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Serum Proteins

Serum proteins are a diverse group of biomolecules found in the blood plasma.
They play crucial roles in various physiological processes, including transport, immune function, and maintenance of fluid balance.
This category encompasses a wide range of proteins, such as albumins, globulins, and clotting factors, which can be measured and analyzed to provide insights into an individual's health status.
Serum protein analysis is a valuable tool in clinical diagnostics, permetting the detection and monitoring of various diseases and conditions.
Understanding the composition and dynamics of serum proteins is essential for researchers and clinicians aiming to optimize research protocols, ensure reproducibility, and improve patient outcomes.

Most cited protocols related to «Serum Proteins»

All samples were stored at − 80 °C until use. Serum levels of C-reactive protein (CRP) were determined by an immuno-turbidimetric technique using an Olympus AU 400 biochemical analyzer (Olympus Optical, Tokyo, Japan), and erythrocyte sedimentation rate (ESR) was measured according to the Fahreus and Westergren method. ANAs were detected using indirect immunofluorescence on HEP2 cells, and the autoantibodies of the ENA complex (anti-U1RNP, anti-Ro, anti-La, anti-DNA-topoisomerase I, anti-Jo-1, anti-P protein, anti-Sm, and anti-centromere) were assayed by immunoblot. Plasma levels of Hsp90 were assessed by a high-sensitivity ELISA kit (eBioscience, Vienna, Austria) according to the manufacturer's protocol. The assay recognizes human Hsp90 alpha. The calculated sensitivity is 0.03 ng/mL. The absorbance value was established at 450 nm by an ELISA reader (SUNRISE; Tecan, Grödig, Austria).
Publication 2021
Autoantibodies Biological Assay Cells Centromere DNA Topoisomerases, Type I Ducks Enzyme-Linked Immunosorbent Assay Homo sapiens HSP90 Heat-Shock Proteins Hypersensitivity Indirect Immunofluorescence OCA2 protein, human Plasma Sedimentation Rates, Erythrocyte Serum Proteins Turbidimetry Vision
Whole blood was collected into Tempus tubes (Applied Biosystems, CA, USA) from active TB patients (confirmed by culture for M. tuberculosis); Latent TB patients (defined by a positive tuberculin-skin test (TST) (London) and/or a positive M. tuberculosis antigen-specific IFN-γ release assay, IGRA; healthy controls (recruited in London; TST/IGRA negative). RNA was extracted from whole blood and purified (by Dynabeads, Invitrogen) neutrophils, monocytes, CD4+ and CD8+ T cells and genome-wide transcriptional profiles were generated using Illumina HT12 beadarrays, and analysed using Genespring GX, (see main Methods section). Calculation of “Molecular Distance to Health” 11 (link), transcriptional modular analysis 7 (link), and analysis of significance 12 (link) were performed as previously described. Pathway analysis was performed using Ingenuity (Ingenuity Systems, Inc., CA, USA). Multiplex Serum Protein Measurement was performed using Milliplex Multi-Analyte Profiling System by Millipore UK, Ltd, Dundee. Flow Cytometry was performed on a Beckman Coulter Cyan using Summit Software Version 3.02, followed by FlowJo analysis.
Publication 2010
Antigens Biological Assay BLOOD CD8-Positive T-Lymphocytes Flow Cytometry Genetic Profile Interferon Type II Monocytes Mycobacterium tuberculosis Neutrophil Patients Serum Proteins Transcription, Genetic Tuberculin Test
Detailed materials and methods are provided in the supplementary materials (12 (link)). We performed a genome-proteome-wide association study among 10,708 participants of European-descent in the Fenland study (Table S1) on 10.2 million genetic variants and plasma abundances of 4,775 distinct protein targets measured in plasma using established workflows (15 (link)). Protein targets were measured using the SomaScan v4 assay employing 4,979 single-stranded oligonucleotides (aptamers) with specific binding affinities to 4,775 unique protein targets (68 (link), 69 (link)). We used the term ‘protein target’ to refer to proteins targeted by at least one aptamer. We define significant genetic variant – protein target associations (pQTLs) at a stringent Bonferroni-threshold (p<1.004×10−11) and performed approximate conditional analysis to detect secondary signals for each genomic region identified by distance-based clumping of association statistics. We defined cross-aptamer regions using a combined approach of multi-trait colocalization (46 (link)) and LD-clumping. We classified pQTLs as protein- or pathway-specific by assessing pQTL-specificity across the entire proteome (p<5×10−8) while testing whether associated protein targets were captured by a common GO term or a protein community in a data-driven protein network. We computed the variance explained in plasma abundances of protein targets by cis- (within ±500kb of the protein-encoding gene) or trans-pQTLs according to different specificity categories using linear regression models. We used statistical colocalization (70 (link)) to test for a shared genetic signal between expression or alternative splicing of the protein-encoding gene and the cis-pQTL in one out of at least 49 tissues of the GTEx v8 project (24 (link)). We systematically cross-referenced established genetic risk loci for common complex diseases and phenotypes with pQTLs by identifying cis-pQTLs or strong proxies (r2>0.8) in the GWAS catalog (https://www.ebi.ac.uk/gwas/). We finally performed phenome-wide colocalization screens at 1,548 protein-encoding loci using publicly available (71 (link)) as well as in-house curated genome-wide association statistics for thousands of phenotypes. We applied stringent priors and conservative filters to derive high confidence protein – phenotype links. We used basic functions of R (v.3.6.0), the R package igraph, and the BioRender web application (https://biorender.com/) to create figures. The Fenland study was approved by the National Health Service (NHS) Health Research Authority Research Ethics Committee (NRES Committee – East of England Cambridge Central, ref. 04/Q0108/19), and all participants provided written informed consent.
Publication 2021
Binding Proteins Biological Assay Ethics Committees, Research Europeans Gene Products, Protein Genetic Diversity Genetic Loci Genetic Testing Genome Genome-Wide Association Study Health Services, National link protein Oligonucleotides Phenotype Plasma Plasma Proteins Proteins Protein Targeting, Cellular Proteome Serum Proteins Staphylococcal Protein A Tissues

