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4-(Dimethylamino)-3-nitrobenzoic+acid
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4-(Dimethylamino)-3-nitrobenzoic+acid
Catalog Number:
(10264-384)
Supplier:
Bioss
Description:
Dyrk (for dual specificity tyrosine phosphorylation regulated kinase) is the homolog of the Drosophila mnb (minibrain) gene which is required for neurogenesis. Dyrk is a dual-specificity tyrosine kinase and serine/threonine kinase, which is itself regulated by tyrosine phosphorylation. Several mammalian Dyrk related proteins have been identified and are thought to compose a family of dual specificity protein kinases. Dyrk family members, including Dyrk1A (dual specificity tyrosine-phosphorylation-regulated kinase 1A), Dyrk1B, Dyrk1C, Dyrk2, Dyrk3, Dyrk4A and Dyrk4B, are thought to be involved in diverse cellular functions. Localized to the nucleus and highly expressed in testis, muscle and the developing nervous system, Dyrk1A, also known as MNB or MNBH, functions to phosphorylate serine, threonine and tyrosine residues on various substrates involved in signaling pathways that regulate cell proliferation. Dyrk1A is a candidate gene for learning defects that are involved in Downs syndrome (DS), suggesting a possible role for Dyrk1A in the development of DS. Four isoforms of Dyrk1A exist due to alternative splicing events.
Catalog Number:
(10303-968)
Supplier:
Bioss
Description:
MOZ (monocytic leukemia zinc finger protein) is a chromatin-associated histone acetyltransferase (HAT) that regulates chromatin remodeling and transcription. The MOZ gene was initially isolated as a consequence of two variant translocations that were identified in a distinct subtype of acute myeloid leukemias and resulted in the formation of MOZ fusion proteins. These fusions involve the HAT domain of MOZ with the activation domain of either transcriptional coactivator protein TIF2/GRIP1 or CBP, and lead to enhanced transcriptional activation by a mechanism involving aberrant histone acetylation. Additional MOZ related proteins, including MORF (MOZ related factor) and TIP60 (TAT interacting proteins 60), share significant similarities with MOZ including the putuative HAT domain. MORF also contains a strong transcriptional repression domain at its N terminus and a highly potent activation domain at the C terminus, suggesting that MORF has both HAT activity and contributes to the regulation of transcriptional activation. TIP60 was originally identified as a coactivator for the HIV TAT protein and also functions as a nuclear hormone receptor coactivator that enhances ligand dependent steroid receptor-mediated transactivation involving the androgen, estrogen and progesterone receptors.
Catalog Number:
(10301-378)
Supplier:
Bioss
Description:
Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.
Catalog Number:
(10265-040)
Supplier:
Bioss
Description:
The LIM-only (LMO) proteins, LMO1 and LMO2, are nuclear factors that are characterized by a conserved LIM domain. The LIM domain consists of a cysteine-rich zinc-binding motif that is present in a variety of transcription factors, including the LIM homeobox (LHX) proteins expressed in the central nervous system and involved in cell differentiation. LMO1 and LMO2 are expressed in the adult CNS in a cell type-specific manner, where they are differentially regulated by neuronal activity and are involved in regulating the cellular differentiated phenotype of neurons. LMO2 lacks a specific DNA-binding homeobox domain but rather assembles into transcriptional regulatory complexes to mediate gene expression by interacting with the widely expressed nuclear LIM interactor (NLI). NLI, known also as CLIM-1, and the related protein CLIM-2, facilitate the formation of heteromeric LIM complexes and also enhance the nuclear retention of LIM proteins. LMO2 and the related protein LMO4 are expressed in thymic precursor cells. LMO4 is also expressed in mature T cells, cranial neural crest cells, somite, dorsal limb bud mesenchyme, motor neurons, and Schwann cell progenitors.
Catalog Number:
(10291-296)
Supplier:
Bioss
Description:
Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.
