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Serum Albumin, Human

Serum Albumin, Human is a major plasma protein that serves as a transport and regulatory molecule in the body.
It is synthesized in the liver and plays a crucial role in maintaining oncotic pressure, transporting various substances, and supporting metabolic processes.
Serum Albumin, Human is commonly used in medical research and clinical settings to study physiological and pathological conditions, and its levels can provide insights into a patient's overall health status.
Researchers often utilize Serum Albumin, Human in experiments to investigate its interactions, functions, and potential therapeutic applications.

Most cited protocols related to «Serum Albumin, Human»

Prior to the experiments, HEPES-buffered Ringer’s solution (in some cases EBM-2 medium) was added to empty wells of a 12-well plate (Costar). Filter inserts, containing confluent monolayers of CD34+-ECs, were subsequently placed in the 12-well plate, filled with compound solution containing the fluorescent integrity marker Lucifer Yellow (20 µM; Life Technologies), and then placed on an orbital shaker. After 1 h, filter inserts were withdrawn from the receiver compartment. Aliquots from the donor solution were taken at the beginning and at the end of the experiments and the fluorescence was quantified. At least three inserts with cells and three without cells were tested in each permeability measurement. Fluorescence detection was carried out on a Synergy H1 multiplates reader (Biotek) using the following excitation/emission wavelength (nm) settings: 432/538; 490/516; 542/570 for Lucifer yellow, Fluorescein Na and Cy3-Human Serum Albumin and Human IgG respectively.
To obtain a concentration-independent transport parameter, the clearance principle was used. The increment in cleared volume was calculated by dividing the amount of compound in the receiver compartment by the drug concentration in the donor compartment [7] (link). The volume cleared was plotted versus time and the slope estimated by linear regression analysis. The slope of the clearance curve with inserts alone and inserts with cells is equal to PSf and PSt, respectively, where PS (microliters/minute) is the permeability surface area (square centimeter) product. The PS-value for endothelial monolayer (PSe) was calculated. To generate the endothelial permeability coefficient, Pe (cm/min), the PSe value was divided by the surface area of the filter (A in cm2) insert using the following equation: Pe = [1/PSt−1/PSf]−1/A. To assess possible adsorption to plastics and non-specific binding to cells, the mass balance (%) was calculated from the amount of compound recovered in both compartments at the end of the experiment divided by the total amount added in the donor compartment at time zero. For Pe determination, mass balance value should be between 80% and 120%.
Publication 2014
Adsorption Cells Endothelium Fluorescein Fluorescence HEPES Homo sapiens lucifer yellow Permeability Pharmaceutical Preparations Ringer's Solution Serum Albumin, Human Tissue Donors
Baseline blood samples were frozen at −80°C and stored for later analysis. 25(OH)D, serum calcium, albumin, and levels of parathyroid hormone (PTH) were measured in the Massachusetts General Hospital (MGH) clinical laboratories. 25(OH)D2 and 25(OH)D3 levels were measured by liquid chromatography–tandem mass spectrometry (LC-MS), with interassay coefficients of variation (CVs) of 9.1% for 25(OH)D2 and 8.6% for 25(OH)D3. Total 25(OH)D level was calculated as the sum of 25(OH)D2 level and 25(OH)D3 level. Intact PTH was measured by electrochemiluminescense immunoassay on the Cobas E160 automated analyzer (Roche Diagnostics, Indianapolis, IN, USA). The interassay CV for intact PTH measurement was 4.2%. Calcium and albumin levels were measured by dye-based photometric assays on an automated analyzer.
