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calmodulin  (Sino Biological)
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Sino Biological calmodulin
(A) CamKK2 activity in A549 cells with GDH1 knockdown in the presence or absence of α-KG. A549 cells were cultured under detached conditions with methyl-α-KG prior to CamKK2 immunoprecipitation and kinase assay using AMPKα as a substrate. ADP-glo assay (left) and western blot of p-AMPKα T172 (right) were used to determine kinase activity of CamKK2. (B) Effect of transient CamKK2 knockout on AMPK activation and anoikis induction in LKB1 null or LKB1 wt cells. Anoikis and AMPK activity were assessed by annexin V staining and western blot analysis of p-T172 AMPKα, respectively. (C) Effect of flag-CamKK2 expression on AMPK activity and anoikis induction in LKB1 null cells with GDH1 knockdown. Detached cells with GDH1 knockdown were overexpressed with flag-CamKK2. (D) A549 with empty vector or GDH1 shRNA were treated with increasing concentrations of STO-609 and cultured under detached conditions. Anoikis induction and AMPK activation were assessed as in (B) for (C) and (D). (E) Metabolite-protein binding assay. Purified GST-CamKK2 (left) or flag-AMPKα (right) from transfected 293T cells were incubated with radiolabeled α-KG or fumarate. CamKK2 or AMPKα bound α-KG or fumarate was quantified by scintillation counting. (F) Cellular thermal shift assay using flag-CamKK2 purified from 293T cells treated without or with dimethyl-α-KG or -fumarate. (G) α-KG enhances AMPK binding to CamKK2 in cells. Flag-CamKK2 was enriched from 293T cells treated with or without dimethyl-α-KG and CamKK2 bound endogenous AMPKα was detected by western blot. (H) α-KG enhances AMPK binding to CamKK2 in vitro. Bead-bound GST-CamKK2 was incubated with recombinant AMPKα and <t>calmodulin</t> in the presence of increasing concentrations of α-KG. Unbound proteins were washed away and retained AMPKα or calmodulin were assayed by western blot. Data are mean ± SD of three technical replicates and are representative of three (A-D) or two (E-H) independent biological experiments. p values were determined by a two-tailed Student’s t test (ns: not significant; **: p < 0.01). See also Figure S5.
Calmodulin, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ca2+calmodulin+solution+c02+39/pmc05777230-53-0-2?v=Sino+Biological
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calmodulin - by Bioz Stars, 2026-07
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ca2 calmodulin solution ii  (Sino Biological)
93
Sino Biological ca2 calmodulin solution ii
(A) CamKK2 activity in A549 cells with GDH1 knockdown in the presence or absence of α-KG. A549 cells were cultured under detached conditions with methyl-α-KG prior to CamKK2 immunoprecipitation and kinase assay using AMPKα as a substrate. ADP-glo assay (left) and western blot of p-AMPKα T172 (right) were used to determine kinase activity of CamKK2. (B) Effect of transient CamKK2 knockout on AMPK activation and anoikis induction in LKB1 null or LKB1 wt cells. Anoikis and AMPK activity were assessed by annexin V staining and western blot analysis of p-T172 AMPKα, respectively. (C) Effect of flag-CamKK2 expression on AMPK activity and anoikis induction in LKB1 null cells with GDH1 knockdown. Detached cells with GDH1 knockdown were overexpressed with flag-CamKK2. (D) A549 with empty vector or GDH1 shRNA were treated with increasing concentrations of STO-609 and cultured under detached conditions. Anoikis induction and AMPK activation were assessed as in (B) for (C) and (D). (E) Metabolite-protein binding assay. Purified GST-CamKK2 (left) or flag-AMPKα (right) from transfected 293T cells were incubated with radiolabeled α-KG or fumarate. CamKK2 or AMPKα bound α-KG or fumarate was quantified by scintillation counting. (F) Cellular thermal shift assay using flag-CamKK2 purified from 293T cells treated without or with dimethyl-α-KG or -fumarate. (G) α-KG enhances AMPK binding to CamKK2 in cells. Flag-CamKK2 was enriched from 293T cells treated with or without dimethyl-α-KG and CamKK2 bound endogenous AMPKα was detected by western blot. (H) α-KG enhances AMPK binding to CamKK2 in vitro. Bead-bound GST-CamKK2 was incubated with recombinant AMPKα and <t>calmodulin</t> in the presence of increasing concentrations of α-KG. Unbound proteins were washed away and retained AMPKα or calmodulin were assayed by western blot. Data are mean ± SD of three technical replicates and are representative of three (A-D) or two (E-H) independent biological experiments. p values were determined by a two-tailed Student’s t test (ns: not significant; **: p < 0.01). See also Figure S5.
Ca2 Calmodulin Solution Ii, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ca2+calmodulin+solution+c02+39/pm35184394-113-8-14?v=Sino+Biological
Average 93 stars, based on 1 article reviews
ca2 calmodulin solution ii - by Bioz Stars, 2026-07
93/100 stars
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(A) CamKK2 activity in A549 cells with GDH1 knockdown in the presence or absence of α-KG. A549 cells were cultured under detached conditions with methyl-α-KG prior to CamKK2 immunoprecipitation and kinase assay using AMPKα as a substrate. ADP-glo assay (left) and western blot of p-AMPKα T172 (right) were used to determine kinase activity of CamKK2. (B) Effect of transient CamKK2 knockout on AMPK activation and anoikis induction in LKB1 null or LKB1 wt cells. Anoikis and AMPK activity were assessed by annexin V staining and western blot analysis of p-T172 AMPKα, respectively. (C) Effect of flag-CamKK2 expression on AMPK activity and anoikis induction in LKB1 null cells with GDH1 knockdown. Detached cells with GDH1 knockdown were overexpressed with flag-CamKK2. (D) A549 with empty vector or GDH1 shRNA were treated with increasing concentrations of STO-609 and cultured under detached conditions. Anoikis induction and AMPK activation were assessed as in (B) for (C) and (D). (E) Metabolite-protein binding assay. Purified GST-CamKK2 (left) or flag-AMPKα (right) from transfected 293T cells were incubated with radiolabeled α-KG or fumarate. CamKK2 or AMPKα bound α-KG or fumarate was quantified by scintillation counting. (F) Cellular thermal shift assay using flag-CamKK2 purified from 293T cells treated without or with dimethyl-α-KG or -fumarate. (G) α-KG enhances AMPK binding to CamKK2 in cells. Flag-CamKK2 was enriched from 293T cells treated with or without dimethyl-α-KG and CamKK2 bound endogenous AMPKα was detected by western blot. (H) α-KG enhances AMPK binding to CamKK2 in vitro. Bead-bound GST-CamKK2 was incubated with recombinant AMPKα and calmodulin in the presence of increasing concentrations of α-KG. Unbound proteins were washed away and retained AMPKα or calmodulin were assayed by western blot. Data are mean ± SD of three technical replicates and are representative of three (A-D) or two (E-H) independent biological experiments. p values were determined by a two-tailed Student’s t test (ns: not significant; **: p < 0.01). See also Figure S5.