Catalog Number:
(10282-580)
Supplier:
Bioss
Description:
APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.
Catalog Number:
(10252-674)
Supplier:
Bioss
Description:
CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.
Catalog Number:
(10325-024)
Supplier:
Bioss
Description:
The p21 activated kinases (PAK) are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and RAC1, and have been implicated in a wide range of biological activities. The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in regulating the apoptotic events in the dying cell.P21-activated kinase (PAK) is actually a family of serine/threonine protein kinases, members of which are activated by small molecular weight GTPases. The three most common isoforms are PAK 1, PAK 2, and PAK 3 (also known as alpha PAK, gamma PAK, and beta PAK, respectively). These kinases contain numerous regulatory elements that trigger diverse signaling processes such as those initiated by activated GTPases, interaction with Src homology 3 (SH3) domains, and caspase mediated proteolytic cleavage. Autophosphorylation of serine 141 (serine 144 for PAK 1 and serine 139 PAK 3), catalyzed by Cdc42, is required for activation of PAK.
Catalog Number:
(10282-764)
Supplier:
Bioss
Description:
Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.
Catalog Number:
(10240-674)
Supplier:
Bioss
Description:
Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Catalog Number:
(10286-142)
Supplier:
Bioss
Description:
The transcription factor GA-binding protein (GABP) is composed of two subunits, the Ets-related GABP-alpha and a GABP-alpha-associated subunit, GABP beta. GABP alpha binds to a specific DNA sequence and GABP beta exists as b1 and b2 splice variants that differ in their C-termini. In primary neuronal cultures, GABP beta is expressed in both the cytoplasm and the nucleus, whereas GABP alpha is expressed mainly in the nucleus. GABP is constitutively expressed as either a GABP alpha beta heterodimer or a GABP alpha b heterotetramer, both of which can modify GABP-dependent transcription in vitro and in vivo. The GABP alpha beta tetrameric complex performs many different functions, such as stimulating transcription of the adenovirus E4 gene, differentially activating BRCA1 expression in human breast cell lines, potentiating Tat-mediated activation of long terminal repeat promoter transcription and viral replication in certain cell types, acting as a coordinator of mitochrondrial and nuclear transcription for cytochrome oxidase in neurons and assisting in the regulation of rpL32 gene transcription.
Catalog Number:
(10252-630)
Supplier:
Bioss
Description:
Myosin VI a molecular motor involved in intracellular vesicle and organelle transport, is the only Myosin motor that binds to the pointed end of Actin. This unique Myosin has only one light chain in the lever-arm domain and has highly irregular stepping with a wide range of step sizes, unlike that of other characterized Myosins. It associates with Clathrin-coated vesicles and disabled 2, indicating a role for Myosin VI in endocytosis. Mouse Myosin VI is expressed within the sensory hair cells of the cochlea. Human Myosin VI is mapped to the centromeric region of chromosome 6, a region that shows syntenic homology with the corresponding mouse chromosome 9 region, where the Snell’s Waltzer mutation is located. The behavioral effects of the mouse Snell’s Waltzer mutation are lack of responsiveness to sound, hyperactivity, head tossing and circling, due to the disorganization and fusing of stereocilia bundles within the inner ear. Defects of Myosin VI cause autosomal dominant nonsyndromic sensori-neural deafness in humans. Human Myosin VI is expressed in fetal cochlea and brain, as well as in adult brain.
Catalog Number:
(10233-678)
Supplier:
Bioss
Description:
Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases.
Catalog Number:
(89331-144)
Supplier:
Genetex
Description:
Purity: Purified by protein A chromatography or sequential differential precipitations Species Reactivity: Bacteria Tested Applications: ELISA Pkg Size: 500 ul
Catalog Number:
(10408-982)
Supplier:
Bioss
Description:
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).
Catalog Number:
(10420-830)
Supplier:
Bioss
Description:
Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B.
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