k-252b Search Results


80
Santa Cruz Biotechnology k 252b
K 252b, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/k-252b/pm09282920-69-9-16?v=Santa+Cruz+Biotechnology
Average 80 stars, based on 1 article reviews
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90
Microm International GmbH pkc inhibitors k252a
Pkc Inhibitors K252a, supplied by Microm International GmbH, 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/k-252b/pmc01131600-5-5-27?v=Microm+International+GmbH
Average 90 stars, based on 1 article reviews
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90
Biozol Diagnostica Vertrieb GmbH k252b (cas no: 99570-78-2)
Reelin protein levels are reduced in cultured cerebellar neurons after inhibition of ecto-phosphorylation. ( a ) Schematic representation of the protein backbone of full-length Reelin (R-450) and its proteolytic fragments N-R6, N-R2, R3-8, R3-6 and R7-8 after N- and C-terminal processing by ADAMTS-4. Serine 1283 (circle) and the putative CK2 phosphorylation site SDGD in murine Reelin are indicated. ( b ) Supernatants of cultured cerebellar neurons were subjected to immunoprecipitation (IP) with Reelin antibody G10 or non-immune control antibody (Ig) followed by immunoblot analysis of the immunoprecipitates with a phospho-serine antibody (pSer). Full-length Reelin (R-450) and its fragments N-R6 and N-R2 are indicated. ( c, d ) Cultures of cerebellar neurons were treated with the CK2-specific inhibitor TBB or with the cell-impermeable broad-spectrum ecto-protein kinase inhibitor <t>K252b.</t> Cell lysates ( c ) and culture supernatants ( d ) were subjected to immunoblot analysis with Reelin antibody G10. GAPDH antibody was used to control loading of cell lysates. Representative immunoblots are shown. Lanes not adjacent to each other but from the same blot are separated by a vertical line. ( e ) Quantification of Reelin levels in cell lysates and cell culture supernatants. Mean values + SD from 4 independent experiments are shown for Reelin levels after TBB or K252b treatment relative to control treatment (set to 100%) (*p<0.05; Kruskal-Wallis One Way Analysis of Variance on Ranks with Dunn’s Multiple Comparison Test). ( f ) Wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were subjected to in vitro phosphorylation using CK2 and radioactive ATP followed by blotting and analysis using a Phosphor-Imager. Diffuse signals and one distinct band with radiolabeled, phosphorylated proteins were observed (left panel). Full-length Reelin (R-450) and its serine 1283-containing fragments N-R6, R3-6 and R3-8 are indicated. Similar amounts of wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were detected by immunoblot analysis with Reelin antibody G10 (right panel), showing that equal amounts of wild-type and mutated Reelin were used for in vitro phosphorylation. A grey arrow points to an additional band, which could not be assigned to one of the known Reelin forms.
K252b (Cas No: 99570 78 2), supplied by Biozol Diagnostica Vertrieb GmbH, 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/k-252b/bio_rxiv__2022__01__06__474241-191-13-19?v=Biozol+Diagnostica+Vertrieb+GmbH
Average 90 stars, based on 1 article reviews
k252b (cas no: 99570-78-2) - by Bioz Stars, 2026-08
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86
Kyowa Hakko Kirin Korea Co Ltd k 252b
Reelin protein levels are reduced in cultured cerebellar neurons after inhibition of ecto-phosphorylation. ( a ) Schematic representation of the protein backbone of full-length Reelin (R-450) and its proteolytic fragments N-R6, N-R2, R3-8, R3-6 and R7-8 after N- and C-terminal processing by ADAMTS-4. Serine 1283 (circle) and the putative CK2 phosphorylation site SDGD in murine Reelin are indicated. ( b ) Supernatants of cultured cerebellar neurons were subjected to immunoprecipitation (IP) with Reelin antibody G10 or non-immune control antibody (Ig) followed by immunoblot analysis of the immunoprecipitates with a phospho-serine antibody (pSer). Full-length Reelin (R-450) and its fragments N-R6 and N-R2 are indicated. ( c, d ) Cultures of cerebellar neurons were treated with the CK2-specific inhibitor TBB or with the cell-impermeable broad-spectrum ecto-protein kinase inhibitor <t>K252b.</t> Cell lysates ( c ) and culture supernatants ( d ) were subjected to immunoblot analysis with Reelin antibody G10. GAPDH antibody was used to control loading of cell lysates. Representative immunoblots are shown. Lanes not adjacent to each other but from the same blot are separated by a vertical line. ( e ) Quantification of Reelin levels in cell lysates and cell culture supernatants. Mean values + SD from 4 independent experiments are shown for Reelin levels after TBB or K252b treatment relative to control treatment (set to 100%) (*p<0.05; Kruskal-Wallis One Way Analysis of Variance on Ranks with Dunn’s Multiple Comparison Test). ( f ) Wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were subjected to in vitro phosphorylation using CK2 and radioactive ATP followed by blotting and analysis using a Phosphor-Imager. Diffuse signals and one distinct band with radiolabeled, phosphorylated proteins were observed (left panel). Full-length Reelin (R-450) and its serine 1283-containing fragments N-R6, R3-6 and R3-8 are indicated. Similar amounts of wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were detected by immunoblot analysis with Reelin antibody G10 (right panel), showing that equal amounts of wild-type and mutated Reelin were used for in vitro phosphorylation. A grey arrow points to an additional band, which could not be assigned to one of the known Reelin forms.
K 252b, supplied by Kyowa Hakko Kirin Korea Co Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/k-252b/pm10374923-56-2-9?v=Kyowa+Hakko+Kirin+Korea+Co+Ltd
Average 86 stars, based on 1 article reviews
k 252b - by Bioz Stars, 2026-08
86/100 stars
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N/A
K252b (#K-170) is a highly pure, natural, and biologically active compound.
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N/A
K252b is an indolocarbazole isolated from the actinomycete Nocardiopsis first described as an inhibitor of protein kinase C However as this compound does not freely pass through the cell membrane it is used to inhibit
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N/A
A staurosporine analogue isolated from a nocardiopsis strain; a potent inhibitor of protein kinase C. K-252b exhibits potent antitumour activity but shows no antimicrobial activity in vitro, or in vivo toxicity in rodents; also active
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N/A
Inhibitor of ectokinase. Inhibitor of ectokinase.
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Image Search Results