Journal: Molecular cell

Article Title: The PLAG1-GDH1 axis promotes anoikis resistance and tumor metastasis through CamKK2-AMPK signaling in LKB1-deficient lung cancer

doi: 10.1016/j.molcel.2017.11.025

Figure Lengend Snippet: (A) CamKK2 activity in A549 cells with GDH1 knockdown in the presence or absence of α-KG. A549 cells were cultured under detached conditions with methyl-α-KG prior to CamKK2 immunoprecipitation and kinase assay using AMPKα as a substrate. ADP-glo assay (left) and western blot of p-AMPKα T172 (right) were used to determine kinase activity of CamKK2. (B) Effect of transient CamKK2 knockout on AMPK activation and anoikis induction in LKB1 null or LKB1 wt cells. Anoikis and AMPK activity were assessed by annexin V staining and western blot analysis of p-T172 AMPKα, respectively. (C) Effect of flag-CamKK2 expression on AMPK activity and anoikis induction in LKB1 null cells with GDH1 knockdown. Detached cells with GDH1 knockdown were overexpressed with flag-CamKK2. (D) A549 with empty vector or GDH1 shRNA were treated with increasing concentrations of STO-609 and cultured under detached conditions. Anoikis induction and AMPK activation were assessed as in (B) for (C) and (D). (E) Metabolite-protein binding assay. Purified GST-CamKK2 (left) or flag-AMPKα (right) from transfected 293T cells were incubated with radiolabeled α-KG or fumarate. CamKK2 or AMPKα bound α-KG or fumarate was quantified by scintillation counting. (F) Cellular thermal shift assay using flag-CamKK2 purified from 293T cells treated without or with dimethyl-α-KG or -fumarate. (G) α-KG enhances AMPK binding to CamKK2 in cells. Flag-CamKK2 was enriched from 293T cells treated with or without dimethyl-α-KG and CamKK2 bound endogenous AMPKα was detected by western blot. (H) α-KG enhances AMPK binding to CamKK2 in vitro. Bead-bound GST-CamKK2 was incubated with recombinant AMPKα and calmodulin in the presence of increasing concentrations of α-KG. Unbound proteins were washed away and retained AMPKα or calmodulin were assayed by western blot. Data are mean ± SD of three technical replicates and are representative of three (A-D) or two (E-H) independent biological experiments. p values were determined by a two-tailed Student’s t test (ns: not significant; **: p < 0.01). See also Figure S5.

Article Snippet: Calmodulin , SignalChem , Cat#C02-39B-500.

Techniques: Activity Assay, Knockdown, Cell Culture, Immunoprecipitation, Kinase Assay, Glo Assay, Western Blot, Knock-Out, Activation Assay, Staining, Expressing, Plasmid Preparation, shRNA, Protein Binding, Purification, Transfection, Incubation, Thermal Shift Assay, Binding Assay, In Vitro, Recombinant, Two Tailed Test

KEY RESOURCES TABLE

Journal: Molecular cell

Article Title: The PLAG1-GDH1 axis promotes anoikis resistance and tumor metastasis through CamKK2-AMPK signaling in LKB1-deficient lung cancer

doi: 10.1016/j.molcel.2017.11.025

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Calmodulin , SignalChem , Cat#C02-39B-500.

Techniques: Recombinant, Caspase-Glo Assay, Chromatin Immunoprecipitation, ATP Bioluminescent Assay, Malate Assay, Activation Assay, Isolation, shRNA, Sequencing, Plasmid Preparation, Software, Expressing