229873 Results for: "2-(5-Methyl-2-phenyl-1,3-oxazol-4-yl)acetic+acid"

Supplier: Prosci

DFF40 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD for caspase activated deoxyribonuclease. The human homologue of mouse CAD was more recently identified by three groups independently and termed CPAN, DFF40, and human CAD, respectively. DFF45/ICAD is the inhibitory protein of DFF40/CAD and forms complex with DFF40/CAD. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually causes the degradation of DNA in the nuclei. Activation of DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

IRS-1 Antibody: Following tyrosine phosphorylation, the insulin receptor substrate 1 and 2 (IRS-1 and IRS-2) can form a protein scaffolding for the assembly of a host of Src homology 2 (SH2) domain-containing proteins. IRS-1 tyrosine phosphorylation can occur through the activity of several cytokine and growth factor receptors such as interleukin (IL)-4, IL-9, interferon-gamma, in addition to the insulin and insulin-like growth factor 1 receptors. The scaffolding provided by IRS-1 and IRS-2 is necessary for insulin signal transduction across the cell membrane. IRS-1 tyrosine phosphorylation, and thus formation of the IRS scaffolding is inhibited by tumor necrosis factor (TNF), and this inhibition can itself be blocked by rapamycin, an inhibitor of the mammalian target of rapamycin (TOR). TNF activity could also be blocked by inhibition of the Akt kinase and the PTEN tumor suppressor, suggesting that TNF impairs insulin signaling through IRS-1 by activation of the TOR signaling pathway.

Supplier: Prosci

RIP1 Antibody: RIP1 (Receptor Interacting Protein), also known as RIPK1, is a crucial 74 kD adaptor kinase in several of stress-induced signaling pathways and on the crossroad of a cell’s decision to live or die. RIP1 contains an N-terminal region with homology to protein kinases, an intermediate domain capable of association with MAPKKK and a C-terminal region containing a death domain motif present in the Fas and TNFR1 intracellular domains. Full length RIP1 is important for signallling to NF-kappa-B, MAPKs and necrosis, whereas caspase-8 generates a C-terminal RIP1 cleavage fragment, promoting TNF-induced apoptosis. It is required for TNFRSF1A-mediated and TLR3-induced NF-kappa-B activation. RIP1-deficient mice fail to thrive, displaying extensive apoptosis in both lymphoid and adipose tissues and dying at 1-3 days of age.

Supplier: Rockland Immunochemical

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD (for caspase activated deoxyribonuclease). The human homologue of mouse CAD was more recently identified by three groups independently and termed CPAN, DFF40, and human CAD, respectively. DFF45/ICAD is the inhibitory protein of DFF40/CAD and forms complex with DFF40/CAD. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually causes the degradation of DNA in the nuclei. Activation of DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

ATOH8 Antibody: Basic helix-loop-helix (bHLH) transcription factors play important roles in differentiation processes during embryonic development of vertebrates. ATOH8 (MATH6) is a tissue-restricted member of the atonal superfamily of bHLH transcription factors that exhibits 43-57% identity in the bHLH domain with other mammalian atonal paralogs including the NeuroD and Neurogenin factors. In the mouse, ATOH8 has been implicated in the specification and differentiation of neuronal cell lineages in the brain and may also participate in kidney development. Recent studies show that ATOH8 is a novel component of the pancreatic transcriptional network during embryonic development and suggest a potential role as a modulator of the differentiation program initiated by the pro-endocrine factor Neurog3. It is indispensable for early embryonic development, suggesting a more widespread function for this factor in tissue-specific differentiation processes that are dependent on class II bHLH genes.

