Biotinylated bovine serum albumin

Manufactured by Merck Group

Sourced in Sao Tome and Principe

Biotinylated bovine serum albumin is a protein-based reagent used in various biotechnology applications. It consists of the protein bovine serum albumin (BSA) that has been modified to covalently attach biotin molecules. The biotin moiety allows for specific interactions and detection methods involving streptavidin or avidin.

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Lab products found in correlation

Streptavidin, by Thermo Fisher Scientific (2 mentions) Heparin biotin, by Merck Group (1 mentions) Cyclooctatetraene, by Merck Group (1 mentions) Horseradish peroxidase hrp, by Merck Group (1 mentions) Alexa fluor 488 labeled anti hla antibody, by BioLegend (1 mentions) Poly l lysine (pll), by Merck Group (1 mentions) Bsa standard, by Merck Group (1 mentions) Streptavidin, by Merck Group (1 mentions)

6 protocols using biotinylated bovine serum albumin

Quantifying LPL Activity in Conditioned Media and on Surfaces

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For LPL activity in conditioned media, plasmids bearing WT or mutant LPL variants were transiently transfected into HEK293 cells. LPL was released from the surface of cells through the addition of heparin, media was collected and the LPL secreted in media was assayed for activity using 10 μM DGGR essentially as previously described^{35 (link)}.
For LPL activity on a surface, a 96-well black-sided, clear-bottom plate, was functionalized by a brief incubation with biotinylated bovine serum albumin (Sigma, 1 mg/ml, 5 minutes), washed three times with PBS, incubated with streptavidin (Invitrogen, 0.1 mg/ml, 20 minutes) and washed again with PBS. Plates sat on ice with PBS in the wells until the experiment was ready to proceed. Wells were then treated as follows: A) No LPL (Buffer), B) biotinylated bovine LPL (~150 nM, 5 minute incubation), C) Heparin-Biotin (Sigma, 1 mg/ml, 5 minutes) + bovine LPL (150 nM, 5 minutes). Wells were washed three more times with PBS and substrate was added (150 mM NaCl, 0.4% Triton-X, 20 mM Tris 8.0, 14 μM DGGR). Wells were excited at 529 nm with a 590 nm cut-off and read for emission at 600 nm on a SpectaMax 5 plate reader.

Hayne C.K., Yumerefendi H., Cao L., Gauer J.W., Lafferty M.J., Kuhlman B., Erie D.A, & Neher S.B. (2018). We FRET So You Don’t Have To: New Models of the Lipoprotein Lipase Dimer. Biochemistry, 57(2), 241-254.

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Quartz Slide Preparation for Single-Molecule Studies

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Home-built quartz slides were prepared as previously described^{36 (link)} with 5 minute epoxy (Staples) used for sealing the edges of the slide. The surface of the slides was pre-functionalized by brief incubation with biotinylated bovine serum albumin (Sigma, 1 mg/ml, 5 minutes), washing, and followed by incubating with streptavidin (Invitrogen, 0.1 mg/ml, 20 minutes) and washing. For slides utilizing heparin attachment, biotin-heparin (Sigma) was either added directly to the slides or pre-incubated with the LPL before addition. Immediately preceding data collection, LPL was deposited onto the slide surface in Buffer A (20 mM Tris, 300 mM sodium chloride, 5% glycerol, 1 mM deoxycholate, pH 7.5) and incubated for 5 minutes. Unbound LPL was then washed out with imaging buffer (Buffer A with the addition of ~50 μM cyclooctatetraene (Sigma), a triplet state quencher to lessen fluorophore blinking.)

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Enzyme-Linked Immunoassay Preparation

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Horseradish peroxidase, HRP (type VI, ≥250 units per mg solid), biotinylated Bovine Serum Albumin, b-BSA (A8549) and avidin-fluorescein isothiocyanate, Av-FITC from egg white (A2901) were purchased from Sigma Aldrich.

Sitsanidis E.D., Schirmer J., Lampinen A., Mentel K.K., Hiltunen V.M., Ruokolainen V., Johansson A., Myllyperkiö P., Nissinen M, & Pettersson M. (2021). Tuning protein adsorption on graphene surfaces via laser-induced oxidation. Nanoscale Advances, 3(7), 2065-2074.

