mbp fused proteins Search Results


human his6–blm protein blm966 – 1417 fused to mbp  (Cancer Research Technology Limited)
90
Cancer Research Technology Limited human his6–blm protein blm966 – 1417 fused to mbp
Human His6–Blm Protein Blm966 – 1417 Fused To Mbp, supplied by Cancer Research Technology Limited, 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/mbp+fused+proteins/pm15282207-270-5-19?v=Cancer+Research+Technology+Limited
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human his6–blm protein blm966 – 1417 fused to mbp - by Bioz Stars, 2026-07
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gst- or mbp-fused proteins  (Merck KGaA)
90
Merck KGaA gst- or mbp-fused proteins
Gst Or Mbp Fused Proteins, supplied by Merck KGaA, 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/mbp+fused+proteins/pm38506228-252-4-27?v=Merck+KGaA
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gst- or mbp-fused proteins - by Bioz Stars, 2026-07
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protein subunit h constructs fused with mbp  (SUNY Upstate Medical University)
90
SUNY Upstate Medical University protein subunit h constructs fused with mbp
Protein Subunit H Constructs Fused With Mbp, supplied by SUNY Upstate Medical University, 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/mbp+fused+proteins/pmc03470569-186-6-16?v=SUNY+Upstate+Medical+University
Average 90 stars, based on 1 article reviews
protein subunit h constructs fused with mbp - by Bioz Stars, 2026-07
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synthetic gene encoding a maltose binding protein (mbp) fused to ctip00–843  (GenScript corporation)
90
GenScript corporation synthetic gene encoding a maltose binding protein (mbp) fused to ctip00–843
Synthetic Gene Encoding A Maltose Binding Protein (Mbp) Fused To Ctip00–843, 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/mbp+fused+proteins/pm38922686-55-21-25?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
synthetic gene encoding a maltose binding protein (mbp) fused to ctip00–843 - by Bioz Stars, 2026-07
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synthetic gene encoding a maltose binding protein (mbp) fused to ctip-800–843  (GenScript corporation)
90
GenScript corporation synthetic gene encoding a maltose binding protein (mbp) fused to ctip-800–843
Synthetic Gene Encoding A Maltose Binding Protein (Mbp) Fused To Ctip 800–843, 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/mbp+fused+proteins/pmc11317151-46-21-25?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
synthetic gene encoding a maltose binding protein (mbp) fused to ctip-800–843 - by Bioz Stars, 2026-07
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maltose-binding protein (mbp)–fused zyg-12 749–777  (Absolute Biotech)
90
Absolute Biotech maltose-binding protein (mbp)–fused zyg-12 749–777
UNC-84 and <t>ZYG-12</t> are up-regulated in PZ germ cells in response to DNA damage and can physically associate in vitro. (A) Dissected germline from an UNC-84::GFP worm stained with anti–UNC-84 (N-terminal epitope; red) and anti-GFP (C-terminal epitope; green). Insets show staining in all zones of the germline from the PZ, transition zone (TZ), early pachytene (EP), mid-pachytene (MP), late pachytene (LP), diplotene (DP), and diakinesis (DI), as well as the somatic distal tip cell (DTC) and sheath cell (Sh). Bars: (main image) 100 µm; (insets) 2 μm. The arrow indicates a somatic sheath cell. The asterisk indicates a distal tip cell. (B) UNC-84::GFP is detected at the nuclear periphery in arrested PZ germ cells after cisplatin treatment. The UNC-84::GFP germline after 48 h of 250 µM cisplatin recovery, stained for GFP, RAD-51, and DAPI. (C) ZYG-12::GFP is present in patches in proliferating germ cells in the absence of cisplatin and shows higher intensity in RAD-51–positive nuclei 48 h after removal from 250 µM cisplatin (left). Quantification of pixel intensity plotted as fold GFP fluorescence at the nuclear envelope in RAD-51–positive nuclei compared with RAD-51–negative nuclei in ZYG-12::GFP and ZYG-12::GFP; unc-84(n369) worms (right); n > 90. Error bars indicate 95% CI. ***, P < 0.0001. (D) Image of ZYG-12::GFP (green), UNC-84 (red), RAD-51 (white), and DAPI (blue) localization in the PZ 48 h after 250 µM cisplatin. The arrow indicates a somatic distal tip cell. Bars, 10 µm. (E) MBP::ZYG-12 and UNC-84 coelute as a single complex upon size-exclusion chromatography (Superose 6 column; top). The asterisk represents a degradation product. Fractions were collected and analyzed by SDS-PAGE and Coomassie blue staining (bottom).
