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Egg albumin

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Egg albumin is a laboratory product derived from the white portion of chicken eggs. It is a common component of various culture media and buffers used in various scientific applications, such as cell culture, protein purification, and electrophoresis. Egg albumin serves as a stabilizing agent and protein source in these applications.

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Lab products found in correlation

Bovine serum albumin (bsa), by Merck Group (6 mentions) Gelatin, by Merck Group (3 mentions) Trypsin edta, by Thermo Fisher Scientific (3 mentions) α chymotrypsinogen, by Merck Group (2 mentions) Acrylamide, by Merck Group (2 mentions) Myoglobin, by Merck Group (2 mentions) Casein, by Merck Group (2 mentions) Hemoglobin, by Merck Group (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (2 mentions) Kaolin, by Merck Group (1 mentions) Folin ciocalteau, by Merck Group (1 mentions) Ammonium acetate, by Merck Group (1 mentions) Cyanocobalamin, by Merck Group (1 mentions) Gluten, by Merck Group (1 mentions) Whey protein, by Merck Group (1 mentions) Escherichia coli trans5α, by Transgene (1 mentions) Phenylmethylsulfonyl fluoride pmsf, by Merck Group (1 mentions) Pepstatin a, by Merck Group (1 mentions) Protamine sulfate, by Merck Group (1 mentions) Peptide n glycosidase f pngase f, by New England Biolabs (1 mentions)

Spelling variants of this product

Albumin from chicken egg white (OVA) (6 citations) Chicken egg white albumin (5 citations) Phosphate buffer saline-egg albumin (3 citations) Albumins ( (2 citations) Monoclonal anti-chicken egg albumin (clone OVA-14 mouse IgG1 isotype), (2 citations) Albumin Egg (A-5253), (2 citations) Albumin from chicken egg white (grade II) (2 citations) Albumin from chicken egg (2 citations) Rabbit anti-chicken egg albumin IgG (2 citations) Chicken egg albumin (OVA), (2 citations)

14 protocols using egg albumin

1

Rat Skin Vascular Permeability Assay

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Six-week old male Wistar rats (Japan Clea, Inc. Tokyo, Japan) were used (n = 7–27 in each time point). The homologous antiserum used was prepared according to the method described. Briefly, rats were sensitized by intramuscular injection of 0.2 ml of 10 mg/mL egg albumin (Sigma-Aldrich, St. Louis, MO, USA) to both femurs and intraperitoneal administration of Bordetellapertussis inactive microorganism suspension (B. pertussis, Kitasato Institute Research Center for Biologicals, Saitama, Japan). On day 14, animals were bled and antiserum was collected. Separated antiserum was stored at -80°C.
Rat homologous antiserum (100 μL) was injected into the shaved back skin of rats. After 24 h, sensitized rats were injected with 0.5 mL of mixed solution of 0.5% Evan blue (Fluka, Buchs, Switzerland) and 1% egg albumin (1:1) through the tail vein. Thirty minutes later, rats were sacrificed and the dye content of the shaved dorsal skin was determined quantitatively. Pieces of the dorsal skin containing extravasated dye were removed and soaked overnight in stoppard glass tubes containing 1 ml of mixed solution of 0.6 N H3PO4/acetone (13:5). The absorbance of supernatant was measured at 620 nm using a spectrophotometer and the concentration of the dye in the shaved dorsal skin (μg/site) was determined. Fasting duration was determined as the time between food removal and antigen challenge.
Nakamura S., Hisamura R., Shimoda S., Shibuya I, & Tsubota K. (2014). Fasting mitigates immediate hypersensitivity: a pivotal role of endogenous D-beta-hydroxybutyrate. Nutrition & Metabolism, 11, 40.
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2

Protein Purification Protocol

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β-mercaptoethanol, sodium dodecyl sulphate are products of BDH Chemical Limited, Poole, England. Acrylamide, N,N,N′,N′-tetamethyl ethylenediamine (TEMED), ammonium acetate, kaolin, bovine serum albumin (BSA), folin ciocalteau, egg albumin, α-chymotrypsinogen and low molecular weight protein markers for electrophoresis were purchased from Sigma Chemical Company, St Louiz, Mo, USA. Blue dextran, CM-sephadex C-50, sephadex G-75, Biogel P-100 are products of Pharmacia Fine Chemicals, Uppsala, Sweden. All other chemicals and reagents used were of analytical grade.
Taiwo A.S., Adenike K, & Aderonke O. (2020). Efficacy of a natural coagulant protein from Moringa oleifera (Lam) seeds in treatment of Opa reservoir water, Ile-Ife, Nigeria. Heliyon, 6(1), e03335.
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3