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Publication 2014
beta-glycerol phosphate Biological Assay Buffers Cells Culture Media, Serum-Free Diphosphates Edetic Acid Fluorescein HEPES Lanugo Protease Inhibitors Proteins Serum Proteins Sodium Chloride Tablet Triton X-100
Serum samples contain a substantial portion of large molecular weight proteins and lipoproteins, which affects the identification and quantification of small molecule metabolites by NMR spectroscopy. Consequently, we introduced a step in the protocol to remove serum proteins (deproteinization). There are several routes to serum deproteinization, including organic solvent (acetonitrile, methanol, isopropanol) precipitation, ultrafiltration [28] (link), [44] (link) as well as spectral manipulation methods such as diffusion editing [45] (link). While other researchers have found that ultrafiltration yields poor signal-to-noise ratios, we found that by using an ultrafiltration protocol similar to that described by Tiziani [46] (link) and Weljie et al [47] (link), we could obtain excellent spectra that yielded metabolite concentrations that closely matched known values measured using standard clinical chemistry techniques. Ultrafiltration also has other advantages: it is relatively quick, very reproducible, does not introduce unwanted solvent peaks and is “safe” in terms of avoiding unwanted side-reactions with biofluid metabolites. All 1H-NMR spectra were collected on a either a 500 MHz or 800 MHz Inova (Varian Inc., Palo Alto, CA) spectrometer using the first transient of the tnnoesy-presaturation pulse sequence. The resulting 1H-NMR spectra were processed and analyzed using the Chenomx NMR Suite Professional software package version 6.0 (Chenomx Inc., Edmonton, AB), as previously described [15] . Further details on the NMR sample preparation and NMR data acquisition are provided in File S1.
Publication 2011
1H NMR acetonitrile Diffusion Isopropyl Alcohol Lipoproteins Methanol Proteins Pulse Rate Serum Serum Proteins Solvents Spectroscopy, Nuclear Magnetic Resonance Staphylococcal Protein A Transients Ultrafiltration

Most recents protocols related to «Serum Proteins»

Not available on PMC !

