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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
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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

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ALY Antibody - Mouse Anti-ALY 0.1ml
The protein encoded by this gene is a heat stable nuclear protein and functions as a molecular chaperone It is thought to regulate dimerization DNA binding and transcriptional activity of basic region-leucine zipper (bZIP) proteins
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ALY Antibody - Mouse Anti-ALY 50ul
The protein encoded by this gene is a heat stable nuclear protein and functions as a molecular chaperone It is thought to regulate dimerization DNA binding and transcriptional activity of basic region-leucine zipper (bZIP) proteins
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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
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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
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FMR1 (Drosophila) Antibody- Mouse Anti-FMR1 (Drosophila)
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
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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
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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

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Gemin 3 Antibody- Mouse Anti-Gemin 3
The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA) a common motor neuron degenerative disease The SMN protein is part of a complex containing several proteins of which one SIP1 (SMN interacting protein 1) has been characterized so far The SMN complex is found in both the cytoplasm and in the nucleus where it is concentrated in bodies called gems In the cytoplasm SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs) and they play a critical role in snRNP assembly In the nucleus SMN is required for pre-mRNA splicing likely by serving in the regeneration of snRNPs A DEAD box putative RNA helicase named Gemin 3 which is another component of the SMN complex has been identified Gemin 3 interacts directly with SMN as well as with SmB SmD2 and SmD3 Immunolocalization studies using mAbs to Gemin 3 show that it colocalizes with SMN in gems Gemin 3 binds SMN via its unique COOH-terminal domain and SMN mutations found in some SMA patients strongly reduce this interaction The presence of a DEAD box motif in Gemin 3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs
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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
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Gemin2 Antibody- Mouse Anti-Gemin2
Involved in biogenesis of spliceosomal snRNPs forms complex with Survival of Motor Neurons (SMN) protein interacts tightly with spliceosomal proteins and spliceosomal snRNAs U1 and U5
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Gemin2 Antibody- Mouse Anti-Gemin2
Involved in biogenesis of spliceosomal snRNPs forms complex with Survival of Motor Neurons (SMN) protein interacts tightly with spliceosomal proteins and spliceosomal snRNAs U1 and U5
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Gemin3 Antibody- Mouse Anti-Gemin3
The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA) a common motor neuron degenerative disease The SMN protein is part of a complex containing several proteins of which one SIP1 (SMN interacting protein 1) has been characterized so far The SMN complex is found in both the cytoplasm and in the nucleus where it is concentrated in bodies called gems In the cytoplasm SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs) and they play a critical role in snRNP assembly In the nucleus SMN is required for pre-mRNA splicing likely by serving in the regeneration of snRNPs A DEAD box putative RNA helicase named Gemin 3 which is another component of the SMN complex has been identified Gemin 3 interacts directly with SMN as well as with SmB SmD2 and SmD3 Immunolocalization studies using mAbs to Gemin 3 show that it colocalizes with SMN in gems Gemin 3 binds SMN via its unique COOH-terminal domain and SMN mutations found in some SMA patients strongly reduce this interaction The presence of a DEAD box motif in Gemin 3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs
£183.00

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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
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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.
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