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Description:
The synucleins, including Alpha-synuclein (also designated NACP for nonamyloid component precursor),Beta-synuclein (also designated PNP 14 for neuroprotein 14)and Gamma-synuclein (also designated persyn or BCSG1 for breast cancer-specific gene 1)are presynaptic protein abundant in neurons. Alpha-synuclein, a component of Alzheimer’s disease amyloid plaques, is localized to neuronal cell bodies and synapses. Coordinate expression of Alpha-synucleinand Beta-synuclein may be important during hematopoetic cell differentiation. In patients with Parkinson’s disease, a mutant form of Alpha-synuclein has been found and Gamma-synuclein is associated with axonal pathology.
Description:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).
Description:
Tumor necrosis factor (TNF) is a pleiotropic cytokine whose function is mediated through two distinct cell surface receptors (1,2). These receptors, designated TNF-R1 and TNF-R2, are expressed on most cell types (1,3). The majority of TNF functions are primarily mediated through TNF-R1 (1,4). FAN (for factor associated with neutral sphingomyelinase (N-SMase) activation) is an intermediate protein that interacts with TNF-R1 to initiate TNF signaling events. FAN binds to TNF-R1 at the cytoplasmic NSD (N-SMase activating domain), which results in the initiation of the N-SMase pathway (5). N-SMase has been shown to be involved in TNF-induced Raf-1 activation (6). FAN contains four carboxy-terminal WD-repeat domains which appear to be involved in protein-protein interaction. The FAN WD-repeats may mediate the interaction between FAN and TNF-R1 (5).
Description:
Participates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling.
Description:
The translational product of the Vav proto-oncogene is exclusively expressed in cells of hematopoietic origin and is critical for lymphocyte development and activation. However, the biochemical basis of Vav’s function is unclear. Vav contains a single SH2 domain that is required for its association with the T cell receptor (TCR). Overexpression of Vav or SLP-76 in Jurkat cells leads to NFAT activation and IL-2 production. When co-expressed, Vav and SLP-76 synergize to induce a robust basal and TCR-mediated IL-2 response. Although SLP-76 does not contain a motif that would indicate it to be a member of the tyrosine, serine/threonine or lipid kinase families, it does contain several putative SH2/SH3-binding domains and has been shown to physically associate with the adapter protein GRB2 as well as PLC g1. The discovery of SLP-76 represents an important step in elucidating the mechanism of Vav transformation and TCR-mediated NFAT activation.
Description:
The protein encoded by this gene shares strong similarity with Saccharomyces cerevisiae protein Cdc27, and the gene product of Schizosaccharomyces pombe nuc 2. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eucaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction. This protein was shown to interact with mitotic checkpoint proteins including Mad2, p55CDC and BUBR1, and thus may be involved in controlling the timing of mitosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Description:
The eight members of the recently identified Suppressor of Cytokines Signaling (SOCS) family are SOCS1, SOCS2, SOCS3, SOCS4, SOCS5, SOCS6, SOCS7, and CIS. Structurally the SOCS proteins are composed of an N- terminal region of variable length and amino acid composition, a central SH2 domain, and a C-terminal motif called the SOCS box. The SOCS proteins appear to form part of a classical negative feedback loop that regulates cytokine signal transduction. Transcription of each of the SOCS genes occurs rapidly in vitro and in vivo in response to cytokines, and once produced, the various members of the SOCS family appear to inhibit signaling in different ways. During Th1 differentiation a reduction in the association of Jak1 with the IL4 Receptor correlated with the appearance of SOCS5. SOCS5 protein was preferentially expressed in committed Th1 cells and interacted with the cytoplasmic region of the IL4 Receptor alpha chain irrespective of receptor tyrosine phosphorylation. This unconventional interaction of SOCS5 protein with IL4 Receptor resulted in the inhibition of IL4-mediated signal transducer and activator of transcription-6 activation. T cells from transgenic mice constitutively expressing SOCS5 exhibited a significant reduction of IL4-mediated Th2 development. Therefore, the induced SOCS5 protein in Th1 differentiation environment may play an important role by regulating Th1 and Th2 balance.
Description:
eIF4B is required for the binding of mRNA to ribosomes. It functions in close association with eIF4F and eIF4A. It binds near the 5'-terminal cap of mRNA in the presence of eIF4F and ATP. It promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both eIF4A and eIF4F.
Description:
HLA B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta 2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells.
Description:
Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal.
Description:
DNA-binding protein involved in S phase checkpoint control-coupled apoptosis by mediating p53/TP53-induced apoptosis. Has the ability to inhibit DNA synthesis and S phase arrest coupled to apoptosis. Has affinity to both double- and single-stranded DNA.
Description:
Fibrinogen-like 1 is a member of the fibrinogen family. This protein is homologous to the carboxy terminus of the fibrinogen beta- and gamma- subunits which contains the four conserved cysteines of fibrinogens and fibrinogen related proteins. However, this protein lacks the platelet-binding site, cross-linking region and a thrombin-sensitive site which are necessary for fibrin clot formation. This protein may play a role in the development of hepatocellular carcinomas. Four alternatively spliced transcript variants encoding the same protein exist for this gene. [provided by RefSeq, Jul 2008].
Description:
The ILK protein is important in different biological pathways such as cell adhesion, anchorage-dependent cell cycle progression, oncogenic transformation, and growth factor signaling. The kinase activity of ILK is low in non-activated cells; its activity is stimulated by cell-ECM interactions and by certain growth factors. 3 Negative regulation of ILK is mediated by two phosphatases: PTEN, a tumor suppressor lipid sphatase, and ILKAP, a PP2C protein phosphatase. In tumor cells that do not express PTEN protein, ILK is constitutively active.
UOM:
1 * 100 µl
Promotion
,BOSSBS-5444REA
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