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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
Eme1 (Msm4) Antibody- Mouse Anti-Eme1 (Msm4)
EME1 complexes with methyl methanesulfonate-sensitive UV-sensitive 81 protein (MUS81) to form an endonuclease complex which cleaves branched DNA structures, especially those arising during stalled DNA replication. The protein may be involved in repairing DNA damage and in maintaining genomic stability. It interacts with specifc DNA structures including nicked Holliday junctions, 3'-flap structures and aberrant replication fork structures. Alternative splicing results in multiple transcript variants.
£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
GAD65 Antibody- Mouse Anti-GAD65
Glutamic Acid Decarboxylase (GAD) catalyzes the conversion of L glutamate to g-aminobutyric acid (GABA), the principal inhibitory neurotransmitter in the brain, and a putative paracrine signal molecule in pancreatic islets. GAD has a restricted tissue distribution. It is highly expressed in the cytoplasm of GABAergic neurons in the central nervous system (CNS) and pancreatic beta cells. It is also present in other non-neuronal tissues such as testis, oviduct and ovary. GAD is also transiently expressed in non-GABAergic cells of the embryonic and adult nervous system, suggesting its involvement in development and plasticity. GAD exists as two isoforms, GAD65 and GAD67 (molecular masses of 65 and 67 kD, respectively) that are encoded by two different genes. GAD65 is an ampiphilic, membraneanchored protein, (585 amino acid residues) and is encoded on human chromosome 10. GAD67 is a cytoplasmic protein (594 amino acid residues) and is encoded on chromosome 2. There is 64% amino acid identity between the two isoforms, with the highest diversity located at the N terminus, which in GAD65 is required for targeting the enzyme to GABA-containing secretory vesicles. The two isoforms appear to have distinct intraneuronal distribution in the brain. GAD65 has been identified as an autoantigen in insulindependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS), IDDM is an autoimmune disease that results from T cell mediated destruction of pancreatic insulin-secreting beta cells. Islet-reactive T cells and antibodies primarily to GAD65 (also named beta cell autoantigen) can be detected in peripheral blood of 80% of recent-onset IDD patients and in pre-diabetic high-risk subjects before onset of clinical symptoms. This suggests that GAD may be an important marker in the early stages of the disease. Also, autoantibodies to GAD65 and GAD67 are detected in animal models of IDDM, including the non-obese diabetes (NOD) mouse. In the NOD mouse, T cell reactivity is initially restricted to the C terminal regions of GAD65, but later spreads to other parts of GAD65. Stiff-man syndrome (SMS), a rare disorder of the CNS, is characterized by progressive rigidity of the body musculature with painful spasms, due to impairment of the GABAergic neurotransmission. High-titer autoantibodies directed against GAD 65 and GABAergic neurons (nerve terminals) have been detected in the serum and cerebrospinal fluid (CSF) in 60% of patients with the syndrome. Strikingly, many of the SMS patients also developed late-onset IDDM.
£226.00
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
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
HEF 1/Cas-L (NEDD9)Antibody - Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£226.00
HEF-1/ Cas-L Antibody- Mouse Anti-HEF-1/ Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£183.00
HEF-1/ Cas-L Antibody- Mouse Anti-HEF-1/ Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£226.00
HEF-1/Cas-L (NEDD9) Antibody- Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£183.00
Lamin A/C mutant R453W Antibody ; Mouse Anti-Lamin A/C mutant R453W
Nuclear lamins are intermediate filament proteins that are the major structural component of the nuclear lamina on the inner surface of the nuclear envelope. Lamin A and Lamin C are splice variants of the Lamin A gene. Lamin A/C (CDCD1, LMN1, EMD2) expression is a hallmark of embryonic stem cell differentiation. In addition to adding structural integrity to the nucleus, lamins contribute to the makeup of the nuclear matrix. Lamins also help organize interphase chromatin through interactions with several chromatin proteins, including histones and Lap2, such that alteration in lamin organization (laminopathy) results in disruption of DNA replication, transcription and RNA processing. The R453W mutation is one of the most common causes of autosomal dominant Emery-Dreifuss muscular dystrophy (EDMD)
£226.00
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