Supplier: Prosci

TSLP Receptor Antibody: Thymic stromal lymphopoietin (TSLP) has recently been identified as an important factor capable of driving dendritic cell maturation and activation. It is involved in the positive selection of regulatory T cells, maintenance of peripheral CD4+ T cell homeostasis and the induction of CD4+ T cell-mediated allergic reaction. TSLP is also capable of supporting the growth of fetal liver and adult B cell progenitors and their differentiation to the IgM-positive stage of B cell development. Its receptor TSLP-R will bind TSLP in a low-affinity fashion in transfected cells; co-transfection with IL-7R-alpha cDNA results in high-affinity binding and a functional heteromeric complex. This heteromeric receptor requires stat5 for TSLP-mediated signal transduction and is inhibited by SOCS-1. The approximately 75 kDa band seen in the immunoblot may be a post-translationally modified form of TSLP-R.

Supplier: Prosci

ORAI3 Antibody: Antigen stimulation of immune cells triggers Ca++ entry through Ca++ release-activated Ca++ (CRAC) channels. ORAI3 is one of two mammalian homologs to ORAI1, a recently identified four-transmembrane spanning protein that is an essential component of CRAC. All three homologs have been shown to function as Ca++ plasma membrane channels gated through interactions with STIM1, the store-activated endoplasmic reticulum Ca++ sensor. However, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter.

Supplier: Prosci

Dact2 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact2, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact2 is most prominent during the development of the thymus kidneys, and salivary gland. Dact2 is thought to play a role distinct from that of Dact1 with Dact2 having a greater impact on a beta-catenin-independent process termed planar cell polarity/convergent-extension signaling. Furthermore, Dact2 but not Dact1 can inhibit Nodal signaling by promoting the endocytic degradation of TGF-beta receptors. At least two isoforms of Dact2 are known to exist.

Supplier: Prosci

Rkhd4 Antibody: Rkhd4, also known as MEX3A is a member of a novel family of four homologous human MEX3 proteins each containing two heterogeneous nuclear ribonucleoprotein K homology (KH) domains and one carboxy-terminal RING finger module. MEX3 proteins, including Rkhd4, are phosphoproteins that bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1 export pathway. These proteins are a novel family of evolutionarily conserved RNA-binding proteins, differentially recruited to P bodies and potentially involved in post-transcriptional regulatory mechanisms. While Rkhd2 has been suggested to be associated with susceptibility to essential hypertension type 8, the function of Rkhd4 remains unknown. Rkhd3 and Rkhd4, but not Rkhd2, co-localize with both the hDcp1a decapping factor and Argonaute (Ago) proteins in processing bodies (P bodies), recently characterized as centers of mRNA turnover.

Supplier: Prosci

Lin28 Monoclonal Antibody: Lin28 is a transcription factor that was first identified through its key role in the pathway of developmental timing in C. elegans. The role of Lin28 in development suggested that it might be useful in the creation of stem cells that might be beneficial in cell replacement therapies in the treatment of several degenerative diseases. Artificial stem cells, termed induced pluripotent stem (iPS) cells, can be created by expressing Lin28 in addition to the transcription factors POU5F1, Sox2, and NANOG in mouse fibroblasts. More recently, experiments have demonstrated that iPS cells could be generated using expression plasmids expressing Lin28, Sox2, POU5F1 and c-Myc, eliminating the need for virus introduction, thereby addressing a safety concern for potential use of iPS cells in regenerative medicine.

Supplier: Prosci

CCNT1 Antibody: Cyclins function as regulators of CDK kinases and exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. The cyclin-T1 protein (CCNT1) belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. CCNT1 tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing CCNT1 and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. CCNT1 and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.

Supplier: Rockland Immunochemical

ZEB2, initially identified as Smad interacting-protein 1, is normally located in the nucleus and functions as a DNA-binding transcriptional repressor that interacts with activated SMADs. Like the homologous ZEB1, ZEB2 inhibits the transcription of the E-cadherin gene and induces epithelial-mesenchymal transition, a genetic program controlling cell migration during embryonic development and wound healing, in vitro. ZEB2 can also protect cells from DNA damage-induced apoptosis, suggesting that its expression may contribute to tumor progression. Recent evidence has shown that ZEB2 is often observed in the cytoplasm in numerous cancer tissues, indicating that its localization may be regulated in normal and tumor tissues. Mutations in this gene are also associated with Hirschsprung disease/Mowat-Wilson syndrome.