Maltose Binding Protein (Mbp)–Fused Zyg 12 749–777, supplied by Absolute Biotech, 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/mbp+fused+proteins/pmc05166498-400-7-28?v=Absolute+Biotech
Average 90 stars, based on 1 article reviews
maltose-binding protein (mbp)–fused zyg-12 749–777 - by Bioz Stars, 2026-07
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maltose-binding protein (mbp) fused to b-galactosidase  (Chemie GmbH)
90
Chemie GmbH maltose-binding protein (mbp) fused to b-galactosidase
UNC-84 and <t>ZYG-12</t> are up-regulated in PZ germ cells in response to DNA damage and can physically associate in vitro. (A) Dissected germline from an UNC-84::GFP worm stained with anti–UNC-84 (N-terminal epitope; red) and anti-GFP (C-terminal epitope; green). Insets show staining in all zones of the germline from the PZ, transition zone (TZ), early pachytene (EP), mid-pachytene (MP), late pachytene (LP), diplotene (DP), and diakinesis (DI), as well as the somatic distal tip cell (DTC) and sheath cell (Sh). Bars: (main image) 100 µm; (insets) 2 μm. The arrow indicates a somatic sheath cell. The asterisk indicates a distal tip cell. (B) UNC-84::GFP is detected at the nuclear periphery in arrested PZ germ cells after cisplatin treatment. The UNC-84::GFP germline after 48 h of 250 µM cisplatin recovery, stained for GFP, RAD-51, and DAPI. (C) ZYG-12::GFP is present in patches in proliferating germ cells in the absence of cisplatin and shows higher intensity in RAD-51–positive nuclei 48 h after removal from 250 µM cisplatin (left). Quantification of pixel intensity plotted as fold GFP fluorescence at the nuclear envelope in RAD-51–positive nuclei compared with RAD-51–negative nuclei in ZYG-12::GFP and ZYG-12::GFP; unc-84(n369) worms (right); n > 90. Error bars indicate 95% CI. ***, P < 0.0001. (D) Image of ZYG-12::GFP (green), UNC-84 (red), RAD-51 (white), and DAPI (blue) localization in the PZ 48 h after 250 µM cisplatin. The arrow indicates a somatic distal tip cell. Bars, 10 µm. (E) MBP::ZYG-12 and UNC-84 coelute as a single complex upon size-exclusion chromatography (Superose 6 column; top). The asterisk represents a degradation product. Fractions were collected and analyzed by SDS-PAGE and Coomassie blue staining (bottom).
Maltose Binding Protein (Mbp) Fused To B Galactosidase, supplied by Chemie 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/mbp+fused+proteins/pm12768338-107-11-3?v=Chemie+GmbH
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maltose-binding protein (mbp) fused to b-galactosidase - by Bioz Stars, 2026-07
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mbp-fused osair1 protein  (Promega)
90
Promega mbp-fused osair1 protein
UNC-84 and <t>ZYG-12</t> are up-regulated in PZ germ cells in response to DNA damage and can physically associate in vitro. (A) Dissected germline from an UNC-84::GFP worm stained with anti–UNC-84 (N-terminal epitope; red) and anti-GFP (C-terminal epitope; green). Insets show staining in all zones of the germline from the PZ, transition zone (TZ), early pachytene (EP), mid-pachytene (MP), late pachytene (LP), diplotene (DP), and diakinesis (DI), as well as the somatic distal tip cell (DTC) and sheath cell (Sh). Bars: (main image) 100 µm; (insets) 2 μm. The arrow indicates a somatic sheath cell. The asterisk indicates a distal tip cell. (B) UNC-84::GFP is detected at the nuclear periphery in arrested PZ germ cells after cisplatin treatment. The UNC-84::GFP germline after 48 h of 250 µM cisplatin recovery, stained for GFP, RAD-51, and DAPI. (C) ZYG-12::GFP is present in patches in proliferating germ cells in the absence of cisplatin and shows higher intensity in RAD-51–positive nuclei 48 h after removal from 250 µM cisplatin (left). Quantification of pixel intensity plotted as fold GFP fluorescence at the nuclear envelope in RAD-51–positive nuclei compared with RAD-51–negative nuclei in ZYG-12::GFP and ZYG-12::GFP; unc-84(n369) worms (right); n > 90. Error bars indicate 95% CI. ***, P < 0.0001. (D) Image of ZYG-12::GFP (green), UNC-84 (red), RAD-51 (white), and DAPI (blue) localization in the PZ 48 h after 250 µM cisplatin. The arrow indicates a somatic distal tip cell. Bars, 10 µm. (E) MBP::ZYG-12 and UNC-84 coelute as a single complex upon size-exclusion chromatography (Superose 6 column; top). The asterisk represents a degradation product. Fractions were collected and analyzed by SDS-PAGE and Coomassie blue staining (bottom).
Mbp Fused Osair1 Protein, supplied by Promega, 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/mbp+fused+proteins/pm26788958-62-6-18?v=Promega
Average 90 stars, based on 1 article reviews
mbp-fused osair1 protein - by Bioz Stars, 2026-07
90/100 stars
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Image Search Results


