You searched for: Antibodies

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Note: Conjugates of blue fluorescent dyes like CF®405S and CF®405M are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.CF® dyes are Biotium's next-generation fluorescent dyes. CF®594 is a deep red fluorescent dye (Ex/Em 593/614 nm). It yields the brightest conjugates among spectrally similar dyes, and has excellent photostability.

Supplier: Bioss

β-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a β-1,4 linkage to an acceptor sugar. There are seven members of the β-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. β-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. β-1,4-Gal-T7 uses manganese to catalyze the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding β-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterized by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits.β-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a ∫-1,4 linkage to an acceptor sugar. There are seven members of the β-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. β-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. β-1,4-Gal-T7 uses manganese to catalyze the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding β-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterized by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits.-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a ∫-1,4 linkage to an acceptor sugar.

Supplier: Prosci

MCM3 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein is a subunit of the protein complex that consists of MCM2-7. It has been shown to interact directly with MCM5/CDC46. This protein also interacts with, and thus is acetlyated by MCM3AP, a chromatin-associated acetyltransferase. The acetylation of this protein inhibits the initiation of DNA replication and cell cycle progression.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein is a subunit of the protein complex that consists of MCM2-7. It has been shown to interact directly with MCM5/CDC46. This protein also interacts with, and thus is acetlyated by MCM3AP, a chromatin-associated acetyltransferase. The acetylation of this protein inhibits the initiation of DNA replication and cell cycle progression.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein is a subunit of the protein complex that consists of MCM2-7. It has been shown to interact directly with MCM5/CDC46. This protein also interacts with, and thus is acetlyated by MCM3AP, a chromatin-associated acetyltransferase. The acetylation of this protein inhibits the initiation of DNA replication and cell cycle progression. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Bioss

Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).

Supplier: Thermo Scientific

Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13. 4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several 'framework' genes are found in all haplotypes (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response.

Supplier: Rockland Immunochemical

Supplier: Bioss

β-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a β-1,4 linkage to an acceptor sugar. There are seven members of the β-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. β-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. β-1,4-Gal-T7 uses manganese to catalyze the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding β-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterized by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits.β-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a ∫-1,4 linkage to an acceptor sugar. There are seven members of the β-1,4-Gal-T family, all of which are directed to the golgi apparatus through a hydrophobic sequence at the N-terminus. β-1,4-Gal-T7, also known as B4GALT7 or XGALT1, is a 327 amino acid single-pass type II membrane protein that is expressed at high levels in heart, pancreas and liver. β-1,4-Gal-T7 uses manganese to catalyze the UDP-dependent biosynthesis of glycosphingolipids. The gene encoding β-1,4-Gal-T7 is mutated in Ehlers-Danlos syndrome progeroid type (EDSP), a variant form of Ehlers-Danlos syndrome characterized by progeroid facies, mild mental retardation, short stature, skin hyperextensibility, moderate skin fragility, joint hypermobility principally in digits.-1,4-galactosyltransferases (β-1,4-Gal-T) are type II membrane-bound glycoproteins that are substrate-specific and function to transfer galactose in a ∫-1,4 linkage to an acceptor sugar.

Supplier: Bioss

Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7.

Supplier: Bioss

Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.

Supplier: Bioss

Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.

Supplier: Thermo Scientific

There are two proteins encoded by this gene, oxytocin and neurophysin I. Oxytocin is posterior pituitary hormone which is synthesized as an inactive precursor in the hypothalamus along with its carrier protein neurophysin I. Together with neurophysin, it is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. The precursor seems to be activated while it is being transported along the axon to the posterior pituitary. This hormone contracts smooth muscle during parturition and lactation. It is also involved in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions.

Supplier: Thermo Scientific

Catechol-O-methyltransferase catalyzes the transfer of a methyl group from S-adenosylmethionine to catecholamines, including the neurotransmitters dopamine, epinephrine, and norepinephrine. This O-methylation results in one of the major degradative pathways of the catecholamine transmitters. In addition to its role in the metabolism of endogenous substances, COMT is important in the metabolism of catechol drugs used in the treatment of hypertension, asthma, and Parkinson disease. COMT is found in two forms in tissues, a soluble form and a membrane-bound form . The differences between S-COMT and MB-COMT reside within the N-termini. Several transcript variants are formed through the use of alternative translation initiation sites and promoters.

