29728 Results for: "Sodium perforated tetrahydrate"

Supplier: Prosci

This gene encodes tumor protein p73, which is a member of the p53 family of transcription factors involved in cellular responses to stress and development. The family members include p53, p63, and p73 and have high sequence similarity to one another, which allows p63 and p73 to transactivate p53-responsive genes causing cell cycle arrest and apoptosis. The family members can interact with each other in many ways involving direct or indirect protein interactions, resulting in regulation of the same target gene promoters or regulation of each other's promoters. The p73 protein is expressed at very low levels in normal tissues and is differentially expressed in a number of tumors. The p73 gene expresses at least 35 mRNA variants due to the use of alternate promoters, alternate translation initiation sites, and multiple splice variations. Theoretically this can account for 29 different p73 isoforms; however, the biological validity and the full-length nature of most variants have not been determined.

Supplier: Rockland Immunochemical

Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. Members of the Bcl-2 family are known to be critical regulators of this process. These proteins are characterized by the presence of several conserved motifs termed Bcl-2 homology (BH) domains. A novel, widely expressed member termed Bcl-rambo was recently identified. This protein is localized to mitochondria in mammalian cells and its overexpression induces apoptosis which could be blocked by co-expression of inhibitor of apoptosis proteins (IAPs) such as XIAP, cIAP1, and cIAP2. Bcl-rambo shows overall homology to the anti-apoptotic members containing BH motifs, but unlike Bcl-2, the C-terminal membrane anchor of Bcl-rambo is preceded by a unique 250 amino acid insertion. This region by itself can induce apoptosis more efficiently than the Bcl-2 homology regions, suggesting that Bcl-rambo may be important other pro-apoptotic pathways.

Supplier: Prosci

Progesterone receptors (PRs) are nuclear hormone receptors of the NR3C class, which also includes mineralocorticoid, glucocorticoid and androgen receptors. They exist as homodimers coupled to Hsp90 or HMGB proteins, which are shed upon activation. The major signaling pathway used by progesterone receptors is via direct DNA binding and transcriptional regulation of target genes. They can also signal by binding to other proteins, mainly with transcription factors such as NF-κB, AP-1 or STAT. Progesterone receptors are found in the female reproductive tract, mammary glands, brain and pituitary gland and receptor expression is induced by estrogen. Well established functions of progesterone receptors include ovulation, implantation, mammary gland development and maintenance of pregnancy. In addition, progesterone, signaling through the progesterone receptor, increases the ventilatory response of the respiratory centers to carbon dioxide and decreases arterial and alveolar PCO2 in the luteal phase of the menstrual cycle and during pregnancy. The human gene encoding the progesterone receptor has been localized to 11q22.

Supplier: Prosci

GFP (Green fluorescence protein) is a 27 kDa protein derived from the jellyfish Aequorea victoria, which emits green light when excited by blue light. GFP cDNA produces a fluorescent product when expressed in prokaryotic cells, without the need for exogenous substrates or cofactors. GFP has become an invaluable tool in cell biology research, since its intrinsic fluorescence can be visualized in living cells. GFP fluorescence is stable under fixation conditions and suitable for a variety of applications. GFP has been widely used as a reporter for gene expression, enabling researchers to visualize and localize GFP-tagged proteins within living cells without the need for chemical staining. Other applications of GFP include assessment of protein protein interactions through the yeast two hybrid system and measurement of distance between proteins through fluorescence energy transfer (FRET) protocols. GFP technnology has considerably contributed to a greater understanding of cellular physiology.

Supplier: Prosci

Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of HDAC family have been identified in the past several years. These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

Supplier: Prosci

Gli-2 (also known as Zinc Finger Protein Gli-2, GLI-Kruppel family member GLI-2 or Tax helper protein) belongs to the C2H2-type zinc finger protein subclass of the Gli family. Members of this subclass are characterized as transcription factors that bind DNA through zinc finger motifs. These motifs contain conserved H-C links. Gli family zinc finger proteins are mediators of Sonic hedgehog (Shh) signaling, and they are implicated as potent oncogenes in the embryonal carcinoma cell. The protein encoded by this gene localizes to the cytoplasm and activates patched Drosophila homolog (PTCH) gene expression. Gli-2 is also thought to play a role during embryogenesis. The encoded protein is associated with several phenotypes: Greig cephalopolysyndactyly syndrome, Pallister-Hall syndrome, pre-axial polydactyly type IV, post-axial polydactyly types A1 and B. Expression has been reported for this mRNA in human testis, myometrium, kidney, lung, glioblastomas, and embryonal cell carcinomas. Multiple splice variants have been reported for this protein.