UNC-84 and ZYG-12 are up-regulated in PZ germ cells in response to DNA damage and can physically associate in vitro. (A) Dissected germline from an UNC-84::GFP worm stained with anti–UNC-84 (N-terminal epitope; red) and anti-GFP (C-terminal epitope; green). Insets show staining in all zones of the germline from the PZ, transition zone (TZ), early pachytene (EP), mid-pachytene (MP), late pachytene (LP), diplotene (DP), and diakinesis (DI), as well as the somatic distal tip cell (DTC) and sheath cell (Sh). Bars: (main image) 100 µm; (insets) 2 μm. The arrow indicates a somatic sheath cell. The asterisk indicates a distal tip cell. (B) UNC-84::GFP is detected at the nuclear periphery in arrested PZ germ cells after cisplatin treatment. The UNC-84::GFP germline after 48 h of 250 µM cisplatin recovery, stained for GFP, RAD-51, and DAPI. (C) ZYG-12::GFP is present in patches in proliferating germ cells in the absence of cisplatin and shows higher intensity in RAD-51–positive nuclei 48 h after removal from 250 µM cisplatin (left). Quantification of pixel intensity plotted as fold GFP fluorescence at the nuclear envelope in RAD-51–positive nuclei compared with RAD-51–negative nuclei in ZYG-12::GFP and ZYG-12::GFP; unc-84(n369) worms (right); n > 90. Error bars indicate 95% CI. ***, P < 0.0001. (D) Image of ZYG-12::GFP (green), UNC-84 (red), RAD-51 (white), and DAPI (blue) localization in the PZ 48 h after 250 µM cisplatin. The arrow indicates a somatic distal tip cell. Bars, 10 µm. (E) MBP::ZYG-12 and UNC-84 coelute as a single complex upon size-exclusion chromatography (Superose 6 column; top). The asterisk represents a degradation product. Fractions were collected and analyzed by SDS-PAGE and Coomassie blue staining (bottom).

Journal: The Journal of Cell Biology

Article Title: LINC complexes promote homologous recombination in part through inhibition of nonhomologous end joining

doi: 10.1083/jcb.201604112

Figure Lengend Snippet: UNC-84 and ZYG-12 are up-regulated in PZ germ cells in response to DNA damage and can physically associate in vitro. (A) Dissected germline from an UNC-84::GFP worm stained with anti–UNC-84 (N-terminal epitope; red) and anti-GFP (C-terminal epitope; green). Insets show staining in all zones of the germline from the PZ, transition zone (TZ), early pachytene (EP), mid-pachytene (MP), late pachytene (LP), diplotene (DP), and diakinesis (DI), as well as the somatic distal tip cell (DTC) and sheath cell (Sh). Bars: (main image) 100 µm; (insets) 2 μm. The arrow indicates a somatic sheath cell. The asterisk indicates a distal tip cell. (B) UNC-84::GFP is detected at the nuclear periphery in arrested PZ germ cells after cisplatin treatment. The UNC-84::GFP germline after 48 h of 250 µM cisplatin recovery, stained for GFP, RAD-51, and DAPI. (C) ZYG-12::GFP is present in patches in proliferating germ cells in the absence of cisplatin and shows higher intensity in RAD-51–positive nuclei 48 h after removal from 250 µM cisplatin (left). Quantification of pixel intensity plotted as fold GFP fluorescence at the nuclear envelope in RAD-51–positive nuclei compared with RAD-51–negative nuclei in ZYG-12::GFP and ZYG-12::GFP; unc-84(n369) worms (right); n > 90. Error bars indicate 95% CI. ***, P < 0.0001. (D) Image of ZYG-12::GFP (green), UNC-84 (red), RAD-51 (white), and DAPI (blue) localization in the PZ 48 h after 250 µM cisplatin. The arrow indicates a somatic distal tip cell. Bars, 10 µm. (E) MBP::ZYG-12 and UNC-84 coelute as a single complex upon size-exclusion chromatography (Superose 6 column; top). The asterisk represents a degradation product. Fractions were collected and analyzed by SDS-PAGE and Coomassie blue staining (bottom).