Supplier: Rockland Immunochemical

Actin reorganization is important for the regulation of neuronal morphology. A protein involved in this process, the transducer of cdc42-dependent actin assembly 1 (TOCA-1) protein, a member of the evolutionarily conserved pombe CDC15 homology (PCH) protein family, is an essential component of the Cdc42 pathway. TOCA-1 binds both N-WASP and Cdc42 and is essential for Cdc42- and PIP2-induced actin polymerization, suggesting that TOCA-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Decreased expression of TOCA-1 significantly enhances neurite elongation in PC-12 cells; its overexpression in the same cells suppresses neurite elongation. It has been suggested that TOCA-1 negatively regulates axon branching by regulating membrane trafficking by regulating membrane trafficking through the F-BAR/EFC domain. Multiple isoforms of TOCA-1 are known to exist.

Supplier: Rockland Immunochemical

Matrilin (MATNs) are a family of non-collagenous extracellular matrix proteins consisting of four known members that have been proposed to play key roles in the formation of both collagen-dependent and collagen-independent filamentous networks. The matrilin family all share a structure made up of von Willebrand factor A domains, epidermal growth factor-like domains and a coiled coil alpha-helical module. MATN1 and MATN3 are expressed mainly in cartilage, while MATN2 and MATN4 occur in a wide variety of extracellular matrices. The matrilin genes are strictly and differently regulated and their expression may serve as markers for cellular differentiation and diseases such as astrocytoma and liver carcinoma. Recent studies show that MATN2 is a permissive substrate for axonal growth and cell migration, and it is required for successful nerve regeneration.

Supplier: Rockland Immunochemical

Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMAa and PUMAb. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

Supplier: Rockland Immunochemical

TNFAIP3, also known as A20, is located in chromosome band 6q23, a region that is often deleted in B cell lymphomas. Recently, it was identified as a tumor suppressor gene in Hodgkin lymphoma and several subtypes of non-Hodgkin lymphomas. TNFAIP3 was initially identified as a zinc-finger protein that is rapidly and transiently induced by TNF-a, inhibiting NF-kB-dependent gene expression, and protecting cells from TNF-a-cytotoxicity. Overexpression of TNFAIP3 also inhibits the TLR2- and TLR4-mediated interleukin-8 synthesis in airway epithelial cells, suggesting that TNFAIP3 also acts as a negative regulator of TLR-mediated inflammatory responses, thereby protecting the host against harmful over-responses to pathogens. At least two isoforms of TNFAIP3 are known to exist.

Supplier: Prosci

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. [provided by RefSeq].

Supplier: Rockland Immunochemical

Karyopherin, a cytosolic and heterodimeric protein complex consisting of alpha and beta subunits, is responsible for targeting proteins with nuclear localization signals to the nuclear pore complex by an energy requiring, Ran-dependent mechanism. The alpha subunit and imported substrate enter the nucleus and accumulate in the nucleoplasm, while the beta subunit accumulates at the NPC. KPNA2 is the alpha subunit 2 of karyopherin, which forms a complex with importin subunit beta-1 and functions as a cargo carrier that transports various complexes from cytoplasm into nucleus. It is ubiquitously expressed and contains an IBB/importin beta domain, ten Armadillo repeats that bind "cargo" and three intervening nuclear localization sequences (NLSs). It has recently been reported to play an important role in tumorigenesis and tumor progression.

Supplier: Rockland Immunochemical

The p53 tumor-suppressor gene integrates numerous signals that control cell life and death. Several novel molecules involved in p53 pathway, including Chk2, p53R2, p53AIP1, Noxa, PIDD, and PID/MTA2, were recently discovered. The transcriptional activity of p53 is modulated by protein stability and acetylation. PID/MTA2, also termed MTA1-L1, was found to be a subunit of nucleosome remodeling and deacetylating (NRD/NuRD) complex. PID/MTA2 modulates the enzymatic activity of the histone deacetylase complex and its expression reduces the levels of acetylated p53. Deacetylation of p53 by PID/MTA2 represses p53-dependent transcriptional activation and modulates p53-mediated cell growth arrest and apoptosis. PID/MTA2 is ubiquitously expressed in human tissues.