DBP was measured in duplicate by commercial enzyme-linked immunosorbent assay (ELISA; Cat. No. DVDBP0, R&D Systems, Minneapolis, MN, USA) according to the manufacturer's instructions. The assay was conducted after diluting serum samples 1:2000 in Calibrator Diluent RD6-11 (Part No. 895489, R&D Systems). The interassay CV was 8.5% at a concentration of 40 µg/mL. The assay recovered between 93% and 110% of a 100- to 200-µg/mL dose of exogenous DBP added to human serum samples containing between 25 and 200 µg/mL of endogenous DBP. The manufacturer reports no significant cross-reactivity with human albumin, vitamin D3, or α-fetoprotein.
In a subset of patients in whom adequate serum was available (n = 45), total 1,25(OH)2D3 was measured by LC-MS/MS in the Mayo Clinic Medical Laboratories (Rochester, MN, USA).
Publication 2011
Albumins alpha-Fetoproteins Biological Assay BLOOD Calcifediol Calcium Cholecalciferol Clinical Laboratory Services Cross Reactions Diagnosis Enzyme-Linked Immunosorbent Assay Freezing Homo sapiens Immunoassay Liquid Chromatography Parathyroid Hormone Patients Photometry Serum Serum Albumin, Human Tandem Mass Spectrometry
The previously prepared 1,008 low energy 3D chemical structures in the AfroDb library were saved in.mol2 format and initially treated with LigPrep [63] , distributed by Schrodinger Inc. This implementation was carried out with the graphical user interface (GUI) of the Maestro software package [64] , using the OPLS forcefield [65] (link)–[67] (link). Protonation states at biologically relevant pH were correctly assigned (group I metals in simple salts were disconnected, strong acids were deprotonated, strong bases protonated, while topological duplicates and explicit hydrogens were added). A set of ADMET-related properties (a total of 46 molecular descriptors) were calculated by using the QikProp program [68] running in normal mode. QikProp generates physically relevant descriptors, and uses them to perform ADMET predictions. An overall ADME-compliance score – drug-likeness parameter (indicated by #stars), was used to assess the pharmacokinetic profiles of the compounds within the AfroDb library. The #stars parameter indicates the number of property descriptors computed by QikProp that fall outside the optimum range of values for 95% of known drugs. The methods implemented were developed by Jorgensen et al. [69] (link)–[70] and among the calculated descriptors are: the total solvent-accessible molecular surface, in Å2 (probe radius 1.4 Å) (range for 95% of drugs: 300–1000 Å2); the hydrophobic portion of the solvent-accessible molecular surface, in Å2 (probe radius 1.4 Å) (range for 95% of drugs: 0–750 Å2); the total volume of molecule enclosed by solvent-accessible molecular surface, in Å3 (probe radius 1.4 Å) (range for 95% of drugs: 500–2000 Å3); the logarithm of aqueous solubility, (range for 95% of drugs: −6.0 to 0.5) [69] (link), [71] (link); the logarithm of predicted binding constant to human serum albumin, (range for 95% of drugs: −1.5 to 1.2) [72] (link); the logarithm of predicted blood/brain barrier partition coefficient, logB/B (range for 95% of drugs: −3.0 to 1.0) [73] (link)–[75] (link); the predicted apparent Caco-2 cell membrane permeability (BIPcaco-2) in Boehringer–Ingelheim scale, in nm/s (range for 95% of drugs: <5 low, >100 high) [76] (link)–[78] (link); the predicted apparent Madin-Darby canine kidney (MDCK) cell permeability in nm s−1 (<25 poor, >500 great) [77] (link); the index of cohesion interaction in solids, Indcoh, calculated from the HBA, HBD and the surface area accessible to the solvent, SASA ( ) by the relation Indcoh = HBA HBD1/2/ (0.0 to 0.05 for 95% of drugs) [71] (link); the globularity descriptor, Glob =  , where r is the radius of the sphere whose volume is equal to the molecular volume (0.75 to 0.95 for 95% of drugs); the predicted polarizability, (13.0 to 70.0 for 95% of drugs); the predicted logarithm of IC50 value for blockage of HERG K+ channels, logHERG (concern<−5) [79] (link)–[80] (link); the predicted skin permeability, (−8.0 to −1.0 for 95% of drugs) [81] (link)–[82] (link); and the number of likely metabolic reactions, #metab (range for 95% of drugs: 1–8).