EXAMPLE 8

In order to determine whether Nanobodies could inhibit the interaction of native CD80 and CD86 with CD28-Ig or CTLA4-Ig, Raji cells were incubated with serial dilutions of purified protein from confirmed clones or an irrelevant Nanobody. Next, either HuCD28-HuIgG1 or HuCTLA4-HuIgG1 was added to the cells/Nanobody suspension without washing the cells in between. After a wash step, cell-bound CD28- or CTLA4-HuIg was revealed using a phycoerythrin-conjugated F(ab′)2 derived from affinity purified goat-anti-human IgG1 antiserum (bovine serum protein crossabsorbed). Percentage inhibition was determined based on MFI values of controls having received an irrelevant specificity Nanobody (high control) or no CD28- or CTLA4-Ig fusion protein at all (low control).

Example FACS profiles of representative inhibitory and non-inhibitory Nanobodies are shown in FIG. 7.

Results from both ELISA and FACS based assays are summarized in Table C-6.

Patent 2024
Biological Assay Bos taurus Cardiac Arrest Cells Clone Cells CTLA-4-Ig CTLA4 protein, human Enzyme-Linked Immunosorbent Assay Goat Homo sapiens IgG1 Immune Sera Phycoerythrin Proteins Psychological Inhibition Serum Proteins Technique, Dilution VHH Immunoglobulin Fragments

Example 14

Variables tested include: concentration of HA, concentration of zinc oxide, concentration of titanium dioxide, addition of vitamin C, and serum preparation method.

FIGS. 94A-94C are tables summarizing embodiments of cosmetic serums of the present disclosure with varying additives and concentrations of components suitable for protection against ultraviolet radiation (UV). Table 33 provides an embodiment of a hydrating serum of the present disclosure with vitamin C.

TABLE 33
Embodiment of Hydrating serum of
the present disclosure with vitamin C
% Silk Solution  1.0% w/v
(60 minute boil, 25 kDA)
Hyaluronic Acid 0.75% w/v
(sodium hyaluronate)
Lemongrass Oil20 uL/15 mL
silk solution
Sodium Ascorbyl Phosphate  6 g
Lactic Acid1.2 mL

A serum of the present disclosure can be made with from about 0.25% to about 10% sodium hyaluronate (increasing % results in more viscous serum). 0.5% to about 10% silk solutions can be used to prepare a serum of the present disclosure. A serum of the present disclosure can be clear and have a yellow tinted color. A serum of the present disclosure can have a pH=6. A serum of the present disclosure can have a lubricious texture that is rubbed in easily without residue.

Concentration of HA:

Hyaluronic acid (Sodium Hyaluronate) was tested as an ingredient in the UV silk serum due to its hygroscopic properties and widely accepted use in cosmetic products to promote hydration of skin. 1%, 2.5% and 5% HA solutions were tested. With increasing HA %, the serum became more viscous and gel like. 1% HA was not feasible for the UV serum due to the fact that the UV additives (zinc oxide, titanium dioxide) are not water soluble and need to be dispersed. 1% HA was not viscous enough for dispersion and the UV additives precipitated out. 2.5% gave the best consistency based on preferred feel, texture and viscosity and was able to disperse the UV additives. 5% was a very thick, viscous serum.

