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Acetylated Lysine Antibody - Mouse Anti-Acetylated Lysine 0.1ml
CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation including c-jun and the adenoviral oncoprotein E1A The protein encoded by this gene associates with p300/CBP It has in vitro and in vivo binding activity with CBP and p300 and competes with E1A for binding sites in p300/CBP It has histone acetyl transferase activity with core histones and nucleosome core particles indicating that this protein plays a direct role in transcriptional regulation
£226.00
Acetylated Lysine Antibody - Mouse Anti-Acetylated Lysine 50ul
CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation including c-jun and the adenoviral oncoprotein E1A The protein encoded by this gene associates with p300/CBP It has in vitro and in vivo binding activity with CBP and p300 and competes with E1A for binding sites in p300/CBP It has histone acetyl transferase activity with core histones and nucleosome core particles indicating that this protein plays a direct role in transcriptional regulation
£183.00
FMR1 (Drosophila) Antibody- Mouse (monoclonal) Anti-FMR1
Fragile X syndrome is the most common inherited form of mental retardation It is caused by loss of FMR1 gene activity due to either lack of expression or expression of a mutant form of the protein In mammals FMR1 is a member of a small protein family that consists of FMR1 FXR1 and FXR2 All three members bind RNA and contain sequence motifs that are commonly found in RNA-binding proteins including two KH domains and an RGG boxThe Drosophila genome contains a single gene homologous to the FXR family dFMR1 is subjected to transcriptional and posttranscriptional regulation during development and it homomerizes like its human counterpart dFMR1 profile of expression recapitulates that of the human FXR protein family it is highly enriched in muscles in central nervous system and in gonads In the larval brain anti-dFMR1 also recognizes mushroom bodies a centre that mediates learning and memory These features make the fly an ideal system to analyse the role of the FXR family and to identify genes in the FMRP pathway
£226.00
FXR2 Antibody- Mouse Anti-FXR2
FXR2 is a RNA binding protein containing two KH domains and one RCG box which is similar to FMRP and FXR1 It associates with polyribosomes predominantly with 60S large ribosomal subunits It may self-associate or interact with FMRP and FXR1 Fragile X syndrome is caused by the absence of the fragile X mental-retardation protein (FMRP) FMRP is the archetype of a class of cytoplasmic mRNA-binding proteins that includes the fragile X-related 1 and 2 proteins (FXR1 and FXR2) The fragile X-related proteins FXR1 and FXR2 contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins
£226.00
FXR2 Antibody- Mouse Anti-FXR2
FXR2 is a RNA binding protein containing two KH domains and one RCG box which is similar to FMRP and FXR1 It associates with polyribosomes predominantly with 60S large ribosomal subunits It may self-associate or interact with FMRP and FXR1 Fragile X syndrome is caused by the absence of the fragile X mental-retardation protein (FMRP) FMRP is the archetype of a class of cytoplasmic mRNA-binding proteins that includes the fragile X-related 1 and 2 proteins (FXR1 and FXR2) The fragile X-related proteins FXR1 and FXR2 contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins
£183.00
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-C1/C2 Antibody- Mouse Anti-hnRNP-C1/C2
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 C1 and C2 are encoded by one gene the two alternatively spliced transcript variants have been described
£226.00
hnRNP-C1/C2 Antibody- Mouse Anti-hnRNP-C1/C2
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 C1 and C2 are encoded by one gene the two alternatively spliced transcript variants have been described
£183.00
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
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 B1 Antibody- Mouse Anti-Lamin B1
An important part of the 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 alpha helices and a carboxy terminal 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
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
£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
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