Reelin protein levels are reduced in cultured cerebellar neurons after inhibition of ecto-phosphorylation. ( a ) Schematic representation of the protein backbone of full-length Reelin (R-450) and its proteolytic fragments N-R6, N-R2, R3-8, R3-6 and R7-8 after N- and C-terminal processing by ADAMTS-4. Serine 1283 (circle) and the putative CK2 phosphorylation site SDGD in murine Reelin are indicated. ( b ) Supernatants of cultured cerebellar neurons were subjected to immunoprecipitation (IP) with Reelin antibody G10 or non-immune control antibody (Ig) followed by immunoblot analysis of the immunoprecipitates with a phospho-serine antibody (pSer). Full-length Reelin (R-450) and its fragments N-R6 and N-R2 are indicated. ( c, d ) Cultures of cerebellar neurons were treated with the CK2-specific inhibitor TBB or with the cell-impermeable broad-spectrum ecto-protein kinase inhibitor K252b. Cell lysates ( c ) and culture supernatants ( d ) were subjected to immunoblot analysis with Reelin antibody G10. GAPDH antibody was used to control loading of cell lysates. Representative immunoblots are shown. Lanes not adjacent to each other but from the same blot are separated by a vertical line. ( e ) Quantification of Reelin levels in cell lysates and cell culture supernatants. Mean values + SD from 4 independent experiments are shown for Reelin levels after TBB or K252b treatment relative to control treatment (set to 100%) (*p<0.05; Kruskal-Wallis One Way Analysis of Variance on Ranks with Dunn’s Multiple Comparison Test). ( f ) Wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were subjected to in vitro phosphorylation using CK2 and radioactive ATP followed by blotting and analysis using a Phosphor-Imager. Diffuse signals and one distinct band with radiolabeled, phosphorylated proteins were observed (left panel). Full-length Reelin (R-450) and its serine 1283-containing fragments N-R6, R3-6 and R3-8 are indicated. Similar amounts of wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were detected by immunoblot analysis with Reelin antibody G10 (right panel), showing that equal amounts of wild-type and mutated Reelin were used for in vitro phosphorylation. A grey arrow points to an additional band, which could not be assigned to one of the known Reelin forms.

Journal: bioRxiv

Article Title: Serine 1283 in extracellular matrix glycoprotein Reelin is crucial for Reelin’s function in brain development

doi: 10.1101/2022.01.06.474241

Figure Lengend Snippet: Reelin protein levels are reduced in cultured cerebellar neurons after inhibition of ecto-phosphorylation. ( a ) Schematic representation of the protein backbone of full-length Reelin (R-450) and its proteolytic fragments N-R6, N-R2, R3-8, R3-6 and R7-8 after N- and C-terminal processing by ADAMTS-4. Serine 1283 (circle) and the putative CK2 phosphorylation site SDGD in murine Reelin are indicated. ( b ) Supernatants of cultured cerebellar neurons were subjected to immunoprecipitation (IP) with Reelin antibody G10 or non-immune control antibody (Ig) followed by immunoblot analysis of the immunoprecipitates with a phospho-serine antibody (pSer). Full-length Reelin (R-450) and its fragments N-R6 and N-R2 are indicated. ( c, d ) Cultures of cerebellar neurons were treated with the CK2-specific inhibitor TBB or with the cell-impermeable broad-spectrum ecto-protein kinase inhibitor K252b. Cell lysates ( c ) and culture supernatants ( d ) were subjected to immunoblot analysis with Reelin antibody G10. GAPDH antibody was used to control loading of cell lysates. Representative immunoblots are shown. Lanes not adjacent to each other but from the same blot are separated by a vertical line. ( e ) Quantification of Reelin levels in cell lysates and cell culture supernatants. Mean values + SD from 4 independent experiments are shown for Reelin levels after TBB or K252b treatment relative to control treatment (set to 100%) (*p<0.05; Kruskal-Wallis One Way Analysis of Variance on Ranks with Dunn’s Multiple Comparison Test). ( f ) Wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were subjected to in vitro phosphorylation using CK2 and radioactive ATP followed by blotting and analysis using a Phosphor-Imager. Diffuse signals and one distinct band with radiolabeled, phosphorylated proteins were observed (left panel). Full-length Reelin (R-450) and its serine 1283-containing fragments N-R6, R3-6 and R3-8 are indicated. Similar amounts of wild-type Reelin (Reelin WT ) and S/A 1283 -mutated Reelin (Reelin S/A ) were detected by immunoblot analysis with Reelin antibody G10 (right panel), showing that equal amounts of wild-type and mutated Reelin were used for in vitro phosphorylation. A grey arrow points to an additional band, which could not be assigned to one of the known Reelin forms.

Article Snippet: The CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB; CAS 17374-26-4) was from Santa Cruz Biotechnology and K252b (CAS No: 99570-78-2) was from Biozol (Eching, Germany).

Techniques: Cell Culture, Inhibition, Immunoprecipitation, Western Blot, In Vitro