Concentration of Mineral Filters: Zinc Oxide and Titanium Dioxide:

Zinc oxide and titanium dioxide were explored as UV additives that are considered safe. These additives mechanically protect from UV radiation by forming a physical reflective barrier on the skin. Both are not soluble in water and must be dispersed for the current aqueous solution. Zinc oxide concentration varied from 2.5%, 3.75%, 5%, 5.625%, 10%, 12% and 15%. Titanium dioxide concentrations varied from 1.25%, 1.875%, 3%, 5% and 10%. Increasing the concentration of UV additives resulted in minor increases of white residue and how well dispersed the additives were, however if mixed well enough the effects were negligible. Zinc oxide and titanium dioxide were mixed together into serums in order to achieve broad spectrum protection. Zinc oxide is a broad spectrum UV additive capable of protecting against long and short UV A and UV B rays. However titanium dioxide is better at UV B protection and often added with zinc oxides for best broad spectrum protection. Combinations included 3.75%/1.25% ZnO/TiO2, 5.625%/1.875% ZnO/TiO2, 12%/3% ZnO/TiO2, 15%/5% ZnO/TiO2. The 3.75%/1.25% ZnO/TiO2 resulted in spf 5 and the 5.625%/1.875% ZnO/TiO2 produced spf 8.

Vitamin C:

Sodium ascorbyl phosphate was used as a vitamin C source. Formulations were created with the vitamin C concentration equal to that in the silk gel (0.67%). Formulations were also created with 20% sodium ascorbyl phosphate which is soluble in water.

Serum Preparation:

The vitamin C (sodium ascorbyl phosphate) must first be dissolved in water. Sodium hyaluronate is then added to the water, mixed vigorously and left to fully dissolve. The result is a viscous liquid (depending on HA %). The viscosity of the HA solution allows even dispersion of the zinc oxide and titanium dioxide and therefore HA must be mixed before addition of UV additives. The zinc oxide and titanium dioxide are then added to the solution and mixed vigorously with the use of an electric blender. Silk solution is then added and mixed to complete the serum formulation.

Chemical Filters:

A UV serum of the present disclosure can include one, or a combination of two or more, of these active chemical filter ingredients: oxybenzone, avobenzone, octisalate, octocrylene, homosalate and octinoxate. A UV serum of the present disclosure can also include a combination of zinc oxide with chemical filters.

In an embodiment, a UV serum of the present disclosure can be applied approximately 15 minutes before sun exposure to all skin exposed to sun, and can be reapplied at least every 2 hours. In an embodiment, a UV serum of the present disclosure includes water, zinc oxide, sodium hyaluronate, titanium dioxide, silk, and vitamin C or a vitamin C derivative such as sodium ascorbyl phosphate. In an embodiment, a UV serum of the present disclosure protects skin and seals in moisture with the power of silk protein. In an embodiment, a UV serum of the present disclosure improves skin tone, promotes collagen production and diminishes the appearance of wrinkles and fine lines with the antioxidant abilities of vitamin C. In an embodiment, a UV serum of the present disclosure delivers moisture for immediate and long-term hydration throughout the day with concentrated hyaluronic acid. In an embodiment, a UV serum of the present disclosure helps prevent sunburn with the combined action of zinc oxide and titanium dioxide. In an embodiment, a UV serum of the present disclosure is designed to protect, hydrate, and diminish fine lines while shielding skin from harsh UVA and UVB rays. In an embodiment, the silk protein in a UV serum of the present disclosure stabilizes and protects skin while sealing in moisture, without the use of harsh chemical preservatives or synthetic additives. In an embodiment, the vitamin C/derivative in a UV serum of the present disclosure acts as a powerful antioxidant that supports skin rejuvenation. In an embodiment, the sodium hyaluronate in a UV serum of the present disclosure nourishes the skin and delivers moisture for long-lasting hydration. In an embodiment, the zinc oxide and titanium dioxide in a UV serum of the present disclosure shields skin from harmful UVA and UVB rays. The silk protein stabilization matrix in a UV serum of the present disclosure protects the active ingredients from the air, to deliver their full benefits without the use of harsh chemicals or preservatives. The silk matrix also traps moisture within the skin furthering the hydrating effect of the sodium hyaluronate.