Publication 2013
Acids ADMET Blood-Brain Barrier cDNA Library Cell Membrane Permeability Hydrogen Madin Darby Canine Kidney Cells Metals Permeability Pharmaceutical Preparations Radius Salts Sasa Serum Albumin, Human Skin Solvents Stars, Celestial
Initially, 2.5 × 109 induced yeast for the first round and 1.4 – 5 × 107 induced yeast for subsequent rounds were washed and resuspended in buffer (20 mM HEPES pH 7.5, 150 mM sodium chloride, 0.1% (w/v) ovalbumin, 1 mM EDTA) and then incubated with anti-Alexa Fluor 647 or anti-FITC microbeads (Miltenyi) at 4 °C for 30 min. Each round of MACS selection began with a pre-clear step which involved passing the yeast, through an LD column (Miltenyi) to remove yeast expressing nanobodies that bound nonspecifically to magnetic beads. After pre-clearing, human serum albumin (HSA) binding nanobodies were enriched over four rounds of MACS selection by staining the yeast alternately with Alexa Fluor 647 or FITC labeled HSA (Sigma) and microbeads, then passing them through an LS column (Miltenyi). During these four selection rounds, yeast were stained with successively lower concentrations of HSA: 1 μM, 250 nM, 75 nM,and 15 nM, in order to enrich for binders with higher affinities. After MACS selection, yeast were plated as single colonies which were picked and grown as clonal populations in a 96 well plate. Following galactose induction of nanobodies, yeast were stained with Alexa Fluor 488 labeled HSA and analyzed by flow cytometry with an Accuri C6 (BD Biosciences) to screen for nanobody binders.
Publication 2018
alexa fluor 488 Alexa Fluor 647 Buffers Clone Cells Edetic Acid Flow Cytometry Fluorescein-5-isothiocyanate Galactose HEPES Microspheres Ovalbumin Population Group Serum Albumin, Human Sodium Chloride VHH Immunoglobulin Fragments Yeast, Dried
The study was approved by the local ethics committee (Bayerische Landesärztekammer, Munich) and subjects gave written, informed consent. Monocytes were enriched from whole blood by negative selection using the Rosette Sep® monocyte enrichment cocktail (STEMCELL Technologies) according to the manufacturer's instructions. Briefly, blood from healthy donors was collected in Falcon tubes containing EDTA at 2 mM final concentration and incubated with enrichment antibody cocktail (50 µl per ml of whole blood) at room temperature for 20 minutes. Cells were then separated by density gradient using Ficoll-Paque™ PLUS (GE Healthcare). Platelets present in the enriched monocyte fraction were discarded by 3 washing steps in PBS, 2% FBS. Finally, monocytes were seeded in either XVivo 10 (Cambrex) or RPMI 10% FBS, 4 mM L-Glutamine with Pen/Strep at a concentration of 5×105 cells/ml in 12-well tissue culture treated plates for 6 days in the presence of either 100 ng/ml rHuGM-CSF (M1) or 100 ng/ml rHuM-CSF (M2). For M2a and M2c polarization, monocytes were incubated in XVivo 10 with rHuM-CSF and 10 ng/ml rHuIL-4 or 10 ng/ml rHuIL-10, respectively. For M1 activation, monocytes were first incubated with rHuM-CSF or rHuGM-CSF for 3 days followed by stimulation with 10 ng/ml LPS and 50 ng/ml rHuIFN-γ for 3 additional days. As indicated by the manufacturer, XVivo 10 media contains human albumin, recombinant human insulin, and human transferrin. It does not contain any exogenous growth factors, artificial stimulators of cellular proliferation, undefined supplements, or protein kinase C stimulators.
Changes in cell morphology were assessed by phase contrast microscopy (Axiovert 135, Zeiss). Phenotypical and functional characterization of MDM was performed after 6 days.
Publication 2012
BLOOD Blood Platelets Cell Proliferation Cells Combined Antibody Therapeutics Dietary Supplements Donor, Blood Edetic Acid Ficoll Glutamine Growth Factor Homo sapiens Insulin Microscopy, Phase-Contrast Monocytes Protein Kinase C Regional Ethics Committees Serum Albumin, Human Stem Cells Streptococcal Infections Tissues Transferrin

