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TEFCO Inc colloidal cbb staining kit
Colloidal Cbb Staining Kit, supplied by TEFCO Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/colloidal+cbb+staining+kit/colloidal+cbb+staining+kit/pm40524331-91-6-10
Average 90 stars, based on 1 article reviews
colloidal cbb staining kit - by Bioz Stars, 2026-09
90/100 stars

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Nucleic Acid Electrophoresis:

Article Title: Pre-ribosomal WDR74 module coordinates the early and late pre-rRNA processing stages for the NVL2-mediated regulation of 60S ribosome biogenesis.
Article Snippet: WD repeat domain 74 (WDR74) is a nucleolar protein involved in the early stages of pre-60S maturation in the ribosome biogenesis pathway.. In later stages, WDR74 interacts with MTR4, an RNA helicase that functions with the exosome nuclease complex, and is dissociated upon ATP hydrolysis by the chaperone-like nuclear VCP-like 2 (NVL2) AAA-ATPase.. We previously reported that ATP hydrolysis-defective NVL2 causes aberrant accumulation of WDR74 on the MTR4–exosome complex at the nucleolar periphery and in the nucleoplasm and that this nuclear redistribution of WDR74 leads to the unusual cleavage of the early rRNA precursor within the internal transcribed spacer 1 sequence.

Acrylamide Gel Assay:

Article Title: Pre-ribosomal WDR74 module coordinates the early and late pre-rRNA processing stages for the NVL2-mediated regulation of 60S ribosome biogenesis.
Article Snippet: WD repeat domain 74 (WDR74) is a nucleolar protein involved in the early stages of pre-60S maturation in the ribosome biogenesis pathway.. In later stages, WDR74 interacts with MTR4, an RNA helicase that functions with the exosome nuclease complex, and is dissociated upon ATP hydrolysis by the chaperone-like nuclear VCP-like 2 (NVL2) AAA-ATPase.. We previously reported that ATP hydrolysis-defective NVL2 causes aberrant accumulation of WDR74 on the MTR4–exosome complex at the nucleolar periphery and in the nucleoplasm and that this nuclear redistribution of WDR74 leads to the unusual cleavage of the early rRNA precursor within the internal transcribed spacer 1 sequence.

Staining:

Article Title: Pre-ribosomal WDR74 module coordinates the early and late pre-rRNA processing stages for the NVL2-mediated regulation of 60S ribosome biogenesis.
Article Snippet: WD repeat domain 74 (WDR74) is a nucleolar protein involved in the early stages of pre-60S maturation in the ribosome biogenesis pathway.. In later stages, WDR74 interacts with MTR4, an RNA helicase that functions with the exosome nuclease complex, and is dissociated upon ATP hydrolysis by the chaperone-like nuclear VCP-like 2 (NVL2) AAA-ATPase.. We previously reported that ATP hydrolysis-defective NVL2 causes aberrant accumulation of WDR74 on the MTR4–exosome complex at the nucleolar periphery and in the nucleoplasm and that this nuclear redistribution of WDR74 leads to the unusual cleavage of the early rRNA precursor within the internal transcribed spacer 1 sequence.

Article Title: Enzymatic sulfation of coelenterazine by human cytosolic aryl sulfotransferase SULT1A1: identification of coelenterazine C2-benzyl monosulfate by LC/ESI-TOF-MS.
Article Snippet: Coelenterazine (CTZ) is known as a light-emitting source for the bioluminescence reaction in marine organisms.. CTZ has two phenolic hydroxy groups at the C2-benzyl and C6-phenyl positions, and a ketoenol type hydroxy group at the C3-position in the core structure of imidazopyrazinone (1⁄4 3,7dihydroimidazopyrazin-3-one).. These hydroxy groups in CTZ could be sulfated by sulfotransferase(s), and the sulfates of Watasenia luciferin (CTZ disulfate at the C2and C6-positions) and Renilla preluciferin (CTZ 3-enol sulfate) have been identified in marine organisms.

Article Title: Reverse mutants of the catalytic 19 kDa mutant protein (nanoKAZ/nanoLuc) from Oplophorus luciferase with coelenterazine as preferred substrate
Article Snippet: .. SDS-PAGE analysis was carried out under reducing conditions using a 12% separation gel (TEFCO, Tokyo, Japan) and the gel was stained with a colloidal CBB staining kit (TEFCO). .. The protein concentrations of nanoKAZ, QL-nanoKAZ, SNH-nanoKAZ, GLase, and aequorin were determined by amino acid composition analysis, as previously described [ ], and other luciferases were determined by the dye-binding method using a commercially available kit (Bio-Rad, Richmond, CA, USA) and bovine serum albumin as a standard (Pierce, Rockford, IL, USA).

