<p>The same gel was first stained with Coomassie Brilliant Blue (CBB, left) and then with silver (right). The molecular weight of marker proteins is given in kDa.</p
<p>A) Native PAGE analysis of BS<sup>3</sup> conjugated pC1-inh (lane 1), pC1-inh (lane 2) and nativ...
<p>The highly abundant proteins myosin-Ig, α-actinin-4 and cytoplasmic actin 1 bound to the 4-AH-cCM...
Gel electrophoresis, particularly one-dimensional electrophoresis (1DE) and two-dimensional electrop...
<p>A and B. Coomasie blue stained gel. Lane M in A and B are protein molecular weight markers and th...
<p><i>Lanes 1–8,</i> eight bands of proteins with the apparent molecular masses of 150 (SSCL-150), 1...
<p>AKFV33 structural proteins (Lane 2) alongside the standard marker (Lane1) separated on 10% SDS-PA...
<p>(A) Coomassie Blue stained SDS-PAGE gel of monomer proteins. Lane 1: Molecular weight marker prot...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>The four gels show (A) molecular weight markers, with molecular weights given in KDa, (B) the Ext...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>Replicates (A and B) of proteins extracted from cells exposed to UV or darkness, electrophoresed ...
Left gel was stained by Coomassie blue and the right gel by silver staining technique. Lane A, cytos...
<p>The 2D gel resolved by isoelectricfocusing in the first dimension (pH range 3–10) followed by SDS...
<p>Two-dimensional separation of the serum proteomes of controls (left) and heroin addicts (right) w...
<p>SDS-PAGE was performed on 10% polyacrylamide gels; 10 µg protein content was loaded in each lane....
<p>A) Native PAGE analysis of BS<sup>3</sup> conjugated pC1-inh (lane 1), pC1-inh (lane 2) and nativ...
<p>The highly abundant proteins myosin-Ig, α-actinin-4 and cytoplasmic actin 1 bound to the 4-AH-cCM...
Gel electrophoresis, particularly one-dimensional electrophoresis (1DE) and two-dimensional electrop...
<p>A and B. Coomasie blue stained gel. Lane M in A and B are protein molecular weight markers and th...
<p><i>Lanes 1–8,</i> eight bands of proteins with the apparent molecular masses of 150 (SSCL-150), 1...
<p>AKFV33 structural proteins (Lane 2) alongside the standard marker (Lane1) separated on 10% SDS-PA...
<p>(A) Coomassie Blue stained SDS-PAGE gel of monomer proteins. Lane 1: Molecular weight marker prot...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>The four gels show (A) molecular weight markers, with molecular weights given in KDa, (B) the Ext...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>Replicates (A and B) of proteins extracted from cells exposed to UV or darkness, electrophoresed ...
Left gel was stained by Coomassie blue and the right gel by silver staining technique. Lane A, cytos...
<p>The 2D gel resolved by isoelectricfocusing in the first dimension (pH range 3–10) followed by SDS...
<p>Two-dimensional separation of the serum proteomes of controls (left) and heroin addicts (right) w...
<p>SDS-PAGE was performed on 10% polyacrylamide gels; 10 µg protein content was loaded in each lane....
<p>A) Native PAGE analysis of BS<sup>3</sup> conjugated pC1-inh (lane 1), pC1-inh (lane 2) and nativ...
<p>The highly abundant proteins myosin-Ig, α-actinin-4 and cytoplasmic actin 1 bound to the 4-AH-cCM...
Gel electrophoresis, particularly one-dimensional electrophoresis (1DE) and two-dimensional electrop...
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