Most recents protocols related to «Serum Albumin, Human»

Example 7

Synthetic urine is prepared by dissolving 14.1 g of NaCl, 2.8 g KCl, 17.3 g of urea, 19 ml ammonia water (25%), 0.60 g CaCl2 and 0.43 g MgSO4 in 0.02 mole/L of HCl. The final pH of synthetic urine is adjusted to 6.04 by using HCl and ammonia water.

40 mg Sigma creatinine is dissolved in 10 ml of synthetic urine solution. 3 mg of human albumin is dissolved in 10 ml of synthetic urine solution to prepare the micro albumin solution.

4 mg Sigma hemin is dissolved in 20 ml of synthetic urine, 20 μL Hemin solution is used as a receptor for urine albumin detection at different creatinine concentration.

A desired volume of the biological sample (synthetic urine) is taken and dispensed on the electrode of the biosensor device and the corresponding cyclic voltammogram is obtained by the CHI-Electrochemical workstation using the potential window, that varies from 0 V to −1 V with scan rate of 0.1 V/sec.

The albumin content in the urine sample binds hemin thereby demonstrates a linear decrease in peak redox current with urine albumin concentration as shown in FIG. 15(a) for different creatinine concentrations. If the concentration of albumin in urine sample is increased, then the albumin increasingly binds with hemin thereby reducing the free hemin concentration on the electrode resulting in the decrease in peak redox current of free hemin. FIG. 16 shows the urine albumin concentrations, urine creatinine concentrations and calculated ACR for different samples.

The values of concentrations of the urine albumin (mg/L) and creatinine for different samples is shown in Table 4.

TABLE 4
SampleUrine albuminUrine CreatinineACR
Number(mg/L)(mg/dL)(mg/g)
1526.719
22026.775
35026.7187
410026.7375
515026.7562
65133.34
720133.315
850133.338
9100133.375
10150133.3113

Patent 2024
Albumins Ammonium Hydroxide Biopharmaceuticals Biosensors Creatinine Hemin Moles Oxidation-Reduction Radionuclide Imaging Receptors, Albumin Serum Albumin, Human Sodium Chloride Sulfate, Magnesium Urea Urine
ELISAs were performed as previously described7 . Briefly, 96-well MaxiSorp plates (Thermo Scientific #442404) were coated with 200 ng of recombinant IL-1RA protein (Biolegend #553906) in PBS and incubated overnight at 4 C. Plates were dumped out and incubated with 2% Human Serum Albumin (HSA) (Celprogen #HSA2001-25-2) in PBS for 2 h at RT. Plates were washed 3× with 200 μl wash buffer (PBS 0.05% Tween). Samples were diluted in 2% HSA and added to the plate to incubate for 2 h at RT. Mouse anti-human IL-1RA (Prospec #ant-238) was used as a positive control. Plates were washed 6× with wash buffer. Goat anti-human IgG Fc (Sigma Aldrich, #AP113P) diluted 1:10000 in 2% HSA was added to the plates and incubated for 1 h at RT. For the positive control, 1:5000 Goat anti-mouse IgG Fc (Thermo Fisher Scientific, #A16088) in 2% HSA was used. Plates were washed 6x. Plates were developed with 100 μl of TMB Substrate Reagent Set (BD Biosciences #555214) and the reaction was stopped after 5 min by the addition of 2 N sulfuric acid. Plates were then read at a wavelength of 450 nm.
Publication 2023
anti-IgG Buffers Enzyme-Linked Immunosorbent Assay Goat Homo sapiens IL1RN protein, human Mus Prospec Recombinant Proteins Serum Albumin, Human sulfuric acid Tweens
Fully conscious, heparinized animals underwent 50% ET with PolyCHb solution (Hb concentration 6%, human albumin 4%; the PolyCHb and human albumin were mixed immediately before ET). The blood was collected through the arterial catheter, and the PolyCHb solution was transfused through the venous catheter by syringe pumps simultaneously at a rate of 1 mL/min. The total blood volume of a guinea pig was calculated as 0.07 (milliliters per gram) × body weight (grams) (Ancill, 1956 (link)). Immediately after ET, AA injection solution was injected to the body via the venous catheter, by a 1 mL disposable syringe. The dosage of AA is calculated by multiplying the target concentration (2 mmol/L) with the blood volume. Blood samples (300 μL) were obtained from the arterial catheter pre-transfusion together at 0 and 4 h after ET. The guinea pigs were individually housed in metabolism cages for 4 h pre- and post-ET to collect the urine samples. The animals were sacrificed 4 h post-ET and the kidneys were dissected and rinsed with pre-cold saline. One kidney was cut in half and frozen immediately in liquid nitrogen, and the other kidney was fixed in 10% paraformaldehyde.
Publication 2023
Animals Arteries BLOOD Blood Transfusion Blood Volume Body Weight Catheters Cavia Cold Temperature Consciousness Freezing Human Body Kidney Metabolism Nitrogen paraform Saline Solution Serum Albumin, Human Syringes Urine Veins
Human serum albumin solution was purchased from Baxter (Vienna, Austria). Vitamin C (AA) injection was supplied by Shenya Animal Healthcare (Shanghai, China). Mouse monoclonal antibodies to heme oxygenase 1 (HO-1, #MA1-112) and mouse monoclonal antibodies to L-ferritin (#MA5-14733) were purchased from Thermo Fisher Scientific (Rockford, United States). Rabbit monoclonal antibody to ß-Actin (#AC026) was purchased from Abclonal (Wuhan, China). Rabbit monoclonal antibody to nuclear factor erythroid 2-related factor 2 (Nrf2, # ab92946), rabbit monoclonal antibodies 4-hydroxy-2-nonenal (4-HNE, #ab46545), goat anti-mouse IgG H&L (HRP) (#ab6789), goat anti-rabbit IgG H&L (HRP) (#ab6721), a catalase (CAT) activity assay kit (#ab83464), a glutathione peroxidase (GPx) assay kit (#ab102530), and an 8-hydroxy 2 deoxyguanosine (8-OHdG) assay kit (#ab201734) were purchased from Abcam (Cambridge, MA, United States). A total antioxidant capacity (T-AOC) assay kit (#A015-2-1) and superoxide dismutase (SOD) kit (#A001-3-1) were obtained from Jiancheng Biotech. (Nanjing, China). A malondialdehyde (MDA) kit (#S0131S) was supplied by Beyotime Biotechnology (Shanghai, China). An enhanced chemiluminescence (ECL) kit (#PF001) was a product from Affinity Biosciences (Changzhou, China).
Publication 2023
8-Hydroxy-2'-Deoxyguanosine Actins Animals anti-IgG Antioxidants Ascorbic Acid Biological Assay Catalase Chemiluminescence Ferritin GA-Binding Protein Transcription Factor Goat Heme Oxygenase-1 Malondialdehyde Mice, House Monoclonal Antibodies Peroxidase, Glutathione Rabbits Serum Albumin, Human Superoxide Dismutase
One milliliter of each sample of liquefied semen was mixed with 2 mL of Ham’s F10 (Sigma, USA), supplemented with 20% human serum albumin (HSA) (Kedrion Biopharma, Italy),
and centrifuged at 300 g for 10 min. The supernatant was decanted, and 1 mL of Ham’s F10 was added. The tubes were gently positioned at a 45-degree angle for one
hour at 37 °C and 5% CO2 for swim-up separation of motile spermatozoa. This supernatant was carefully aspirated, and its volume was adjusted to 1 mL using Ham’s F10.
Publication 2023
Semen Serum Albumin, Human Sperm

