c terminal ddk Search Results


90
GenScript corporation pcmv6-ddk-scyl3 full length (scyl3-fl) and ddk-scyl3 c-terminal deletion of ezrin binding domain (scyl3-δc): 465-688 a.a.
Pcmv6 Ddk Scyl3 Full Length (Scyl3 Fl) And Ddk Scyl3 C Terminal Deletion Of Ezrin Binding Domain (Scyl3 δc): 465 688 A.A., supplied by GenScript corporation, 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/c+terminal+ddk/ddk+scyl3+c+terminal+deletion+of+ezrin+binding+domain++scyl3+%CE%B4c+/pmc09691429__mmc1-38-14-19
Average 90 stars, based on 1 article reviews
pcmv6-ddk-scyl3 full length (scyl3-fl) and ddk-scyl3 c-terminal deletion of ezrin binding domain (scyl3-δc): 465-688 a.a. - by Bioz Stars, 2026-09
90/100 stars
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90
GenScript corporation c-terminal tagged clone of human mprip (ddk (flag)
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
C Terminal Tagged Clone Of Human Mprip (Ddk (Flag), supplied by GenScript corporation, 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/c+terminal+ddk/c+terminal+tagged+clone+of+human+mprip++ddk++flag+/pmc10591482-208-5-9
Average 90 stars, based on 1 article reviews
c-terminal tagged clone of human mprip (ddk (flag) - by Bioz Stars, 2026-09
90/100 stars
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90
Welgen Inc full-length and truncated mouse anxa5 with c-terminal ddk-myc tag
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Full Length And Truncated Mouse Anxa5 With C Terminal Ddk Myc Tag, supplied by Welgen 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/c+terminal+ddk/full+length+truncated+mouse+anxa5+c+terminal+ddk+myc+tag/pmc06826004-401-15-24
Average 90 stars, based on 1 article reviews
full-length and truncated mouse anxa5 with c-terminal ddk-myc tag - by Bioz Stars, 2026-09
90/100 stars
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92
OriGene ampk alpha 1 (prkaa1) (nm_006251) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Ampk Alpha 1 (Prkaa1) (Nm 006251) Human Tagged Orf Clone, supplied by OriGene, 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/c+terminal+ddk/AMPK+alpha+1+(PRKAA1)+(NM_006251)+Human+Tagged+ORF+Clone/origene___rc218572
Average 92 stars, based on 1 article reviews
ampk alpha 1 (prkaa1) (nm_006251) human tagged orf clone - by Bioz Stars, 2026-09
92/100 stars
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94
OriGene cdc37 (nm_007065) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Cdc37 (Nm 007065) Human Tagged Orf Clone, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c+terminal+ddk/CDC37+(NM_007065)+Human+Tagged+ORF+Clone/origene___rc201002
Average 94 stars, based on 1 article reviews
cdc37 (nm_007065) human tagged orf clone - by Bioz Stars, 2026-09
94/100 stars
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90
rocky mountain labs pcmv6-sarm1 with c-terminal myc-ddk tag
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Pcmv6 Sarm1 With C Terminal Myc Ddk Tag, supplied by rocky mountain labs, 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/c+terminal+ddk/pcmv6+sarm1+with+c+terminal+myc+ddk+tag/pm36239430-419-4-15
Average 90 stars, based on 1 article reviews
pcmv6-sarm1 with c-terminal myc-ddk tag - by Bioz Stars, 2026-09
90/100 stars
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90
OriGene c4orf21 (zgrf1) (nm_018392) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
C4orf21 (Zgrf1) (Nm 018392) Human Tagged Orf Clone, supplied by OriGene, 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/c+terminal+ddk/C4orf21+(ZGRF1)+(NM_018392)+Human+Tagged+ORF+Clone/origene___rc229463
Average 90 stars, based on 1 article reviews
c4orf21 (zgrf1) (nm_018392) human tagged orf clone - by Bioz Stars, 2026-09
90/100 stars
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90
OriGene catalase (cat) (nm_001752) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Catalase (Cat) (Nm 001752) Human Tagged Orf Clone, supplied by OriGene, 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/c+terminal+ddk/Catalase+(CAT)+(NM_001752)+Human+Tagged+ORF+Clone/origene___rc210763
Average 90 stars, based on 1 article reviews
catalase (cat) (nm_001752) human tagged orf clone - by Bioz Stars, 2026-09
90/100 stars
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90
OriGene armc5 (nm_001105247) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Armc5 (Nm 001105247) Human Tagged Orf Clone, supplied by OriGene, 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/c+terminal+ddk/ARMC5+(NM_001105247)+Human+Tagged+ORF+Clone/origene___rc226267
Average 90 stars, based on 1 article reviews
armc5 (nm_001105247) human tagged orf clone - by Bioz Stars, 2026-09
90/100 stars
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90
OriGene ampk alpha 2 (prkaa2) (nm_006252) human tagged orf clone
A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. <t>MPRIP</t> is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds <t>actin.</t> <t>C-terminal</t> coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).
Ampk Alpha 2 (Prkaa2) (Nm 006252) Human Tagged Orf Clone, supplied by OriGene, 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/c+terminal+ddk/AMPK+alpha+2+(PRKAA2)+(NM_006252)+Human+Tagged+ORF+Clone/origene___rc210226
Average 90 stars, based on 1 article reviews
ampk alpha 2 (prkaa2) (nm_006252) human tagged orf clone - by Bioz Stars, 2026-09
90/100 stars
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Image Search Results