Protein Stock Solution Preparation

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Cyanocobalamin, aqua cobalamin, casein, egg albumin, myoglobin, and gluten were purchased from Sigma-Aldrich (Sydney, Australia). D2O was purchased from UNSW chemical stores. Brown rice protein (BRP) isolate (90% purity) and yellow pea protein (YPR) (90% purity) isolate were acquired from Axiom Foods, Inc. (through Pacific Resources Intl., Sydney, Australia). All reagents were of analytical grade and were used without further purification. The stock solutions of casein, egg albumin, myoglobin, gluten, rice protein, pea protein (80 μmol/L), and Cyanocobalamin and aqua cobalamin (0.07, 0.22, 0.37, 3.69, 7.38, 8.86, 22.14, 36.90, 51.66, 66.42, 88.56 μmol/L) were prepared using D2O.
Ghosh R., Thomas D.S, & Arcot J. (2023). Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies. Foods, 12(3), 575.
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4

Heterologous Protease Expression in Aspergillus niger

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R. miehei CAU432 has been deposited in the China General Microbiological Culture Collection Center (CGMCC No. 4967) with the whole genome sequenced [24 (link)]. Escherichia coli Trans5α (Transgene, Beijing, China) was used for molecular cloning. A. niger strain FBL-A (ΔglaA) was used for expression of the protease. It was cultured in Czapek-Dox medium. If necessary, 200 μg/mL hygromycin was added for the hygB selection marker. Casein, hemoglobin, gelatin, whey protein, lactoglobulin, bovine serum albumin, myoglobin, egg albumin, protamine sulfate, collagen, phenylmethylsulfonyl fluoride (PMSF), and pepstatin A were obtained from Sigma-Aldrich Corporation (Darmstadt, Germany). Other chemicals used in this study were provided by Biodee Corporation (Beijing, China).
Wang S., Zhang P., Xue Y., Yan Q., Li X, & Jiang Z. (2021). Characterization of a Novel Aspartic Protease from Rhizomucor miehei Expressed in Aspergillus niger and Its Application in Production of ACE-Inhibitory Peptides. Foods, 10(12), 2949.
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5

Characterization of Blood Erythrocytes

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Glutaraldehyde, sodium dodecyl sulfate, sugars were purchased from England (BDH Chemical Limited, Poole). Acrylamide, α-chymotrypsinogen, bovine serum albumin (BSA), egg albumin, and standard marker protein are products of Sigma-Aldrich, St Louis, Missouri, USA. Sephadex G-100, Biogel P-100, and Blue dextran were purchased from Sweden (Pharmacia Fine Chemicals, Uppsala). The quality of other used reagents and chemicals was of research-grade.
A, B, O human blood groups were collected with informed consent from healthy subjects. Rabbit erythrocytes were sourced from the blood of rabbits, reared at the College of Health Sciences, Obafemi Awolowo University, Ile–Ife.
Fresh bovine blood collected in a 10% EDTA (w/v) bottle from a municipal abattoir within Ile–Ife was the source of bovine erythrocytes.
Nubi T., Adewole T.S., Agunbiade T.O., Osukoya O.A, & Kuku A. (2021). Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds. Biotechnology Reports, 31, e00650.
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6

Deglycosylation of Tsetse Salivary Proteins

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Tsetse salivary proteins were treated with peptide-N-glycosidase F (PNGase F, New England Biolabs), which cleaves all N-linked glycans except those with an α-1,3 fucose modification of the chitobiose core [20 (link)]. Deglycosylation was done according to the manufacturer’s instructions: briefly, 1x glycoprotein denaturing buffer (5% SDS, 0.4 M DTT) was added to 10 μg of G. m. morsitans salivary proteins and incubated at 100°C for 10 min. 1x G7 reaction buffer (0.5 M sodium phosphate pH 7.5), 1% NP40 and 1 μl PNGase F were added and incubated at 37°C overnight.
Salivary samples were additionally treated with Endoglycosidase H (Endo H; New England Biolabs), which cleaves the chitobiose core of high-mannose and some hybrid N-linked glycans [21 (link)]. Deglycosylation conditions were the same as described for PNGase F treatment, with an addition of NP40 and the G5 Reaction buffer (50 mM sodium citrate, pH 5.5) used instead of G7; 5000 units of Endo H were used per reaction. Egg albumin (Sigma) was treated in parallel as digestion control for both enzymes.
Kozak R.P., Mondragon-Shem K., Williams C., Rose C., Perally S., Caljon G., Van Den Abbeele J., Wongtrakul-Kish K., Gardner R.A., Spencer D., Lehane M.J, & Acosta-Serrano Á. (2021). Tsetse salivary glycoproteins are modified with paucimannosidic N-glycans, are recognised by C-type lectins and bind to trypanosomes. PLoS Neglected Tropical Diseases, 15(2), e0009071.
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7