Article Title: Evaluation of the disulfide bond positions in recombinant Gaussia luciferase expressed in Escherichia coli cells by site-directed mutagenesis.
Article Snippet: The luciferase (GLase) from the mesopelagic copepod Gaussia princeps (T. Scott) catalyzes the oxidation of coelenterazine (luciferin) with O2, and emits bluegreen light (λmax = 480 nm), 1,2 accompanied by the production of coelenteramide (oxyluciferin) and CO2.. 3 Although the native GLase protein has not been purified from G. princeps specimens, its complementary DNA (cDNA) has been successfully identified through expression cloning in Escherichia coli cells.4 GLase is a single polypeptide chain consisting of a 17amino acid signal peptide sequence for Received: 4 March 2025 | Revised: 24 April 2025 | Accepted: 29 May 2025 DOI: 10.1111/php.70003

Article Title: A fusion protein of the synthetic IgG-binding domain and aequorin: Expression and purification from E. coli cells and its application.
Article Snippet: Aequorin is a Ca2þ-binding photoprotein that is a complex of apoaequorin (apoAQ) and 2peroxycoelenterazine.. In this study, the fusion protein (ZZ-apoAQ) composed of the synthetic IgGbinding domain (ZZ domain) derived from Staphylococcus aureus protein A and apoAQ was expressed into the periplasmic space of Escherichia coli cells.. ZZ-apoAQ was highly purified using Ni-chelate affinity chromatography followed by IgG affinity chromatography.

Article Title: Expression, purification, and characterization of recombinant apoPholasin.
Article Snippet: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record.. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article.. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Article Title: Immunogenic composition
Article Snippet: A sampling buffer for gel electrophoresis (manufactured by TEFCO) was added to the CEA precipitate, and the precipitate was dissolved therein at 95° C. for 3 minutes, followed by performing gel electrophoresis using polyacrylamide gel (manufactured by TEFCO). .. Thereafter, the gel was stained using colloidal CBB staining kit (manufactured by TEFCO), and the rate of encapsulation of CEA into the particles was calculated. ..

Electrophoresis:

Article Title: Enzymatic sulfation of coelenterazine by human cytosolic aryl sulfotransferase SULT1A1: identification of coelenterazine C2-benzyl monosulfate by LC/ESI-TOF-MS.
Article Snippet: Coelenterazine (CTZ) is known as a light-emitting source for the bioluminescence reaction in marine organisms.. CTZ has two phenolic hydroxy groups at the C2-benzyl and C6-phenyl positions, and a ketoenol type hydroxy group at the C3-position in the core structure of imidazopyrazinone (1⁄4 3,7dihydroimidazopyrazin-3-one).. These hydroxy groups in CTZ could be sulfated by sulfotransferase(s), and the sulfates of Watasenia luciferin (CTZ disulfate at the C2and C6-positions) and Renilla preluciferin (CTZ 3-enol sulfate) have been identified in marine organisms.

SDS Page:

Article Title: Reverse mutants of the catalytic 19 kDa mutant protein (nanoKAZ/nanoLuc) from Oplophorus luciferase with coelenterazine as preferred substrate
Article Snippet: .. SDS-PAGE analysis was carried out under reducing conditions using a 12% separation gel (TEFCO, Tokyo, Japan) and the gel was stained with a colloidal CBB staining kit (TEFCO). .. The protein concentrations of nanoKAZ, QL-nanoKAZ, SNH-nanoKAZ, GLase, and aequorin were determined by amino acid composition analysis, as previously described [ ], and other luciferases were determined by the dye-binding method using a commercially available kit (Bio-Rad, Richmond, CA, USA) and bovine serum albumin as a standard (Pierce, Rockford, IL, USA).

Article Title: A fusion protein of the synthetic IgG-binding domain and aequorin: Expression and purification from E. coli cells and its application.
Article Snippet: Aequorin is a Ca2þ-binding photoprotein that is a complex of apoaequorin (apoAQ) and 2peroxycoelenterazine.. In this study, the fusion protein (ZZ-apoAQ) composed of the synthetic IgGbinding domain (ZZ domain) derived from Staphylococcus aureus protein A and apoAQ was expressed into the periplasmic space of Escherichia coli cells.. ZZ-apoAQ was highly purified using Ni-chelate affinity chromatography followed by IgG affinity chromatography.

Article Title: Expression, purification, and characterization of recombinant apoPholasin.
Article Snippet: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record.. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article.. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Article Title: A Novel Catalytic Function of Synthetic IgG-Binding Domain (Z Domain) from Staphylococcal Protein A: Light Emission with Coelenterazine.
Article Snippet: The synthetic IgG-binding domain (Z domain) of staphylococcal protein A has a catalytic function to oxidize coelenterazine to emit light like a coelenterazine-utilizing luciferase.. The Z domain derivatives (ZZ-gCys, Z-gCys and Z-domain) were purified and the luminescence properties were characterized by comparing with coelenterazine-utilizing luciferases, including Renilla luciferase, Gaussia luciferase and the catalytic domain of Oplophorus luciferase.. Three Z domain derivatives showed luminescence activity with coelenterazine and the order of the initial maximum intensity of luminescence was ZZ-gCys (100%) > Z-gCys (36.8%) > Z-domain (1.1%) > bovine serum albumin (0.9%) > staphylococcal protein A (0.1%) and the background value of coelenterazine (0.1%) in our conditions.

Western Blot:

Article Title: Expression, purification, and characterization of recombinant apoPholasin.
Article Snippet: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record.. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article.. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Encapsulation:

Article Title: Immunogenic composition
Article Snippet: A sampling buffer for gel electrophoresis (manufactured by TEFCO) was added to the CEA precipitate, and the precipitate was dissolved therein at 95° C. for 3 minutes, followed by performing gel electrophoresis using polyacrylamide gel (manufactured by TEFCO). .. Thereafter, the gel was stained using colloidal CBB staining kit (manufactured by TEFCO), and the rate of encapsulation of CEA into the particles was calculated. ..



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