficiency anemia in comparison with children and adolescents who do not have this condition. The positive correlation between the level of serum hepcidin and iron in the serum, ferritin, the medium volume of erythrocytes and transferrin saturation was confirmed but the negative one occurred in the level of the serum hepcidin, transferrin and reticulocyte. Transferrin and the unsaturated capacity of iron binding, the total capacity of iron binding and reticulocytes are in a positive correlation but the correlation of transferrin with the parameters of transferrin saturation, iron and hemoglobin is negative. The sex and the age of ...
Abcams Transferrin ELISA Kit (ab108902) suitable for Cell culture supernatant, Saliva, Milk in human. Reliably quantify 1 ng/ml of Transferrin.
Sheep polyclonal antibody conjugated to HRP in a protein matrix preservative. Component in the Bovine Transferrin ELISA Kit (F120), 12mL....
title: The Relationship of Initial Transferrin Saturation to Cardiovascular Parameters and Outcomes in Patients Initiating Dialysis, doi: 10.1371/journal.pone.0087231, category: Article
Describes how the TIBC, UIBC, and transferrin tests are used, when TIBC, UIBC, and transferrin tests are requested, and what the results of these tests might mean
Describes how the TIBC, UIBC, and transferrin tests are used, when TIBC, UIBC, and transferrin tests are requested, and what the results of these tests might mean
A wide range of metals are transported in the body by the protein transferrin, including both essential metal ions and probably also metals used in therapeutic agents. The metal binding sites on transferrin contain tyrosine, histidine and aspartate ligands. This thesis is concerned with studies of the essential metal ion manganese, and with titanium, which is used in anticancer agents. In order to aid the characterisation of Mn(III) and Ti(IV) transferrins, the Mn(III) and Ti(IV) complexes with the model ligand ethylenebis[(a-hydroxyphenyl)glycine](H₄EHPG) have been studied. The Mn(III) complexes rac-Na[Mn(EHPG)].3H₂0 (1) and rac,mesoNa[Mn(EHPG)].H₂0 (2), have been prepared and their X-ray crystal structures determined. Complex 1 contains N(S,S)C(R,R) configurations at the N and C stereogenic centres, whilst in the unit cell of complex 2 there are two independent molecules, 2a (mesa) and 2b (rac), with N(R,R)C(S,R) and N(R,R)C(S,S) configurations, respectively. Enantiomers of each complex ...
Introduction: Transferrin is the main protein in the blood that binds to iron and transports it throughout the body. A transferrin test directly measures the level in the blood. Function: Iron is supplied by the diet. About 10% of the ingested iron is absorbed in the small intestine and transported to the plasma. There the iron is…
This test measures the amount of the protein transferrin in your blood. Levels of tranferrin tell your healthcare provider about the iron supply in your body.
Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins - diagram, schematic, and image 71 ...
AMHERST, Mass. - In recent years cancer researchers, particularly brain tumor specialists, have pinned some hope for delivering anti-tumor drugs on transferrin, a protein that carries the essential element iron into cells. This is because unlike most other proteins, transferrin can cross the blood-brain barrier. But a new study of transferrin and its receptor by chemists at the University of Massachusetts Amherst reveals that transferrin isnt as open to drug loading as hoped, so creating a good delivery system may be more challenging than previously thought. ...