A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. MPRIP is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds actin. C-terminal coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).

Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Article Title: LRRC8A anion channels modulate vascular reactivity via association with Myosin Phosphatase Rho Interacting Protein (MPRIP)

doi: 10.1096/fj.202300561R

Figure Lengend Snippet: A) Immunoprecipitation (IP) of endogenous LRRC8A from VSMCs confirms the presence of LRRC8A in the whole cell (WC) lysate and precipitated protein from WT but not LRRC8A KO cells. MPRIP is present in the WC lysate from both genotypes but is only pulled down in LRRC8A WT cells. B) Proximity Ligation Assay (PLA) signal from α-MPRIP/α-LRRC8A in WT VSMCs. Small white spots represent PLA signal, the larger spots are nuclei. Counts of spots/nucleus from multiple fields of confluent WT and LRRC8A KO VSMCs (20x). PLA spots were smaller and significantly less numerous in KO cells. The bottom image shows red PLA spots with green nuclei as a side-view of cells. C) Confocal images of HEK293T cells co-expressing LRRC8A-meGFP and MPRIP-mCherry. Note co-localization at the plasma membrane, particularly at ruffled borders but not in LRRC8A-containing intracellular vesicles. D) Sites of protein binding to MPRIP. The first Plextrin Homology (PH) domain (aa 44–152) binds actin. C-terminal coiled-coil domains mediate interaction with RhoA and MYPT1 (M). Below the map are the constructs utilized to determine the site of MPRIP binding to LRRC8A (8A) was localized to aa 389–545. Vertical grey lines represent specific cysteines that can be oxidized based upon the Oxymouse database (Cys103, 120, 235, 361, 506, 571, 723, 830). Susceptible cysteines are present in the binding regions for all 4 protein partners. E) Immunoprecipitation of MPRIP-DDK fragments by full length LRRC8A-Myc in HEK293T cells expressing these constructs. Arrows identify overexpressed proteins, or the site where they would be expected to run (see IP: α-Myc) in whole cell lysates (WCL, left) and in immunoprecipitated protein (IP, right). All C-terminal MPRIP deletion mutants associate with LRRC8A, but the C-terminal MPRIP fragment 879–1038 does not associate with LRRC8A. The 213–545 peptide associated with LRRC8A as did the region between 389 and 545 which contains PH2 (see IP: α-LRRC8A).

Article Snippet: A C-terminal tagged clone of human MPRIP (DDK (Flag), Genscript, Cat # OHu00028D) was truncated by insertion of an additional Flag tag followed by a premature stop codon using the QuickChange site-directed mutagenesis kit (Agilent).

Techniques: Immunoprecipitation, Proximity Ligation Assay, Expressing, Clinical Proteomics, Membrane, Protein Binding, Construct, Binding Assay