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Refolding and Purification of pMHC Complexes

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The wild type or H74A mutant of HLA-A2 heavy chain (residues 1-278) with C-terminal BirA tag and β2-microglobulin were expressed as inclusion bodies in E.coli, refolded in vitro in the presence of synthesized variants of the NY-ESO-1157-165 peptide SLLMWITQV (9V), and purified using sizeexclusion chromatography (Chen 2005 , Aleksic 2010 ). The pMHCs used in this study, as in previously reported experiments (Brodovitch 2015 , Limozin 2019) , were 9V and variants 3A, 3Y, or 9L in complex with wild-type HLA-A2, or 9V in complex with the HLA-A2 mutant H74A.
Glass surfaces were prepared as previously described (Brodovitch 2015 , Limozin 2019 ) by sequential cleaning with a mix of 70% sulfuric acid and 30% H202, coating with poly-L lysine (Sigma-Aldrich, 150,000-300,000 MW), activation with glutaraldehyde (2.5%), coupling with biotinylatedbovine serum albumin (100 µg/ml, Sigma) then neutravidin (10µg/ml), and finally coating with biotinylated pMHCs. Absolute calibration of pMHC surface density was done as previously described by labeling with an excess of Alexa Fluor 488 labeled anti-HLA antibody (Biolegend, San Diego) and fluorescence determination.

Robert P., Limozin L., Merwe A.v.d., & Bongrand P. (2020). CD8 co-receptor enhances T cell activation without any effect on initial attachment.

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Functionalized Coverslips for Actin Velocity

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Glass coverslips functionalised with both anti-CD3 antibodies and NY-ESO pMHCs were required for actin velocity quantification. 18 mm, #1.5 coverslips (Scientific Laboratory Supplies, UK) were first sterilized by extensive washing in ethanol. After drying, coverslips were coated with 20 μL of a 1:4 mix of biotinylated Bovine Serum Albumin (BSA) (Sigma Aldrich) and standard BSA (Sigma Aldrich) at concentrations of 200 μg mL⁻¹ and 800 μg mL⁻¹ respectively, followed by incubation at room temperature for 2 h. After washing 3 times in PBS, coverslips were coated with 20 μL of a 10 μg mL⁻¹ solution of streptavidin (Sigma Aldrich) followed by a further 2 h incubation. After washing, 20 μL of a 10 μg mL⁻¹ solution containing either the biotinylated anti-CD3 antibodies, OKT3 or UCHT1, or the biotinylated NY-ESO pMHC, HLA-9V and HLA-4D was placed on each coverslip as required, followed by a further incubation 2 h and washing.

Colin-York H., Javanmardi Y., Skamrahl M., Kumari S., Chang V.T., Khuon S., Taylor A., Chew T.L., Betzig E., Moeendarbary E., Cerundolo V., Eggeling C, & Fritzsche M. (2019). Cytoskeletal Control of Antigen-Dependent T Cell Activation. Cell Reports, 26(12), 3369-3379.e5.

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Peptide Binding Strength on Titanium

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Relative binding strengths of peptides onto Ti and Ti6Al4V surfaces were measured in contact mode and in a liquid medium (PBS pH 7.4) with a functionalized tip. Force measurements were taken at constant loading rates (vertical piezo-velocity of 1 μm/s). The spring constant of the tip was calibrated in the presence of PBS solution using the thermal fluctuation method and found to be approximately 18 pN/nm. For tip functionalization, the ultrasoft AFM cantilever tips (Bio lever-Olympus) were rinsed with copious amounts of Milli-Q water and then dried. In the next step, tip functionalization was performed. The AFM cantilever tips were incubated in 1 μg/mL biotinylated bovine serum albumin (BSA; Sigma Aldrich, St. Louis, MO, United States) solution in PBST, pH 7.0, at room temperature overnight, and the tip was then incubated for 30 min in 100 μg mL⁻¹ streptavidin in PBST and finally in BSA (1%) for 1 h to block the nonspecific binding sites. Thorough rinsing was performed between all steps. Biotinylated peptides were fixed on the tip prior to each measurement.

Panayotov I.V., Végh A.G., Martin M., Vladimirov B., Larroque C., Gergely C., Cuisinier F.J, & Estephan E. (2023). Improving dental epithelial junction on dental implants with bioengineered peptides. Frontiers in Bioengineering and Biotechnology, 11, 1165853.

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