precision protein streptactin hrp conjugate Search Results


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Bio-Rad streptactin hrp (bio rad)
Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using <t>StrepTactin‐HRP.</t> Protein standards (STDS) were imaged colorimetrically.
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Bio-Rad 1.54, precision protein streptactin-hrp conjugate
Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using <t>StrepTactin‐HRP.</t> Protein standards (STDS) were imaged colorimetrically.
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Bio-Rad precision proteintm streptactin hrp conjugate
Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using <t>StrepTactin‐HRP.</t> Protein standards (STDS) were imaged colorimetrically.
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Bio-Rad streptectin-hrp
Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using <t>StrepTactin‐HRP.</t> Protein standards (STDS) were imaged colorimetrically.
Streptectin Hrp, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using StrepTactin‐HRP. Protein standards (STDS) were imaged colorimetrically.

Journal: Protein Science : A Publication of the Protein Society

Article Title: Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity

doi: 10.1002/pro.5118

Figure Lengend Snippet: Cross‐linking of peptide substrate to wild‐type (WT) PRMT1 (tetramer), tetramer interface mutant (TIM)2 PRMT1 (dimer), and dimer interface mutant (DIM) PRMT1 (monomer). The biotinylated H421 peptide substrate was crosslinked to WT, TIM2, or DIM PRMT1 using glutaraldehyde and samples were separated using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride. The blot was probed for biotin using StrepTactin‐HRP. Protein standards (STDS) were imaged colorimetrically.

Article Snippet: The membrane was probed with 1:5000 precision protein StrepTactin‐HRP (Bio‐Rad) in 5% BSA in 1× TTBS.

Techniques: Mutagenesis, Polyacrylamide Gel Electrophoresis