Supplier: Prosci

Tyrosine-protein kinase (TYRO3) belongs to the Tyr protein kinase family (AXL/UFO subfamily). The UFO family of receptor tyrosine kinases is comprised of subfamily members Rse(also referred to as Tyro3 or Sky) and UFO (also called Tyro7 or Axl). Two distinct isoforms of Rse, designated Brt and Etk-2, have been described. Brt differs from Rse at its C-terminus, but more importantly lacks the N-terminal 31 amino acid signal peptide sequence present in Rse, which is replaced by a 27 amino acid Brt-specific sequence. It has been suggested that as a result of this alternative splicing event, Brt resides in the cytoplasm, unlike Rse which is expressed on the cell surface. Ekt-2 also lacks an N-terminal signal peptide which is substituted with a 45 amino acid Ekt-2-specific sequence. Protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation.

Supplier: Rockland Immunochemical

Human immunodeficiency virus (HIV) and related viruses require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b and CCR8 in the chemokine receptor family, and four new human molecules GPR15, STRL33, GPR1 and V28 were recently identified as HIV coreceptors. Among them, CXCR4 is a principal coreceptor for T-cell tropic strains of HIV-1 fusion and entry of human white blood cells. CXCR4 is also required for the infection by dual-tropic strains of HIV-1 and mediates CD-4 independent infection by HIV-2. The alpha-chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1. CXCR4 associates with the surface CD4-gp120 complex before HIV enters target cells. CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells. The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV binding sites.

Supplier: Prosci

RPS6KB1 phosphorylates the Ribosomal Protein-S6. Activation of RPS6KB1 requires a complex, ordered series of conformational changes and phosphorylation reactions. While the role of sequential, multi-site phosphorylation has been extensively detailed, characterization of the priming step required to initiate this cascade has remained elusive. Probably this priming process is dependent on calcium. Calcium-dependent regulation of RPS6KB1 does not specifically target Thr-229 and Thr-389, the key regulatory phosphorylation sites; rather, calcium chelation results in a global inhibition of RPS6KB1 phosphorylation. The initial calcium-dependent process is required to release an inhibitory interaction between the C- and N-termini of RPS6KB1, thus allowing phosphorylation of key domains. The priming event involves formation of a calcium-dependent protein complex that releases the interaction between the N- and C-termini. RPS6KB1 is then accessible for activation by the kinases that target the known regulatory phosphorylation sites.

Supplier: Rockland Immunochemical

Adiponection antibody detects human adiponectin. 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 the CTRPs, which are expressed in a wide variety of tissues, adiponectin is reported to be expressed exclusively by differentiated adipocytes. 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. It is present in high levels in normal human plasma, but is reduced in obese subjects and often in those with increased insulin resistance and type 2 diabetes, suggesting that adiponectin may be a useful pharmacological target in various metabolic diseases. Anti-Adiponectin antibodies are ideal for investigators involved in glucose engery metabolism and apolipoprotein research.

Supplier: Prosci

Progesterone receptors (PRs) are nuclear hormone receptors of the NR3C class, which also includes mineralocorticoid, glucocorticoid and androgen receptors. They exist as homodimers coupled to Hsp90 or HMGB proteins, which are shed upon activation. The major signaling pathway used by progesterone receptors is via direct DNA binding and transcriptional regulation of target genes. They can also signal by binding to other proteins, mainly with transcription factors such as NF-κB, AP-1 or STAT. Progesterone receptors are found in the female reproductive tract, mammary glands, brain and pituitary gland and receptor expression is induced by estrogen. Well established functions of progesterone receptors include ovulation, implantation, mammary gland development and maintenance of pregnancy. In addition, progesterone, signaling through the progesterone receptor, increases the ventilatory response of the respiratory centers to carbon dioxide and decreases arterial and alveolar PCO2 in the luteal phase of the menstrual cycle and during pregnancy. The human gene encoding the progesterone receptor has been localized to 11q22.

Supplier: Prosci

Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation.

