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Ageing Chromatin

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HIV1 integrase Antibody- Mouse Anti-HIV1 integrase
Integrase is an enzyme, a product of the HIV1 Gag/Pol gene; the other two enzymes being reverse transcriptase and protease. The human immunodeficiency virus (HIV-1) uses an enzyme, a so-called integrase, to carry out the integration of its viral DNA into the host chromosome thereby tricking the host cell machinery into making viral proteins. The HIV-1 integrase is a protein of 32 kDa and is composed of three domains. No cellular homologue of HIV integrase has been described, so potential inhibitors to this enzyme could be relatively nontoxic.
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hnRNP-U Antibody- Mouse (monoclonal) Anti-hnRNP-U
The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport While all of the hnRNPs are present in the nucleus some seem to shuttle between the nucleus and the cytoplasm The hnRNP proteins have distinct nucleic acid binding properties hnRNP U is thought to be involved in the packaging of hnRNA into large ribonucleoprotein complexes During apoptosis this protein is cleaved in a caspase-dependent way
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Lamin A Antibody- Mouse Anti-Lamin A
Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A type lamins and B type lamins The A type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel 10 while the B type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 Recent evidence has revealed that mutations in A-type lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A type lamins coincides with cell differentiation and as A type lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A type lamins
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Lamin A Antibody- Mouse Anti-Lamin A
Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A type lamins and B type lamins The A type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel 10 while the B type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 Recent evidence has revealed that mutations in A-type lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A type lamins coincides with cell differentiation and as A type lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A type lamins
£183.00

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MCPH1 (BRIT1) Antibody- Mouse Anti-MCPH1 (BRIT1)
This gene encodes a DNA damage response protein. The encoded protein may play a role in G2/M checkpoint arrest via maintenance of inhibitory phosphorylation of cyclin-dependent kinase 1. Mutations in this gene have been associated with primary autosomal recessive microcephaly 1 and premature chromosome condensation syndrome MCPH1 looks like it might be a useful prognostic indicator in breast cancer associated with BRCA1 inactivation
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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
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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
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Ran Antibody- Rabbit Anti-Ran
Ran (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex The Ran protein is also involved in control of DNA synthesis and cell cycle progression Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1) Mutations in Ran disrupt DNA synthesis Because of its many functions it is likely that Ran interacts with several other proteins Ran regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules Ran could be a key signaling molecule regulating microtubule polymerization during mitosis RCC1 generates a high local concentration of Ran-GTP around chromatin which in turn induces the local nucleation of microtubules Ran is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor Polyglutamine repeat expansion in the AR is linked to Kennedys disease (X-linked spinal and bulbar muscular atrophy) Ran coactivation of the AR diminishes with polyglutamine expansion within the AR and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedys disease
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RanGEF (RCC1) Antibody- Rabbit Anti-RanGEF
Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin RanGTP localization has been proposed to result from the association of Rans GDP/GTP exchange factor RCC1 with chromatin but Ran is shown here to bind directly to chromatin in two modes either dependent or independent of RCC1 and where bound to increase the affinity of chromatin for NE membranes
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RanGEF (RCC1) Antibody- Rabbit Anti-RanGEF (RCC1)
Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin RanGTP localization has been proposed to result from the association of Rans GDP/GTP exchange factor RCC1 with chromatin but Ran is shown here to bind directly to chromatin in two modes either dependent or independent of RCC1 and where bound to increase the affinity of chromatin for NE membranes
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RNA polymerase II CTD Antibody- Mouse Anti-RNA polymerase II CTD
RNA polymerase II carboxy-terminal domain (CTD) interacts with a large multisubunit complex that contains TATA-binding protein (TBP) and is an integral part of the transcription initiation complex Phosphorylation of RNA polymerase IIs largest subunit C-terminal domain (CTD) is a key event during mRNA metabolism Numerous enzymes including cell cycle-dependent kinases and TFIIF-dependent phosphatases target the CTD
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Y14 Antibody- Mouse (monoclonal) Anti-Y14
Y14 is a protein with a conserved RNA-binding motif It is preferentially associated with mRNAs produced by splicing including both nuclear mRNAs and newly exported cytoplasmic mRNAs It is thought that the protein remains associated with spliced mRNAs as a tag to indicate where introns had been present thus coupling pre- and post-mRNA splicing events Previously it was thought that two genes encode this protein RBM8A and RBM8B it is now thought that the RBM8B locus is a pseudogene Two alternative start codons result in two forms of the protein and this gene also uses multiple polyadenylation sites
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Y14 Antibody- Mouse Anti-Y14
Y14 is a protein with a conserved RNA-binding motif It is preferentially associated with mRNAs produced by splicing including both nuclear mRNAs and newly exported cytoplasmic mRNAs It is thought that the protein remains associated with spliced mRNAs as a tag to indicate where introns had been present thus coupling pre- and post-mRNA splicing events Previously it was thought that two genes encode this protein RBM8A and RBM8B it is now thought that the RBM8B locus is a pseudogene Two alternative start codons result in two forms of the protein and this gene also uses multiple polyadenylation sites
£183.00

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