hand casted acrylamide sds page gradient gel Search Results


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Bio-Rad acrylamide monodimensional mini gels
Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% <t>acrylamide)</t> of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.
Acrylamide Monodimensional Mini Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad hand casted sds page gel
Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% <t>acrylamide)</t> of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.
Hand Casted Sds Page Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad hand cast acrylamide
Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% <t>acrylamide)</t> of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.
Hand Cast Acrylamide, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad tgx stain free fastcast acrylamide starter kit
Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% <t>acrylamide)</t> of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.
Tgx Stain Free Fastcast Acrylamide Starter Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad tgx stain free fastcast acrylamide kit
Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% <t>acrylamide)</t> of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.
Tgx Stain Free Fastcast Acrylamide Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hand+casted+acrylamide+sds+page+gradient+gel/pmc11687396-82-36-41?v=Bio-Rad
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tgx stain free fastcast acrylamide kit - by Bioz Stars, 2026-08
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Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% acrylamide) of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.

Journal: FEBS open bio

Article Title: Molecular characterization of accripin11, a soluble shell protein with an acidic C-terminus, identified in the prismatic layer of the Mediterranean fan mussel Pinna nobilis (Bivalvia, Pteriomorphia).

doi: 10.1002/2211-5463.13497

Figure Lengend Snippet: Fig. 5. Purification of overexpressed accripin11 by preparative gel electrophoresis. (A) Dot blot of the first 48 fractions eluted from two batches of preparative SDS/PAGE. The dots were stained with the anti-strepTag2 antibody. Tubes 23–26 from 1st batch and tubes 24–27 from 2nd batch (boxed in black) were pooled, respectively. (B) Silver-stained SDS/PAGE gel (15% acrylamide) of pooled tubes of 1st batch (lane 2) and of 2nd batch (lane 3). Lane 1 is molecular weight standards and lane 4, partially purified accripin11. (C) Western blot (12% acry- lamide) of pooled fractions of the two batches stained with anti-strepTag2 antibody (lane 2 and 3 for 1st and 2nd batch, respectively). Lane 1, molecular weight standards, same as for B.

Article Snippet: ASMs and LSAIMs were run on hand-casted 15% acrylamide monodimensional mini-gels (Bio-Rad Laboratories, Hercules, CA, USA) according to the manufacturer’s instructions.

Techniques: Nucleic Acid Electrophoresis, Dot Blot, SDS Page, Staining, Molecular Weight, Western Blot

Fig. 6. Presence of accripin11 in different shell extracts. (A) SDS/PAGE. (B) Western blot. A and B correspond to 15% acrylamide gels. In A and B, the samples occupy the same lanes; lane 1: molecular weight standards; lane 2: ASMn; lane 3: AIMn; lane 4: ASMp1; lane 5: AIMp1; lane 6: purified accripin11. The western blot was incubated with anti-accripin11. Note that the recombinant purified accripin11 tends to degrade in a component of lower molecular weight, visualized by the antibody. The dashed lines between lane 5 and 6 in A and between lanes 3, 4, 5 and 6 in B indicate that the lanes were spliced together. (C) ELISA test of ASMn, ASMp1 and accripin11 with serial dilutions of anti-accripin11 antibody serum ranging from 5009 to 64 0009. Absorbance values at 405 nm were normalized to highest value (accripin11, 5009 dilution antibody) corresponding to 100% reactivity.

Journal: FEBS open bio

Article Title: Molecular characterization of accripin11, a soluble shell protein with an acidic C-terminus, identified in the prismatic layer of the Mediterranean fan mussel Pinna nobilis (Bivalvia, Pteriomorphia).

doi: 10.1002/2211-5463.13497

Figure Lengend Snippet: Fig. 6. Presence of accripin11 in different shell extracts. (A) SDS/PAGE. (B) Western blot. A and B correspond to 15% acrylamide gels. In A and B, the samples occupy the same lanes; lane 1: molecular weight standards; lane 2: ASMn; lane 3: AIMn; lane 4: ASMp1; lane 5: AIMp1; lane 6: purified accripin11. The western blot was incubated with anti-accripin11. Note that the recombinant purified accripin11 tends to degrade in a component of lower molecular weight, visualized by the antibody. The dashed lines between lane 5 and 6 in A and between lanes 3, 4, 5 and 6 in B indicate that the lanes were spliced together. (C) ELISA test of ASMn, ASMp1 and accripin11 with serial dilutions of anti-accripin11 antibody serum ranging from 5009 to 64 0009. Absorbance values at 405 nm were normalized to highest value (accripin11, 5009 dilution antibody) corresponding to 100% reactivity.

Article Snippet: ASMs and LSAIMs were run on hand-casted 15% acrylamide monodimensional mini-gels (Bio-Rad Laboratories, Hercules, CA, USA) according to the manufacturer’s instructions.

Techniques: SDS Page, Western Blot, Molecular Weight, Incubation, Recombinant, Enzyme-linked Immunosorbent Assay