Ageing (a probabilistic decline in a cells ability to repair itself) is a complex process. It is very likely that the aging process is driven by the interplay of different cellular mechanisms, in feedback loops both, exo and endogenous, resulting in damage to a cells to ability to self-repair.
Whilst that complexity and the involvement of DNA damage and epigenetic modifications are no doubt linked it is also the case that chromatin defects ( the cellular structure packaging the combination of DNA and proteins ) plays a key role in ageing.
A key research question is how these processes are linked. Is it that DNA damage leads to chromatin defects? Alternatively, that changes in chromatic structures impacts DNA replication. Most recently it is hypothesized that DNA damage, epigenetic processes and chromatin aberration are more of network of interlinked processes and that a straight linear explanation may be too simplistic.
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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
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
HDAC1 Antibody ; Mouse Anti-HDAC1
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity
£226.00
Histone H4 Me3K20 Antibody ; Mouse Anti-Histone H4 Me3K20
Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones.
Methylation of position-specific lysine residues in histone N termini is a central modification for regulating epigenetic transitions in chromatin. Each methylatable lysine residue can exist in a mono, di, or tri methylated state. Arginine resdiues can also by mono or di methylated
£226.00
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.
£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
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