Immunohistochemical Visualization of NPY

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Sections were washed three times in KPBS for 10 min and imbedded in a solution containing 300 g/L egg-albumin (Sigma-Aldrich) and 30 g/L gelatin (Sigma-Aldrich), frozen at −80 °C and sub-sliced on a cryotome at −20 °C (Cellab Nordia AB) to 16 μm thick slices. Slices were mounted on positively charged glasses (+Menzel glass, Thermo Scientific) and stored at −20 °C. These slices were then preincubated in 10% Donkey serum, 0.25% Triton X-100 in KPBS for 1 h. After adding rabbit anti-NPY antibody (1:500, #N9528, Sigma-Aldrich, DK) in 5% Donkey serum, 0.25% Triton X-100 in KPBS, sections were incubated overnight at 4 °C. Sections were washed 3 × 10 min in tKPBS, incubated for 2 h at RT with Cy3-conjugated Donkey anti-rabbit antibody (1:200, Jackson Immunoresearch USA) in 1% Donkey serum, 0.25% Triton X-100 in KPBS and washed 1 × 10 min in tKPBS and 2 × 10 min in KPBS. The slides were mounted with DABCO (Sigma-Aldrich) and digitized images obtained using Olympus BX61 microscope and CellSens software.
Melin E., Andersson M., Gøtzsche C.R., Wickham J., Huang Y., Szczygiel J.A., Boender A., Christiansen S.H., Pinborg L., Woldbye D.P, & Kokaia M. (2023). Combinatorial gene therapy for epilepsy: Gene sequence positioning and AAV serotype influence expression and inhibitory effect on seizures. Gene Therapy, 30(7-8), 649-658.
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8

Glycoprotein N-Linked Profiling via ConA Lectin Blotting

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Saliva samples, before and after treatment with PNGase F (New England Biolabs, US) were run on a 12.5% polyacrylamide gel under standard conditions, transferred onto a PVDF membrane (Fisher Scientific, UK), and blocked with 1% BSA (Sigma, St. Louis, US) in PBS-Tw 20 (Sigma, St. Louis, US) overnight at 4 °C. Membrane was incubated with 1 µg/ml biotinylated Concanavalin A (ConA) lectin (Vector Labs, Peterborough, UK) for 1 h at room temperature. After washing, the membrane was incubated with 1:100,000 streptavidin-HRP (Vector Labs, Peterborough, UK). SuperSignal West Pico Chemiluminescent substrate (ThermoFisher, Massachusetts, US) was used to detect the bands. Egg albumin (Sigma, St. Louis, US), a highly mannosylated N-linked glycoprotein68 (link), was used as positive control.
Mondragon-Shem K., Wongtrakul-Kish K., Kozak R.P., Yan S., Wilson I.B., Paschinger K., Rogers M.E., Spencer D.I, & Acosta-Serrano A. (2020). Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis. Scientific Reports, 10, 12903.
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9

Chromatographic purification of α-crystallin

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The samples of native and refolded αH-crystallin were centrifuged at 14,500× g for 30 min using a MiniSpin+ Eppendorf centrifuge. The supernatant was loaded onto the column (Sephacryl S300HR, 2.5 × 90 cm) and separated into fractions at a flow rate of 1.6 mL/min. The column was pre-calibrated with the following proteins from (Sigma-Aldrich): thyroglobulin (660 kDa), ferritin (440 kDa), aldolase (158 kDa), BSA dimer (134 kDa), BSA (67 kDa), egg albumin (45 kDa), and cytochrome c (12.5 kDa). The standard error for protein mass determination was 4%.
Muranov K.O., Poliansky N.B., Borzova V.A, & Kleimenov S.Y. (2023). Refolding Increases the Chaperone-like Activity of αH-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin. International Journal of Molecular Sciences, 24(17), 13473.
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10

Evaluation of Biomolecular Interactions

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Bovine serum albumin (BSA), human serum albumin (HSA), egg albumin, chymotrypsin, trypsin, lysozyme, transferrin, myohemoglobin, hemoglobin, phycocyanin, propidium iodide (PI), and calcein-AM were brought from Sigma-Aldrich. Phalloidin-FITC, 4′,6-diamidino-2-phenylindole (DAPI), DMEM culture medium, foetal bovine serum (FBS), trypsin-EDTA, phosphate-buffered saline (PBS) (pH 7.4), and penicillin-streptomycin solution were purchased from Thermo Fisher. Luria−Bertani (LB) broth medium, agarose, Lactase Dehydrogenase (LDH) kit and Cell Counting Kit-8 (CCK-8) kit were brought from Beyotime Biotechnology (Shanghai, China). THPS (ca. 75 in Water, MW 406.28) solution was brought from Aladdin. Staphylococcus aureus (S. aureus, SA, ATCC25923) and methicillin-resistant staphylococcus aureus (MRSA, ATCC43300) strains were purchased from HuanKai Microbial. Deionized water (18.2 MΩ cm) was used in whole experiments.
Ouyang J., Bu Q., Tao N., Chen M., Liu H., Zhou J., Liu J., Deng B., Kong N., Zhang X., Chen T., Cao Y, & Tao W. (2022). A facile and general method for synthesis of antibiotic-free protein-based hydrogel: Wound dressing for the eradication of drug-resistant bacteria and biofilms. Bioactive Materials, 18, 446-458.
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