Article Snippet: 6×Histidine-tagged UNC-84 912–1,111 and maltose-binding protein (MBP)–fused ZYG-12 749–777 from C. elegans were cloned into a modified bicistronic expression plasmid (pETDuet-1) and were coexpressed in E. coli LOBSTR-RIL(DE3) (Kerafast; ).

Techniques: In Vitro, Staining, Fluorescence, Size-exclusion Chromatography, SDS Page

UNC-84 and FCD-2 are required for the efficient recruitment of FAN-1 after cisplatin treatment. (Left) Dissected germlines from FAN-1::GFP, FAN-1::GFP; unc-84(n369) , FAN-1::GFP; fcd-2 ( tm1268) , and FAN-1::GFP; zyg-12(or577 ) worms in the absence (−) and presence (+) of 250 µM cisplatin. (Right) Quantification of GFP intensity in the given genotypes where the ratio of nucleoplasmic to cytoplasmic signal was determined in the absence and presence of 250 µM cisplatin. n > 50 nuclei. Bar, 10 μm. Error bars indicate 95% CI. ***, P < 0.0001.

Journal: The Journal of Cell Biology

Article Title: LINC complexes promote homologous recombination in part through inhibition of nonhomologous end joining

doi: 10.1083/jcb.201604112

Figure Lengend Snippet: UNC-84 and FCD-2 are required for the efficient recruitment of FAN-1 after cisplatin treatment. (Left) Dissected germlines from FAN-1::GFP, FAN-1::GFP; unc-84(n369) , FAN-1::GFP; fcd-2 ( tm1268) , and FAN-1::GFP; zyg-12(or577 ) worms in the absence (−) and presence (+) of 250 µM cisplatin. (Right) Quantification of GFP intensity in the given genotypes where the ratio of nucleoplasmic to cytoplasmic signal was determined in the absence and presence of 250 µM cisplatin. n > 50 nuclei. Bar, 10 μm. Error bars indicate 95% CI. ***, P < 0.0001.

Article Snippet: 6×Histidine-tagged UNC-84 912–1,111 and maltose-binding protein (MBP)–fused ZYG-12 749–777 from C. elegans were cloned into a modified bicistronic expression plasmid (pETDuet-1) and were coexpressed in E. coli LOBSTR-RIL(DE3) (Kerafast; ).

Techniques:

UNC-84, ZYG-12, and the microtubule network are required for efficient repair of DNA cross-links. (A) Schematic of UNC-84 domains and mutations (top). TM, transmembrane domain. Percentages of progeny inviability of wild-type (WT) worms and unc-84(n369) , unc-84(P91S) , unc-84(S988F) , unc-84(C994Y) , and unc-84(G1002D) after exposure to the given concentrations of cisplatin (bottom). n > 10. cispl, cisplatin. (B) Percentages of progeny inviability after exposure to the given concentrations of cisplatin of wild-type worms and worms harboring mutations in KASH domain–containing proteins unc-83(e1408) , anc-1(e1873) , kdp-1 (RNAi), and zyg-12( RNAi) at 20°C, as well as wild type, zyg-12(or577) , and zyg-12(or577) ; cku-70(tm1524) at the semipermissive temperature of 16°C. n > 10. (C) Percentages of RAD-51–positive nuclei after treatment with 100 µM cisplatin in wild type, unc-84(n369) , kdp-1 (RNAi), zyg-12(or577) , and zyg-12(or577);cku-70(tm1524) at 16°C. n > 30. (D) Percentages of RAD-51–positive nuclei after treatment with 100 µM cisplatin in wild-type and cku-70(tm1524) worms in the presence of the given concentrations of colchicine. n > 30. Error bars indicate 95% CI. P-values were determined by two-way analyses of variance. *, P < 0.05; **, P < 0.001; ***, P < 0.0001.

