Product References
A Single Amino Acid Residue Regulates PTEN-Binding and Stability of the Spinal Muscular Atrophy Protein SMN.
Cells
Rademacher S,Detering NT,Schüning T,Lindner R,Santonicola P,Wefel IM,Dehus J,Walter LM,Brinkmann H,Niewienda A,Janek K,Varela MA,Bowerman M,Di Schiavi E,Claus P
MA1-13003 was used in Immunocytochemistry, Immunoprecipitation, and Western Blotting to identify regulatory phosphorylation sites that modulate function and stability.
Tue Nov 03 00:00:00 EST 2020
A Single Amino Acid Residue Regulates PTEN-Binding and Stability of the Spinal Muscular Atrophy Protein SMN.
Cells
Rademacher S,Detering NT,Schüning T,Lindner R,Santonicola P,Wefel IM,Dehus J,Walter LM,Brinkmann H,Niewienda A,Janek K,Varela MA,Bowerman M,Di Schiavi E,Claus P
MA1-13003 was used in Immunocytochemistry, Immunoprecipitation, and Western Blotting to identify regulatory phosphorylation sites that modulate function and stability.
Tue Nov 03 00:00:00 EST 2020
A Single Amino Acid Residue Regulates PTEN-Binding and Stability of the Spinal Muscular Atrophy Protein SMN.
Cells
Rademacher S,Detering NT,Schüning T,Lindner R,Santonicola P,Wefel IM,Dehus J,Walter LM,Brinkmann H,Niewienda A,Janek K,Varela MA,Bowerman M,Di Schiavi E,Claus P
MA1-13003 was used in Immunocytochemistry, Immunoprecipitation, and Western Blotting to identify regulatory phosphorylation sites that modulate function and stability.
Tue Nov 03 00:00:00 EST 2020
A Single Amino Acid Residue Regulates PTEN-Binding and Stability of the Spinal Muscular Atrophy Protein SMN.
Cells
Rademacher S,Detering NT,Schüning T,Lindner R,Santonicola P,Wefel IM,Dehus J,Walter LM,Brinkmann H,Niewienda A,Janek K,Varela MA,Bowerman M,Di Schiavi E,Claus P
MA1-13003 was used in Immunocytochemistry, Immunoprecipitation, and Western Blotting to identify regulatory phosphorylation sites that modulate function and stability.
Tue Nov 03 00:00:00 EST 2020
A ZPR1 mutation is associated with a novel syndrome of growth restriction, distinct craniofacial features, alopecia, and hypoplastic kidneys.
Clinical genetics
Ito YA,Smith AC,Kernohan KD,Pena IA,Ahmed A,McDonell LM,Beaulieu C,Bulman DE,Smidt A,Sawyer SL,Dyment DA,Boycott KM,Clericuzio CL
MA1-13003 was used in Western Blotting to study the association of a homozygous missense mutation in ZPR1 with a rare and recognisable multisystem syndrome.
Mon Oct 01 00:00:00 EDT 2018
Deficiency of the zinc finger protein ZPR1 causes neurodegeneration.
Proceedings of the National Academy of Sciences of the United States of America
Doran B,Gherbesi N,Hendricks G,Flavell RA,Davis RJ,Gangwani L
MA113003 was used in immunocytochemistry to study the role of zinc finger protein ZPR1 in neurodegeneration
Tue May 09 00:00:00 EDT 2006
ZPR1 is essential for survival and is required for localization of the survival motor neurons (SMN) protein to Cajal bodies.
Molecular and cellular biology
Gangwani L,Flavell RA,Davis RJ
MA1-13003 was used in immunohistochemistry to investigate the role of ZPR1 for the motor neurons (SMN) survival and the localization of the survival motor neurons (SMN) protein to Cajal bodies
Fri Apr 01 00:00:00 EST 2005
Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein.
Molecular cell
Narayanan U,Achsel T,Lührmann R,Matera AG
MA1-13003 was used in immunoprecipitation and western blot to study the coupled nuclear import of U snRNPs and the survival of motor neurons protein
Fri Oct 22 00:00:00 EDT 2004
Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein.
Nature cell biology
Gangwani L,Mikrut M,Theroux S,Sharma M,Davis RJ
MA113003 was used in immunocytochemistry and western blot to investigate the changes of ZPR1-SMN interaction in Spinal muscular atrophy
Sun Apr 01 00:00:00 EST 2001
Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein.
Nature cell biology
Gangwani L,Mikrut M,Theroux S,Sharma M,Davis RJ
MA113003 was used in immunocytochemistry and western blot to investigate the changes of ZPR1-SMN interaction in Spinal muscular atrophy
Sun Apr 01 00:00:00 EST 2001