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Description:
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Description:
Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes By similarity. Acts as a transcriptional activator or repressor By similarity. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3' By similarity. When overexpressed, promotes cells to enter into S phase and proliferation
Description:
GRASP (GRP1-associated scaffold protein, tamalin) is a 395 amino acid proteinencoded by the human gene GRASP. GRASP is a scaffold protein that com-prises multiple protein-interacting domains, including a 95 kDa postsynapticdensity protein (PSD-95)/discs-large/ZO-1 (PDZ) domain, a leucine-zipperregion and a carboxyl-terminal PDZ-binding motif. GRASP is involved withintracellular trafficking and contributes to the macromolecular organizationof group 1 metabotropic glutamate receptors (mGluRs) at synapses. GRASPforms a heteromer composed of GRASP , PSCD2 and at least one mGluR-1. Italso interacts with PSCD3, mGluR-2, mGluR-3 and mGluR-5. GRASP is highlyexpressed in brain and has lower levels of expression in lung, heart, embryo, kidney and ovary.
Description:
Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.
Description:
The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR). The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death. Overexpression of the NR2B subunit of the receptor has been associated with increases in learning and memory while aged, memory impaired animals have deficiencies in NR2B expression. Tyr1472 on NR2B is phosphorylated and this may lead to the increased expression of the NMDAR at the synapse that plays a role in synaptic plasticity.
Description:
MEK 1 (MAP Kinase Kinase, also known as MKK) is an integral component of the MAP kinase cascade that regulates cell growth and differentiation and this pathway also plays a key role in synaptic plasticity in brain. Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. Conversely there also appears to be a feedback phosphorylation of MEK 1 by MAP kinase. The sites on MEK 1 that are phosphorylated by MAP kinase are Thr292 and Thr386.
Description:
The three Mitogen-Activated Protein Kinases (MAPKs) are evolutionarily conserved protein kinases that control a vast array of cellular processes. p38 MAPK is one these kinases and it is activated by both inflammatory cytokines and by stress. The p38 MAPK is thought to be particularly important in diseases like asthma and autoimmunity but it also plays important roles in the stress response of the nervous system. Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr180 and Tyr182.
Description:
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats and is localized in the nucleus.
Description:
Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA
Description:
MEK 1 (MAP Kinase Kinase, also known as MKK) is an integral component of the MAP kinase cascade that regulates cell growth and differentiation and this pathway also plays a key role in synaptic plasticity in brain. Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. Conversely there also appears to be a feedback phosphorylation of MEK 1 by MAP kinase. The sites on MEK 1 that are phosphorylated by MAP kinase are Thr292 and Thr386.
Description:
A member of the family of mammalian F-box proteins. F-box proteins are an expanding family of eukaryotic proteins characterized by an approximately 40 aminoacid motif, the F box (so named because cyclin F was one of the first proteins in which this motif was identified). Some F-box proteins have been shown to be critical for the controlled degradation of cellular regulatory proteins.
Description:
At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. GSTM2 is a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione.Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs.
UOM:
1 * 50 µG
Promotion
,PRSI29-649EA
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