Journal: The Journal of Cell Biology

Article Title: LINC complexes promote homologous recombination in part through inhibition of nonhomologous end joining

doi: 10.1083/jcb.201604112

Figure Lengend Snippet: UNC-84, ZYG-12, and the microtubule network are required for efficient repair of DNA cross-links. (A) Schematic of UNC-84 domains and mutations (top). TM, transmembrane domain. Percentages of progeny inviability of wild-type (WT) worms and unc-84(n369) , unc-84(P91S) , unc-84(S988F) , unc-84(C994Y) , and unc-84(G1002D) after exposure to the given concentrations of cisplatin (bottom). n > 10. cispl, cisplatin. (B) Percentages of progeny inviability after exposure to the given concentrations of cisplatin of wild-type worms and worms harboring mutations in KASH domain–containing proteins unc-83(e1408) , anc-1(e1873) , kdp-1 (RNAi), and zyg-12( RNAi) at 20°C, as well as wild type, zyg-12(or577) , and zyg-12(or577) ; cku-70(tm1524) at the semipermissive temperature of 16°C. n > 10. (C) Percentages of RAD-51–positive nuclei after treatment with 100 µM cisplatin in wild type, unc-84(n369) , kdp-1 (RNAi), zyg-12(or577) , and zyg-12(or577);cku-70(tm1524) at 16°C. n > 30. (D) Percentages of RAD-51–positive nuclei after treatment with 100 µM cisplatin in wild-type and cku-70(tm1524) worms in the presence of the given concentrations of colchicine. n > 30. Error bars indicate 95% CI. P-values were determined by two-way analyses of variance. *, P < 0.05; **, P < 0.001; ***, P < 0.0001.

Article Snippet: 6×Histidine-tagged UNC-84 912–1,111 and maltose-binding protein (MBP)–fused ZYG-12 749–777 from C. elegans were cloned into a modified bicistronic expression plasmid (pETDuet-1) and were coexpressed in E. coli LOBSTR-RIL(DE3) (Kerafast; ).

Techniques:

LINC complexes facilitate DNA repair through both the inhibition of NHEJ and the promotion of HR. (A) In response to DSBs, wild-type UNC-84 interacts with ZYG-12 at the nuclear envelope to form a LINC complex that connects the cytoskeleton with the nucleoplasm. Motors that associate with microtubules are unknown. In the nucleoplasm, UNC-84 (human Sun-1) interacts with NHEJ machinery (KU70/KU80/LIG-4 and DNA-PK in mammals) to drive microtubule-dependent inhibition of NHEJ and the promotion of RAD-51 loading/HR. (B) After DNA cross-links, UNC-84 also recruits FAN-1 to the nucleus to facilitate processing of interstrand cross-links; additional nucleases are involved in processing cross-links. (C) In the absence of UNC-84, NHEJ is not inhibited, and HR is also impaired in response to DSBs. Additionally, FAN-1 is not recruited to the nucleus upon induction of cross-links, and other nucleases may be inappropriately engaged. Blue, ZYG-12; purple, UNC-84; green, DNA-PK/KU70/KU80; orange, FAN-1. MT, microtubule; Ce, C. elegans ; WT, wild-type.

Journal: The Journal of Cell Biology

Article Title: LINC complexes promote homologous recombination in part through inhibition of nonhomologous end joining

doi: 10.1083/jcb.201604112

Figure Lengend Snippet: LINC complexes facilitate DNA repair through both the inhibition of NHEJ and the promotion of HR. (A) In response to DSBs, wild-type UNC-84 interacts with ZYG-12 at the nuclear envelope to form a LINC complex that connects the cytoskeleton with the nucleoplasm. Motors that associate with microtubules are unknown. In the nucleoplasm, UNC-84 (human Sun-1) interacts with NHEJ machinery (KU70/KU80/LIG-4 and DNA-PK in mammals) to drive microtubule-dependent inhibition of NHEJ and the promotion of RAD-51 loading/HR. (B) After DNA cross-links, UNC-84 also recruits FAN-1 to the nucleus to facilitate processing of interstrand cross-links; additional nucleases are involved in processing cross-links. (C) In the absence of UNC-84, NHEJ is not inhibited, and HR is also impaired in response to DSBs. Additionally, FAN-1 is not recruited to the nucleus upon induction of cross-links, and other nucleases may be inappropriately engaged. Blue, ZYG-12; purple, UNC-84; green, DNA-PK/KU70/KU80; orange, FAN-1. MT, microtubule; Ce, C. elegans ; WT, wild-type.

Article Snippet: 6×Histidine-tagged UNC-84 912–1,111 and maltose-binding protein (MBP)–fused ZYG-12 749–777 from C. elegans were cloned into a modified bicistronic expression plasmid (pETDuet-1) and were coexpressed in E. coli LOBSTR-RIL(DE3) (Kerafast; ).

Techniques: Inhibition