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PABP Antibody- Mouse Anti-PABP
The poly(A)-binding protein (PABP) which is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA is required for poly(A) shortening and translation initiation Grange et al (1987) isolated a melanoma cell cDNA encoding human PABP The predicted 633-amino acid protein contains 4 repeats of an approximately 80-amino acid unit in its N-terminal half The authors found that this repeat region is highly conserved between human and yeast PABP and is sufficient for poly(A) binding In vitro translation of the human PABP cDNA yielded a protein with an apparent molecular mass of 73 kD by SDS-PAGE Northern blot analysis indicated that PABP is expressed as a 29-kb mRNA in human melanoma cells Gorlach et al (1994) noted that each of the 4 repeats of PABP is a ribonucleoprotein (RNP) consensus sequence RNA-binding domain They determined that PABP has a pI of approximately 103 and is a very abundant stable protein Immunofluorescence studies of mammalian cells indicated that PABP is located exclusively in the cytoplasm However using both indirect immunofluorescence and tagging of PABP1 by fusion to the green fluorescent protein (GFP) Afonina et al (1998) demonstrated that PABP1 shuttles between the nucleus and cytoplasm PABP1 accumulated in the nucleus when transcription was inhibited suggesting that active transcription is required for nuclear export of PABP1
£226.00
PABP Antibody- Mouse Anti-PABP
The poly(A)-binding protein (PABP) which is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA is required for poly(A) shortening and translation initiation Grange et al (1987) isolated a melanoma cell cDNA encoding human PABP The predicted 633-amino acid protein contains 4 repeats of an approximately 80-amino acid unit in its N-terminal half The authors found that this repeat region is highly conserved between human and yeast PABP and is sufficient for poly(A) binding In vitro translation of the human PABP cDNA yielded a protein with an apparent molecular mass of 73 kD by SDS-PAGE Northern blot analysis indicated that PABP is expressed as a 29-kb mRNA in human melanoma cells Gorlach et al (1994) noted that each of the 4 repeats of PABP is a ribonucleoprotein (RNP) consensus sequence RNA-binding domain They determined that PABP has a pI of approximately 103 and is a very abundant stable protein Immunofluorescence studies of mammalian cells indicated that PABP is located exclusively in the cytoplasm However using both indirect immunofluorescence and tagging of PABP1 by fusion to the green fluorescent protein (GFP) Afonina et al (1998) demonstrated that PABP1 shuttles between the nucleus and cytoplasm PABP1 accumulated in the nucleus when transcription was inhibited suggesting that active transcription is required for nuclear export of PABP1
£183.00
PARP2 Antibody- Goat Anti-PARP2
Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks.
£226.00
PDE10A Antibody- Rabbit Anti- Phosphodiesterase 10A
Cyclic nucleotide phosphodiesterases (PDEs) catalyse the hydrolytic inactivation of the common intracellular second messengers cyclic adenosine and guanosine 3 5-monophosphate (cAMP and cGMP) Thus these enzymes play a critical role in the regulation of a wide range of physiological processes modulated by cyclic nucleotide signalling The PDE10 enzyme belongs to a family of PDEs that hydrolyse both cAMP and cGMP
£226.00
PDE1A Antibody- Rabbit Anti- Phosphodiesterase 1A
Cyclic nucleotide phosphodiesterases (PDEs) catalyse the hydrolytic inactivation of the common intracellular second messengers cyclic adenosine and guanosine 3 5-monophosphate (cAMP and cGMP) Thus these enzymes play a critical role in the regulation of a wide range of physiological processes modulated by cyclic nucleotide signalling PDE1 has three subtypes PDE1A PDE1B and PDE1C PDE1A and PDE1B have higher affinity for cGMP than for cAMP whereas PDE1C has high affinity for both cAMP and cGMP
£183.00
PDE4B Antibody- Rabbit Anti- Phosphodiesterase 4B
Cyclic nucleotide phosphodiesterases (PDEs) catalyse the hydrolytic inactivation of the common intracellular second messengers cyclic adenosine and guanosine 3 5-monophosphate (cAMP and cGMP) Thus these enzymes play a critical role in the regulation of a wide range of physiological processes modulated by cyclic nucleotide signallingThe PDE4 enzyme belongs to a family of cAMP-dependent PDEs that provide the major means of inactivating the key intracellular second messenger cAMP Four genes (4A 4B 4C and 4D) encode around 20 distinct isoform members of the PDE4 family Each isoform is characterized by a unique N-terminal region
£226.00
Progerin Antibody ; Mouse Anti-Progerin
Progerin is a 614 amino acid protein involved in Hutchinson-Gilford progeria syndrome. Progerin is most often generated by a point mutation (C1824T) in the LMNA gene that codes for lamin A and C. This mutation activates a cryptic splice site and gives rise to a form of lamin A with a 50-amino acids internal deletion within the carboxyl-terminal domain of the protein. Approximately 80% of Hutchinson-Gilford progeria syndrome cases carry a single copy of the most common mutation, a silent point mutation, G608G (GGC > GGT), within exon 11 of LMNA gene
£226.00