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Human serum albumin is a laboratory product derived from human blood plasma. It serves as a protein-rich component in various cell culture media and other in vitro applications.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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The Human Albumin ELISA Kit is a quantitative assay designed to measure the concentration of human albumin in biological samples. It utilizes the enzyme-linked immunosorbent assay (ELISA) technique to detect and quantify the target analyte.
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Human albumin is a laboratory equipment product used for various applications in medical and scientific research. It is a purified protein derived from human blood plasma that serves as a key component in various laboratory procedures and experiments. The core function of human albumin is to maintain oncotic pressure and assist in the transport of various substances within the body. This product is typically used in a controlled laboratory setting to support specific research and analytical needs.
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The human albumin ELISA kit is a laboratory assay used to quantitatively measure the concentration of albumin, a protein found in human blood plasma. The kit utilizes the enzyme-linked immunosorbent assay (ELISA) technique to detect and analyze the levels of human albumin in a given sample.
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NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.

More about "Serum Albumin, Human"

Serum albumin, a major plasma protein, plays a crucial role in various physiological processes.
It is synthesized in the liver and serves as a transport and regulatory molecule, maintaining oncotic pressure, transporting substances, and supporting metabolic activities.
This versatile protein is widely utilized in medical research and clinical settings to study both normal and pathological conditions.
Researchers often employ human serum albumin (HSA) and bovine serum albumin (BSA) in their experiments, leveraging their unique properties and functions.
HSA, in particular, is commonly used in cell culture media, such as RPMI 1640, to provide a nutrient-rich environment for cells.
Additionally, DMSO and FBS (fetal bovine serum) are frequently used alongside albumin to enhance cell growth and survival.
The quantification of serum albumin levels can provide valuable insights into a patient's overall health status, and various ELISA (Enzyme-Linked Immunosorbent Assay) kits are available to accurately measure human albumin concentrations.
These kits, including the Human Albumin ELISA Quantitation Set and Human Albumin ELISA Kit, enable researchers and clinicians to assess albumin levels and monitor changes related to physiological or pathological conditions.
Sodium chloride (NaCl), a common salt, is often employed in albumin-based solutions to maintain the appropriate osmotic balance and pH, ensuring the stability and functionality of the protein.
By understanding the interplay between serum albumin and these related substances, researchers can optimize their experimental designs and uncover new insights into the diverse roles of this essential plasma protein.