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APPL1 Antibody - Rabbit Anti-APPL1 50ul
The protein encoded by this gene has been shown to be involved in the regulation of cell proliferation and in the crosstalk between the adiponectin signalling and insulin signalling pathways The encoded protein binds many other proteins including RAB5A DCC AKT2 PIK3CA adiponectin receptors and proteins of the NuRD/MeCP1 complex This protein is found associated with endosomal membranes but can be released by EGF and translocated to the nucleus
£226.00
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
£226.00
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
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
£226.00
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
Lamin B2 Antibody- Mouse Anti-Lamin B2
An important part of the cell nucleus is formed by nuclear lamina Nuclear lamins form a network of 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 Adel10 while the B-type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 The nuclear lamins comprise a unique subclass of the intermediate filament protein family They share a molecular domain organisation with the other intermediate filament proteins in that they are fibrous molecules that have an aminoterminal globular head a central rod of a-helices and a carboxyterminal globular domain Many biochemical and molecular features of lamins have been studied but their functions remain still largely undetermined One of the functions ascribed to the lamina is the maintenance of the structural integrity of the nucleus Besides interactions with the nuclear membrane and other intermediate filaments lamins interact with the nuclear chromatin Eukaryotic chromatin is organised into loops which are attached to the nuclear matrix This organisation is thought to contribute to compaction of the chromatin and regulation of gene expression Lamins as part of the nuclear matrix may be involved in these processes since chromatin binding sites have been detected in both A- and B-type lamins
£183.00
Lamin C Antibody- Rabbit Anti-Lamin C
An important part of the cell nucleus is formed by nuclear lamina Nuclear lamins form a network of 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 Adel10 while the B-type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 The nuclear lamins comprise a unique subclass of the intermediate filament protein family They share a molecular domain organisation with the other intermediate filament proteins in that they are fibrous molecules that have an aminoterminal globular head a central rod of a-helices and a carboxyterminal globular domain Many biochemical and molecular features of lamins have been studied but their functions remain still largely undetermined One of the functions ascribed to the lamina is the maintenance of the structural integrity of the nucleus Besides interactions with the nuclear membrane and other intermediate filaments lamins interact with the nuclear chromatin Eukaryotic chromatin is organised into loops which are attached to the nuclear matrix This organisation is thought to contribute to compaction of the chromatin and regulation of gene expression Lamins as part of the nuclear matrix may be involved in these processes since chromatin binding sites have been detected in both A- and B-type lamins
£226.00
LAP2a Antibody- Rabbit Anti-LAP2a
Lamins are type V intermediate filament proteins and are grouped into constitutively expressed B-type lamins and developmentally regulated A- type lamins Lamin-binding proteins in the nuclear lamina and the nuclear interior include several protein families and/or types of proteins in higher eu karyotes such as the inner nuclear membrane proteins lamin B receptor emerin and MANI three isoforms of lamina-associated polypeptide 1 (LAP 1) and several isoforms of LAP 2 Up to six LAP 2 isoforms derive from a single gene by alternative splicing in mammals and various isoforms have been described in Xenopus The best characterized LAP2 isoforms are the inner nuclear membrane protein LAP 2 beta and the nucleoplasmic protein LAP 2 alpha which are identical in their N-terminal 187-amino acid constant region but differ in their C termini While LAP 2 beta binds to B-type lamins at the nuclear periphery and was suggested to regulate nuclear lamina growth LAP 2 alpha specifically interacts with A-type lamins within the nuclear interior as part of a detergent/salt-resistant nucleoskeletal structure
£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
£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
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
£183.00
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
£226.00
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
£183.00
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
£183.00
RNA polymerase II CTD Antibody- Mouse Anti-RNA polymerase II CTD-phosphorylated
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
£183.00
TRF1 Antibody- Mouse Anti-TRF1
The TRF1 gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex It is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase acting in cis to limit the elongation of individual chromosome ends The protein structure contains a C-terminal Myb motif a dimerization domain near its N-terminus and an acidic N-terminus Two transcripts of this gene are alternatively spliced products
£183.00