Supplier: Prosci

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

Supplier: Rockland Immunochemical

SHANK proteins are scaffolding adaptors that have been shown to integrate neurotransmitter receptors into the cortical cytoskeleton at postsynaptic densities. SHANK1-3 of the SHANK/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). SHANK recruits betaPIX and PAK to dendritic spines to regulate postsynaptic structure and interacts with ionotropic receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development. Anti-SHANK1/SHANK3 is ideal for research in Neuroscience, including autism spectrum disorder, and Cell Adhesion.

Supplier: Rockland Immunochemical

The gene for CDK2NA generates several transcripts/proteins which differ from each other in their first exons. Three of these transcripts are generated by alternative splicing (isoform 1 a.k.a p16INK4A, isoform 2 and isoform 3 a.k.a p12), two of which are known to function as inhibitors of CDK4 kinase. One other transcript that is generated from this gene contains an alternate reading frame (ARF), with the first exon located 20kb upstream of the remainder of the gene (isoform 4 a.k.a. p14ARF, p19ARF, ARF). In spite of the structural and some functional differences, all the proteins encoded by the CDKN2A gene are involved in cell cycle G1 control.

Supplier: Rockland Immunochemical

Op18 belongs to the stathmin family of genes and encodes a ubiquitous cytosolic phosphoprotein that may function as an intracellular relay integrating several signaling pathways such as those involved in cell proliferation and differentiation. Op18 has also been shown to be involved in the regulation of the microtubule filament system by destabilizing microtubules, thereby preventing assembly and promoting the disassembly of microtubules. More recently, op18 has been implicated as a potential target of the ASK1-p38 MAP kinase cascade, suggesting that the ASK1-p38 cascade may regulate microtubule dynamics through op18. Op18 is highly expressed in a wide variety of human malignancies, including leukemia, prostate cancer, ovarian carcinoma, and breast carcinoma, suggesting that op18 may be an ideal target for anti-cancer therapeutics.

Supplier: Rockland Immunochemical

Neuroligin-1 is a neuronal cell surface protein belonging to the type-B carboxylesterase/lipase family. It is a necessary component in the maturation of excitatory synapses for their normal, functional development, and is necessary to the regulation of synaptic plasticity and the development of long-term memory within the adult amygdala in mammals. It is believed to participate in cell-cell-interaction through the assembly of intracellular junction by the binding of beta-neurexins, and may also be a factor in the maintenance and assembly of synaptic junctions. It is also thought to have involvement in excitatory synaptic specification. Within brain tissue, Neuroligin-1 is primarily observed in neurons and spinal cord. Anti-Neuroligin-1 is ideal for research in Neuroscience, including narcolepsy and synaptic neurotransmission: GABAergic inhibition, as well as Cell Adhesion.

Supplier: Rockland Immunochemical

POU5F1, also commonly known as Oct-4, is a maternally expressed octamer-binding protein that was the first transcription factor described for the early stages of development. The role of POU5F1 in embryonic development suggested that it might be useful in the creation of stem cells that might be useful in cell replacement therapies in the treatment of several degenerative diseases. Artificial stem cells, termed induced pluripotent stem (iPS) cells, can be created by expressing POU5F1 and the transcription factors Sox2, Klf4 and Lin28 along with c-Myc in mouse fibroblasts. More recently, experiments have demonstrated that iPS cells could be generated using expression plasmids expressing POU5F1, Sox2, KlfF4 and c-Myc, eliminating the need for virus introduction, thereby addressing a safety concern for potential use of iPS cells in regenerative medicine.

