Assertion: serum albumin | /r/HasProperty | hsa
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text: viewerPowerPoint Scheme depicts antioxidant (highlighted in blue) and the pro‐oxidant potential (highlighted in red) of human serum albumin (HSA).
text: Human serum albumin (HSA) is an abundant multifunctional non‐glycosylated, negatively charged plasma protein, with ascribed ligand‐binding and transport properties, antioxidant functions, and enzymatic activities.
text: View more information on Human serum albumin (HSA) is the most abundant protein in human plasma with a molecular weight of 66,437 Da (based on amino acid composition).
text: Human serum albumin (HSA) has unique properties that make it attractive as a nutrient in cell culture media and as an excipient for lyophilized biologic drug formulations and when produced as nanoparticulates for drug delivery.
text: Two types of serum albumin are used in pharmaceutical and biotechnology applications: human serum albumin (HSA) and bovine serum albumin.
text: Human serum albumin (HSA) has a molecular mass of 66,348 Da and is composed of three homologous domains, numbered I, II, and III (Figure 1) (
text: Human serum albumin (HSA) is a protein consisting of 585 amino acids with a molecular mass of 66.7 kDa, is highly water soluble and has a strong negative charge.
text: In this sense, bovine serum albumin (BSA) is well regarded as a favorite template in various MIPs-based biochemical/analytical assays mainly due to its low price, easy availability, and high structural homology to human serum albumin (HSA).
text: The addition of heat-inactivated (hi) fetal calf serum (FCS), 0.5% human serum albumin (HSA), or 0.5% bovine serum albumin (BSA) efficiently prevented NET formation of human neutrophils following stimulation with LPS and CaI, but not after stimulation with PMA.
text: In human experiments, supplements added to culture media typically vary from no supplement to heat inactivated FCS (0.05 to 10% or 0.1 to 10%) and human serum albumin (HSA; 0.05 to 2 %), yet other supplements such as (heat inactivated) human plasma, (heat inactivated) human serum, and BSA can also be found at variable concentration (Supplementary Table 1, Figure 5).
text: NET formation of neutrophils was studied in RPMI 1,640 with 10 mM HEPES (RPMI/HEPES), RPMI/ HEPES + 0.5% human serum albumin (HSA) or + 1% heat inactivated (56°C) fetal calf serum (hiFCS).
text: Media supplements in studies dealing with human neutrophils (460 publications total) ranged from no supplement to FCS (0.05% to 10%), hiFCS (0.1 to 10%), human plasma (HP, 3 to 100%), hiHP (2 to 5%), human serum (HS, 0.2 to 100%), hiHS (0.1 to 100%) and serum albumin (HSA, 0.05 to 2%; BSA, 0.1 to 2%) (Supplementary Table 1).
text: A series of binding studies using radiolabeled PGE, PGE, PGA, and PGFfound that the only plasma protein that significantly binds to the above prostaglandins is human serum albumin (HSA).
text: Human serum albumin (HSA) is either alone or an associative biomarker in several chronic diseases like necrosis, nephrosis, hepatitis, malnutrition, arthritis, immune disorders, cancer, diabetes and in some severe infections.
text: The primary object of the present invention is to provide an electrochemically active and albumin-binding device, for collection and retention of biological samples, for a subsequent quantitative detection of albumin and its complexes, particularly, urine albumin, human serum albumin (HSA), glycated albumin (GA), and methemalbumin (MHA), in biological samples of reduced volume.
text: Another object of the present invention to provide a point-of-care biosensor, adapted to receive the electrochemically-active and albumin binding device, for the detection and quantitative measurement of urine albumin, human serum albumin (HSA), glycated albumin (GA), and methemalbumin (MHA), in biological samples of reduced volume, through a measurement of redox current flowing through the electrochemically active device, on the application of an electric potential.
text: It is also an object of the present invention to provide a method for the detection and quantitative measurement of urine albumin, human serum albumin (HSA), glycated albumin (GA), and methemalbumin (MHA), through an accurate measurement redox current flowing through the electrochemically-active and albumin binding devices.
text: Accordingly, the present invention provides an albumin-binding and an electrochemically active biosensor, for an accurate detection and quantitative measurement of albumin and its complexes such as bioanalytes such as urine albumin, human serum albumin (HSA), glycated albumin (GA), and methemalbumin (MHA), in reduced volumes of biological samples of urine and blood.
text: The device 100 of present invention is used for the detection and quantitative measurement of albumin bioanalytes such as urine albumin, human serum albumin (HSA), glycated albumin (GA) and methemalbumin (MHA), either individually or in combination, in human biological samples.
text: A database member 306 is provided in the housing 301 to store standard values of redox current and bioanalyte concentration of human serum albumin (HSA), glycated albumin (GA), methemalbumin (MA) and urine albumin, present in the biological samples.
text: Accordingly, the bioanalyte that is advantageously selected for its measurement is a globular protein—human serum albumin (HSA), and urine albumin through a measurement of redox current flowing through electrochemically-active devices, on the application of an electric potential.
text: Abstract Human serum albumin (HSA) is widely used in clinical and cell culture applications.
text: Human serum albumin (HSA) is a soluble, globular, and unglycosylated monomeric protein; it functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones, and plays an important role in stabilizing extracellular fluid volume (1).
text: Human serum albumin (HSA) is, with a blood concentration of 35–50 mg/mL, the most abundant plasma protein comprising more than half the amount of proteins in the blood plasma.
text: The serum proteins used for precoating were human serum albumin (HSA), human serum immunoglobulin G (IgG), and fibrinogen.