|
|
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
HDAC2 Antibody ; Mouse Anti-HDAC2
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.Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity
£226.00
HDAC3 Antibody ; Mouse Anti-HDAC3
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. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation
£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