Supplier: Thermo Scientific

PA5-16918 targets CD138 in IHC applications and shows reactivity with Human samples. The PA5-16918 immunogen is recombinant protein encoding aa 18-218 human CD138. CD138/Syndecan-1 is a transmembrane heparin sulphate proteoglycan which is made up of one core protein and five glycosaminoglycan. CD138 is expected to play a role in cell adhesion. It is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. It is a selective marker for B cell lymphoblastic leukemia and lymphoplasmocytoid leukemia. It is lost from the apoptotic myeloma cells; hence is a useful marker for viable myeloma cells.

Supplier: Thermo Scientific

MAGEB2 is a member of the MAGEB gene family. The members of this family have their entire coding sequences located in the last exon, and the encoded proteins show 50 to 68% sequence identity to each other. The promoters and first exons of the MAGEB genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls. This gene is localized in the DSS (dosage-sensitive sex reversal) critical region. It is expressed in testis and placenta, and in a significant fraction of tumors of various histological types. The MAGEB genes are clustered on chromosome Xp22-p21.

Supplier: Thermo Scientific

GIPR also called glucose-dependent insulinotropic polypeptide, is a 42-amino acid polypeptide synthesized by K cells of the duodenum and small intestine. This protein was originally identified as an activity in gut extracts that inhibited gastric acid secretion and gastrin release, but subsequently was demonstrated to stimulate insulin release potently in the presence of elevated glucose. The insulinotropic effect on pancreatic islet beta-cells was then recognized to be the principal physiologic action of GIP. Together with glucagon-like peptide-1, GIP is largely responsible for the secretion of insulin after eating. The protein is involved in several other facets of the anabolic response.

Supplier: Bioss

Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A.

Supplier: Bioss

Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors. Isoform TrkA-III is resistant to NGF, constitutively activates AKT1 and NF-kappa-B and is unable to activate the Ras-MAPK signaling cascade. Antagonizes the anti-proliferative NGF-NTRK1 signaling that promotes neuronal precursors differentiation. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed.

Supplier: Thermo Scientific

The maf oncogene was identified by structural analysis of the AS42 avian transforming retrovirus genome. The Maf family is divided into two subclasses, large Mafs (vMaf, cMaf, MafB and Nrl) and small Mafs (MafF, MafK, and MafG). Both subclasses contain leucinezipper motifs, which allow homodimerization as well as heterodimerization with a variety of other bZip transcription factors. Large Mafs also contain an acidic transactivation domain absent in the small Maf proteins. Although they do not possess inherent transactivation activity, small Maf proteins can act as positive regulators of transcription by targeting transcriptionally active dimerization partners to specific DNA regulatory elements. Conversely, small Mafs can act also as negative regulators of transcription by recruiting transcriptional repressors or by forming homodimers that can replace active dimers. Human MafF was isolated in a yeast one-hybrid system from a human myometrium cDNA library. Human MAFF encodes a 164 amino acids proten. Like other small MAFF proteins, it contains an extended leucine zipper structure and lacks an N-terminal transactivating domain. The three small Maf proteins have been implicated in a number of physiological processes, including development, differentiation, haematopoiesis and stress response. Interestingly, these three proteins regulate the stress response via different mechanisms.

Supplier: Rockland Immunochemical

Rat IgG Fab Fragment

Supplier: Bioss

Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence.

Supplier: Thermo Scientific

Bad is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin are found to be involved in the regulation of this protein. Bad is phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation

Supplier: Bioss

Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).

Supplier: Thermo Scientific

Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of VHL gene is the basis of familial inheritance of VHL syndrome. The protein is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein.

Supplier: Thermo Scientific

PA5-16681 targets Calretinin in IHC (P) applications and shows reactivity with Human, mouse, and Rat samples. The PA5-16681 immunogen is recombinant full-length mouse calretinin protein. Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

Supplier: Thermo Scientific

DUSP4 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. DUSP4 inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus.

Supplier: Thermo Scientific

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. PKC eta is one of the PKC family members. This protein is most abundant in lung, less in heart and skin.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.