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2-Iodophenyl+isothiocyanate
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2-Iodophenyl+isothiocyanate
Catalog Number:
(10458-832)
Supplier:
Bioss
Description:
RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.
Catalog Number:
(10311-740)
Supplier:
Bioss
Description:
C3orf36 (chromosome 3 open reading frame 36), also known as FLJ22173, MGC125760 or MGC125761, is a 165 amino acid protein encoded by a gene that maps to human chromosome 3p25.3. Chromosome 3 is made up of approximately 214 million bases encoding over 1,100 genes. Notably, there is a chemokine receptor gene cluster and a variety of human cancer related loci on chromosome 3. Particular regions of the chromosome 3 short arm are deleted in many types of cancer cells. Key tumor suppressing genes on chromosome 3 encode apoptosis mediator RASSF1, cell migration regulator HYAL1 and angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth disease are a few of the numerous genetic diseases associated with chromosome 3.
Catalog Number:
(10254-418)
Supplier:
Bioss
Description:
The inositol polyphosphate 5-phosphatases selectively remove the phosphate from the 5-position of various phosphatidylinositols, which generate second messengers in response to extracellular signals. Synaptojanins are characterized by an N-terminal SAC1-like sequence, a central 5-phosphate domain, and a unique C-terminal sequence and have been shown to use phosphatidylinositol 4,5-bisphosphate as a substrate. Synaptojanins exist as two isoforms, synaptojanin 1 and 2, which differ in the C-terminal domain, and each isoform has multiple variants produced by alternative splicing. Synaptojanin 1 is expressed as two major forms: the shorter is found in brain while the longer is expressed in peripheral tissues. Eight splice variants of synaptojanin 2 have been detected, including a brain specific isoform. Synaptojanins are thought to participate in the endocytosis of synaptic vesicles and the regulation of the actin cytoskeleton.
Catalog Number:
(10272-400)
Supplier:
Bioss
Description:
eIF3K (Eukaryotic translation initiation factor 3 subunit K, Muscle-specific gene M9 protein) is a widely expressed translation initiation factor that belongs to the eIF3 subunit K family. Translation initiation factor 3 (eIF3) is a multisubunit complex containing at least 12 subunits. eIF3 binds to the 40S ribosomal subunit, promotes the binding of methionyl-tRNAi and mRNA, and interacts with several other initiation factors to form the 40S initiation complex. eIF3K is the smallest subunit of eIF3 and it interacts with several other subunits of eIF3 and the 40S ribosomal subunit. eIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is ubiquitously expressed in human tissues. eIF3K is distributed both in nucleus and cytoplasm and colocalizes with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).
Catalog Number:
(10364-654)
Supplier:
Bioss
Description:
HLA-A 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. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described. [provided by RefSeq, Jul 2008]
Catalog Number:
(10336-096)
Supplier:
Bioss
Description:
Apelin is a neuropeptide expressed in the supraoptic and paraventricular nuclei and is an endogenous ligand for APJ, a G protein-coupled orphan receptor which is an alternative coreceptor with CD4 for HIV-1. Apelin and APJ are ubiquitously expressed in peripheral tissues, with highest levels reported for heart and lungs, as well several regions within the central nervous system. The actions of apelin remain largely unknown: Apelin inhibits HIV-1 entry in cells coexpressing CD4 and APJ; the oral intake of Apelin in colostrum and breast milk could have a role in the modulation of the immune responses in neonates; more recent studies have also indicated a role for Apelin in the central control of body fluid homeostasis, by influencing AVP release and drinking behavior. In the cardiovascular system several actions of Apelin have been described, including endothelium-dependent vasodilatation, vasoconstriction through direct action on smooth muscle and positive inotropism.
Catalog Number:
(10336-600)
Supplier:
Bioss
Description:
Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and is found associated with the sulfonylurea receptor SUR. Mutations in this gene are a cause of familial persistent hyperinsulinemic hypoglycemia of infancy (PHHI), an autosomal recessive disorder characterized by unregulated insulin secretion. Defects in this gene may also contribute to autosomal dominant non-insulin-dependent diabetes mellitus type II (NIDDM), transient neonatal diabetes mellitus type 3 (TNDM3), and permanent neonatal diabetes mellitus (PNDM). Multiple alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq]
Catalog Number:
(10397-072)
Supplier:
Bioss
Description:
The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
Catalog Number:
(10424-254)
Supplier:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
Catalog Number:
(10464-382)
Supplier:
Bioss
Description:
This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.
Catalog Number:
(10671-264)
Supplier:
Bioss
Description:
Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.
Catalog Number:
(10667-840)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. ZNRF1 (zinc and ring finger 1), also known as NIN283, is a 227 amino acid protein that contains one RING-type zinc finger and localizes to the lysosome and the endosome, as well as to cytoplasmic vesicles and the peripheral membrane. Expressed primarily in nervous system tissue, but also present in testis and thymus, ZNRF1 functions as an E3 ubiquitin-protein ligase that is thought to play a role in the establishment and maintenance of neuronal plasticity. Multiple isoforms of ZNRF1 exist due to alternative splicing events.
Catalog Number:
(10667-744)
Supplier:
Bioss
Description:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the Elongin B/C complex. Several other families of proteins also contain SOCS boxes, but differ from the SOCS proteins in the type of domain they contain upstream of the SOCS box. The largest family of SOCS box-containing proteins is the ankyrin repeat and SOCS box-containing (ASB) protein family. ASB-7 (ankyrin repeat and SOCS box-containing 7) is a 318 amino acid protein that contains one SOCS box domain and seven ANK repeats and belongs to the ASB family. Existing as multiple alternatively spliced isoforms, ASB-7 functions as a substrate-recognition component of an E3 ubiquitin-protein ligase complex and, working in conjunction with other proteins, plays a role in the ubiquitination and subsequent proteasomal degradation of target proteins.
Catalog Number:
(10355-546)
Supplier:
Bioss
Description:
Disabled 1 (Dab1) is an 80 kDa protein that is encoded by the Disabled-1 gene locus which is mutated in scrambler and yotari mutant mice. Phenotypically, the mutation of this gene produces motor defects and ataxia, disruption of neuronal migration, and severe cerebellar hypoplasia. Dab1 is an intracellular adapter protein that functions in downstream signaling events initiated by the secreted protein reelin. Dab1 contains a phosphotyrosine binding (PTB) domain in the amino terminus. Tyrosine phosphorylation of Dab1 is increased by reelin binding to the Very Low Density Lipoprotein Receptor (VLDLR) and Apolipoprotein E Receptor 2 (ApoER2) through stimulation of Src family kinases. Src family kinase and c-Abl activities are themselves then stimulated by binding to tyrosine phosphorylated Dab1. Dab1 also mediates activation of Akt (PKB) by reelin resulting in inhibition of glycogen synthase kinase 3 beta (GSK-3 beta) and decreased phosphorylation of the microtubule-associated protein, Tau. Dab1 serine 491 is phosphorylated in a Cdk5-dependent manner and regulates, likely indirectly, Reelin-induced signaling during neural cortex development.
Catalog Number:
(10396-376)
Supplier:
Bioss
Description:
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.
Catalog Number:
(10349-964)
Supplier:
Bioss
Description:
Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.
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