Supplier: Prosci

Anthrax Edema Factor Antibody: Anthrax infection is initiated by the inhalation, ingestion, or cutaneous contact with Bacillus anthracis endospores. B. anthracis produces three polypeptides that comprise the anthrax toxin: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA binds to two related proteins on the cell surface; these are termed tumor epithelial marker 8 (TEM8)/anthrax toxin receptor (ATR) and capillary morphogenesis protein 2 (CMG2), although it is still unclear which is physiologically relevant. Following PA binding to its receptor, PA is cleaved into two fragments by a furin-like protease. The bound fragment binds both LF and EF; the resulting complex is then endocytosed which allows the translocation of LF and EF into the cytoplasm. EF is a calmodulin and Ca++-dependent adenylate cyclase responsible for the edema seen in the disease. It is thought to benefit the B. anthracis bacteria by inhibiting cells of the host immune system.

Supplier: Prosci

TRAF2 Antibody: Tumor necrosis factor (TNF) receptor associated factors (TRAFs) were initially discovered as adaptor proteins that link the TNF receptor superfamily to signaling pathways and are thus important regulators of cell death and cellular response to stress. TRAF proteins share a homology region that allows them to bind to cell receptors and other TRAF proteins, causing the activation of different signal cascades depending on the TRAFs involved. For example, TRAF2 and TRAF3 directly bind to the CD40, a NF receptor superfamily member involved in inducing B cell immunity, and are critical for NF-kappa B activation in mouse B lymphocytes. TRAF2 along with TRAF6 has also been shown to be required for CD40 signaling in nonhemopoietic cells. TRAF2 also interacts with the TRFR superfamily member lymphotoxin-beta receptor (LTbetaR) in association with TRAF3 and the apoptosis inhibitors cIAP1 and Smac.

Supplier: Prosci

IRE1p Antibody: Accumulation of malfolded proteins in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) and the upregulation of the ER molecular chaperones GRP78 and GRP 94. These proteins are normally bound to ER transmembrane proteins such as IRE1p and ATF6 but ER stress causes their dissociation. This allows IRE1p, a serine-threonine protein kinase to transduce the unfolded protein signal from the ER to the nucleus. IRE1p also has an endoribonuclease activity that is required to splice X-box binding protein (XBP1) mRNA converting it to a potent UPR transcriptional activation. Depletion of IRE1p through the expression of a dominant negative form of IRE1p has no effect on transfected cells, but cell death via apoptosis occurs under stress conditions that cause unfolded proteins to accumulate in the ER. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Supplier: Prosci

Nanos3 Antibody: Nanos is a zinc-finger containing, RNA-binding protein that has been implicated in germ cell development in both invertebrates and vertebrates. In Drosophila, Nanos represses apoptosis during development to ensure proper germ-line development. Unlike Nanos1 whose expression in mice is dispensable, the Nanos2 and Nanos3 proteins are required for germ cell development. Nanos2-null primordial germ cells (PGCs) die only in the male gonads and show no defects in females, while Nanos3-null PGCs are lost during the migration stage regardless of sex. Nanos2 and Nanos3 have distinct expression patterns during embryo development, suggesting that these two proteins do not have redundant functions. However, expression of Nanos2 can at least partially replace Nanos3 function in a Nanos3-null background. Nanos3 expression can not rescue Nanos2-null defects.

Supplier: Prosci

CTRP1 Antibody: Adipose tissue of an organism plays a major role in regulating physiologic and pathologic processes such as metabolism and immunity by producing and secreting a variety of bioactive molecules termed adipokines. One highly conserved family of adipokines is adiponectin/ACRP30 and its structural and functional paralogs, the C1q/tumor necrosis factor-alpha-related proteins (CTRPs) 1-7. Unlike adiponectin, which is expressed exclusively by differentiated adipocytes, the CTRPs are expressed in a wide variety of tissues. These proteins are thought to act mainly on liver and muscle tissue to control glucose and lipid metabolism. An analysis of the crystal structure of adiponectin revealed a structural and evolutionary link between TNF and C1q-containing proteins, suggesting that these proteins arose from a common ancestral innate immunity gene. In obese (ob/ob) mice, RT-PCR analysis showed that mCTRP1 transcripts are seen at substantially higher levels in adipose tissues compared to those of normal mice.