"Other Essentials"

Supplier: ProSci Inc.

NSF (N-ethylmaleimide sensitive fusion protein) is a critical component of the SNARE (soluble NSF attachment protein receptors) protein complex that is involved in synaptic vesicle trafficking. Specifically, NSF has been found to be essential in membrane fusion. Furthermore, NSF has been recently demonstrated to bind other protein complexes such as AMPA receptor subunits (GluR2), GATE-16, LMA-1 and Rabs suggesting a more diverse role in the assembly of various protein complexes (Whiteheart et al., 2004).

Supplier: Bioss

LGI4, also known as leucine-rich glioma-inactivated protein 4, is a 537 amino acid secreted glycosylated protein that is widely expressed, with highest levels found within the nervous system. Interestingly, siRNA knockdown studies of LGI4 expression in Schwann cells have been shown to result in the inhibition of myelination, thus suggesting that LGI4 is an essential component of myelin formation and axon segregation. LGI4 shares significant homology with its other family members, LGI1, LGI2 and LGI3. Significantly, mutations in the gene encoding LGI1 have been linked to human temporal lobe epilepsy and, given the sequence similarity of LGI4, it is likely that it also may be implicated in the pathology of seizures. LGI4 is localized subcellularly to the Golgi, ER and vesicles. There are two isoforms of LGI4 that are produced as a result of alternative splicing events.

Supplier: Bioss

LGI4, also known as leucine-rich glioma-inactivated protein 4, is a 537 amino acid secreted glycosylated protein that is widely expressed, with highest levels found within the nervous system. Interestingly, siRNA knockdown studies of LGI4 expression in Schwann cells have been shown to result in the inhibition of myelination, thus suggesting that LGI4 is an essential component of myelin formation and axon segregation. LGI4 shares significant homology with its other family members, LGI1, LGI2 and LGI3. Significantly, mutations in the gene encoding LGI1 have been linked to human temporal lobe epilepsy and, given the sequence similarity of LGI4, it is likely that it also may be implicated in the pathology of seizures. LGI4 is localized subcellularly to the Golgi, ER and vesicles. There are two isoforms of LGI4 that are produced as a result of alternative splicing events.

Supplier: Bioss

LGI4, also known as leucine-rich glioma-inactivated protein 4, is a 537 amino acid secreted glycosylated protein that is widely expressed, with highest levels found within the nervous system. Interestingly, siRNA knockdown studies of LGI4 expression in Schwann cells have been shown to result in the inhibition of myelination, thus suggesting that LGI4 is an essential component of myelin formation and axon segregation. LGI4 shares significant homology with its other family members, LGI1, LGI2 and LGI3. Significantly, mutations in the gene encoding LGI1 have been linked to human temporal lobe epilepsy and, given the sequence similarity of LGI4, it is likely that it also may be implicated in the pathology of seizures. LGI4 is localized subcellularly to the Golgi, ER and vesicles. There are two isoforms of LGI4 that are produced as a result of alternative splicing events.

Supplier: Bioss

LGI4, also known as leucine-rich glioma-inactivated protein 4, is a 537 amino acid secreted glycosylated protein that is widely expressed, with highest levels found within the nervous system. Interestingly, siRNA knockdown studies of LGI4 expression in Schwann cells have been shown to result in the inhibition of myelination, thus suggesting that LGI4 is an essential component of myelin formation and axon segregation. LGI4 shares significant homology with its other family members, LGI1, LGI2 and LGI3. Significantly, mutations in the gene encoding LGI1 have been linked to human temporal lobe epilepsy and, given the sequence similarity of LGI4, it is likely that it also may be implicated in the pathology of seizures. LGI4 is localized subcellularly to the Golgi, ER and vesicles. There are two isoforms of LGI4 that are produced as a result of alternative splicing events.

Supplier: Bioss

Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

Supplier: Bioss

The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.

Supplier: ProSci Inc.

IKK alpha Antibody: Nuclear factor kappa B (NF-kappa B) is a ubiquitous transcription factor and an essential mediator of gene expression during activation of immune and inflammatory responses. NF-kappa B mediates the expression of a great variety of genes in response to extracellular stimuli including IL-1, TNFa, and bacteria product LPS. NF-kappa B is associated with I kappa B proteins in the cell cytoplasm, which inhibit NF-kappa B activity. The long-sought I kappa B kinase (IKK), which phosphorylates I kappa B, and mediates I kappa B degradation and NF-kappa B activation, was recently identified by several laboratories. IKK is a serine protein kinase, and the IKK complex contains alpha and beta subunits (IKK alpha and IKK beta ). IKK alpha and IKK beta interact with each other and both are essential for the NF-kappa B activation. IKK alpha specifically phosphorylates IkB-alpha. IKK alpha is expressed in variety of human tissues.

Supplier: Bioss

The Drosophila atonal gene produces a protein with basic helix loop helix (bHLH) domains that plays an essential role in the development of the Drosophila nervous system. Mammalian atonal homolog 2 (MATH-2) is a helix-loop-helix (HLH) transcription factor that is structurally homologous to the product of Drosophila atonal gene. MATH-2 is a 337 amino acid protein with an atonal-related basic HLH domain. In mice, expression of MATH-2 takes place by embryonic day 11.5 and initially localizes to the wall of brain vesicles and in the spinal cord. It is expressed in the cortical plate and the mantle layer in the developing central nervous system, and is limited to the nervous system in adults. Adult mouse cerebrums produce a high level of MATH-2 RNA with lower levels in other neuronal tissues. Research studies suggest that MATH-2 may function as a trans-acting factor involved in the development and maintenance of the mammalian nervous system.

Supplier: Bioss

The Ras p21 family of guanine nucleotide proteins has been widely studied in view of its apparent role in signal transduction pathways and high frequency of mutations in human malignancies. It is now clear, however, that the Ras proteins (H-, K- and N-Ras p21) are members of a much larger superfamily of related proteins. Six members of this family, Rap 1A, Rap 1B, Rap 2, R-Ras, Ral A and Ral B, exhibit approximately 50% amino acid homology to Ras. The six mammalian Rho proteins (Rho A, B, C, G, 7 and 8) are approximately 30% homologous to Ras and are expressed in a wide range of cell types. Both Ras p21 and Rho p21, as well as other members of the Ras superfamily, contain a carboxy-terminal CAAX sequence (C, cysteine; A, aliphatic amino acid; X, any amino acid) which in the case of Ras has been shown to be essential for correct localization and function.

Supplier: Biorbyt

Anti-POLR2H Rabbit Polyclonal Antibody

Supplier: Bioss

Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

Supplier: Bioss

Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

Supplier: Bioss

Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 4 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP3. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

Supplier: Bioss

Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.

Supplier: Bioss

Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.