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Gemin1/SMN Antibody- Mouse Anti-SMN
This gene is part of a 500 kb inverted duplication on chromosome 5q13 This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region The telomeric and centromeric copies of this gene are nearly identical and encode the same protein However mutations in this gene the telomeric copy are associated with spinal muscular atrophy mutations in the centromeric copy do not lead to disease The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy The critical sequence difference between the two genes is a single nucleotide in exon 7 which is thought to be an exon splice enhancer It is thought that gene conversion events may involve the two genes leading to varying copy numbers of each gene The protein encoded by this gene localizes to both the cytoplasm and the nucleus Within the nucleus the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs) This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN 4 and also interacts with several proteins known to be involved in the biogenesis of snRNPs such as hnRNP U protein and the small nucleolar RNA binding protein Two transcript variants are produced by this gene
£226.00
hnRNP-Q Antibody- Mouse Anti-hnRNP-Q
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss-of-function mutations of the survival of motor neurons (SMN) protein SMN is complexed with several proteins including Gemin2 Gemin3 and Gemin4 and plays important roles in small nuclear ribonucleoprotein (snRNP) biogenesis and in pre-mRNA splicing The hnRNP Q proteins interact with SMN they are required for efficient pre-mRNA splicing in vitro The hnRNP Q proteins may provide a molecular link between the SMN complex and splicing
£226.00
hnRNP-Q Antibody- Mouse Anti-hnRNP-Q
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss-of-function mutations of the survival of motor neurons (SMN) protein SMN is complexed with several proteins including Gemin2 Gemin3 and Gemin4 and plays important roles in small nuclear ribonucleoprotein (snRNP) biogenesis and in pre-mRNA splicing The hnRNP Q proteins interact with SMN they are required for efficient pre-mRNA splicing in vitro The hnRNP Q proteins may provide a molecular link between the SMN complex and splicing
£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
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
SMN (Gemin1) Antibody- Mouse Anti-SMN
This gene is part of a 500 kb inverted duplication on chromosome 5q13 This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region The telomeric and centromeric copies of this gene are nearly identical and encode the same protein However mutations in this gene the telomeric copy are associated with spinal muscular atrophy mutations in the centromeric copy do not lead to disease The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy The critical sequence difference between the two genes is a single nucleotide in exon 7 which is thought to be an exon splice enhancer It is thought that gene conversion events may involve the two genes leading to varying copy numbers of each gene The protein encoded by this gene localizes to both the cytoplasm and the nucleus Within the nucleus the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs) This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN 4 and also interacts with several proteins known to be involved in the biogenesis of snRNPs such as hnRNP U protein and the small nucleolar RNA binding protein Two transcript variants are produced by this gene
£183.00
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
£226.00
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