Patent 2024
Acids Antioxidants Ascorbic Acid avobenzone Collagen Electricity Feelings Figs Furuncles homosalate Hyaluronic acid Minerals octinoxate octisalate octocrylene oxybenzone Pharmaceutical Preservatives Proteins Radiation Rejuvenation SERPINA3 protein, human Serum Serum Proteins Silk Skin Skin Pigmentation sodium ascorbyl phosphate Sodium Hyaluronate Strains Sunburn titanium dioxide Viscosity Vitamin A Vitamins west indian lemongrass oil Zinc Oxide
Not available on PMC !

Example 25

The instant study is designed to test the immunogenicity in mice of candidate MeV vaccines comprising a mRNA polynucleotide encoding MeV hemagglutinin (HA) protein, MeV Fusion (F) protein or a combination of both.

Mice are immunized intravenously (IV), intramuscularly (IM), or intradermally (ID) with candidate vaccines. Up to three immunizations are given at 3-week intervals (i.e., at weeks 0, 3, 6, and 9), and sera are collected after each immunization until weeks 33-51. Serum antibody titers against MeV HA protein or MeV F protein are determined by ELISA.

Patent 2024
Antigens Enzyme-Linked Immunosorbent Assay Hemagglutinin Immunization Immunogenicity, Vaccine Immunoglobulins Mus Polynucleotides Proteins RNA, Messenger Serum Serum Proteins Vaccines
Concentration of nicotine and its principal metabolite cotinine were measured from prenatally e-cig exposed mice plasma at PD7 by LCMS/MS analysis using Cotinine-d3 (MilliporeSigma, St. Louis, MO, USA) as an internal standard (IS) following a previously published method [44 (link)]. In brief, samples were prepared by protein precipitation of 25 µL mouse plasma using acetonitrile at 1:8 ratio. Mass Spectrometer was operated in positive polarity under the multiple reaction monitoring mode using electrospray ionization technique. The transitions of m/z 163.2 → 132.1, 177.2 → 98.0 and 180.2 → 101.2 were used to measure the nicotine, cotinine, and IS, respectively. The elution of nicotine (MilliporeSigma), cotinine (MilliporeSigma), and IS were at 1.89, 1.77, and 1.76 min, respectively. This was achieved with a mobile gradient phase consisting of 5 mM ammonium bicarbonate, acetonitrile, and methanol (3:1, v/v) at a 0.3 mL/min flow rate on a Kinetex EVO C18 column (Phenomenex, Torrance, CA, USA).
Publication 2023
acetonitrile ammonium bicarbonate Cotinine Laser Capture Microdissection Methanol Mice, House Nicotine Plasma Plasma Proteins Serum Proteins
The fermentation broth was collected at various fermentation times and then centrifuged at 8,000 × g for 15 min at 4°C. The soluble protein content of the supernatant of the extract was determined by BCA kit with bovine serum albumin as the standard. BCA was measured in a 96-well plate. Two hundred μL dye solution was added to 25 μL sample and then incubated at 37°C for 30 min, and then the absorbance of the solution was measured at 562 nm. The conversion formula of bovine serum protein standard curve is Y=0.0007X+0.1441 , R2=0.9987 .
Publication 2023
Bos taurus Fermentation Proteins Serum Albumin, Bovine Serum Proteins

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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 BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.
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Antibody diluent is a liquid solution used to dilute antibody samples for various laboratory applications. It is designed to maintain the stability and activity of the antibodies during the dilution process.
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Target Retrieval Solution is a reagent used in immunohistochemistry (IHC) and immunocytochemistry (ICC) procedures. It is designed to facilitate the retrieval of target antigens that have been masked or altered during the fixation and processing of tissue samples. The solution helps to unmask the antigens, making them accessible for subsequent binding to specific antibodies used in the IHC or ICC analysis.

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