Supplier: Rockland Immunochemical

5-hydroxymethylcytosine (5-hmC) has been recently discovered in mammalian DNA. This results from the enzymatic conversion of 5-methylcytosine into 5-hydroxymethylcytosine by the TET family of oxygenases. So far, the 5-hmC bases have been identified in Purkinje neurons, in granule cells and embryonic stem cells where they are present at high levels (up to 0,6% of total nucleotides in Purkinje cells). Preliminary results indicate that 5-hmC may have important roles distinct from 5-mC. Although its precise role has still to be shown, early evidence suggests a few putative mechanisms that could have big implications in epigenetics: 5-hydroxymethylcytosine may well represent a new pathway to demethylate DNA involving a repair mechanism converting 5-hmC to cytosine and, as such open up entirely new perspectives in epigenetic studies. Due to the structural similarity between 5-mC and 5-hmC, these bases are experimentally almost indistinguishable. Recent articles demonstrated that the most common approaches (e.g. enzymatic approaches, bisulfite sequencing) do not account for 5-hmC. The development of the affinity-based technologies appears to be the most powerful way to differentially and specifically enrich 5-mC and 5-hmC sequences. Anti-5hmC Antibody is ideal for research in Epigenetics and Gene Expression.

Supplier: Rockland Immunochemical

CXCR4 antibody detects a G coupled -protein receptor. Human immunodeficiency virus (HIV) and related viruses require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b and CCR8 in the chemokine receptor family, and four new human molecules GPR15, STRL33, GPR1 and V28 were recently identified as HIV coreceptors. Among them, CXCR4 (fusin, LESTR or HUMSTR) is a principal coreceptor for T-cell tropic strains of HIV-1 fusion and entry of human white blood cells. CXCR4 is also required for the infection by dual-tropic strains of HIV-1 and mediates CD-4 independent infection by HIV-2. The a-chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1. CXCR4 associates with the surface CD4-gp120 complex before HIV enters target cells. CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells. The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV binding sites. Anti-CXCR4 antibodies are ideal for investigators involved in Cytokines and Growth Factors or Infectious Disease reasearch.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. /IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

Supplier: Prosci

Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA. On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.

Supplier: Prosci

Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-κ-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652', leading to activate the NF-κ-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters.

Supplier: Thermo Fisher Scientific

Accurately monitor pH, ion concentration, mV, ORP, and temperature with the Orion™ Star™ A324 pH/ISE Portable Meter for challenging field testing.

Supplier: Rockland Immunochemical

EBI3 is a subunit in two distinct heterodimeric cytokines: interleukin-27 (IL-27) and IL-35. Like interleukin-23 (IL-23), IL-27 is a recently discovered member of the IL-6/IL-12 family of proinflammatory and immunoregulatory cytokines. It exists as a heterodimer composed of the p40-related protein EBI3 and an IL-12 p35-related protein termed p28. IL-27 is produced after activation by antigen-presenting cells and induces proliferation of naïve but not memory CD4+ T-cells. It acts by binding to its receptor WSX-1 (also known as TCCR) and gp130 which results in the activation of a Jak/STAT signaling cascade, suggesting the IL-27 is involved in the regulation of immune processes. It has been suggested that IL-27 can also be used as a therapeutic agent against cancer as it can also induce tumor-specific anti-tumor activity mediated through CD8+ T-cells, IFN-gamma, and T-bet. IL-35 is composed of EBI3 and the p35 subunit of IL-12 and has been reported to have therapeutic effects against collagen-induced arthritis by expanding the population of regulatory T cells and suppressing Th17 cells. At least two isoform of EBI3 are known to exist.

Supplier: Rockland Immunochemical

Combo Pack: This primary and secondary antibody pair comes with matched antibody pairs to detect and quantify endogenous protein levels of human AKT3. AKT3 Antibody detects AKT3 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. Anti-AKT3 Antibody is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

Supplier: Rockland Immunochemical

Combo Pack: This primary and secondary antibody pair comes with matched antibody pairs to detect and quantify endogenous protein levels of human AKT2. AKT2 Antibody detects AKT2 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. Anti-AKT2 Antibody is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

Supplier: Prosci

Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila).Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle,that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein, also designated MEN)
functions as an RNA polymerase II elongation factor that increases the rateof transcription by suppressing transient pausing by RNA polymerase II. Also, ELL is thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, and has lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary.The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes which undergo translocation with the MLL gene on chromo-some 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia,also designated ALL-1 and HRX) is a 430 kDa protein that regulates embryonal and hematopoietic development.

Supplier: Prosci

Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: Rockland Immunochemical

Combo Pack: This primary and secondary antibody pair comes with matched antibody pairs to detect and quantify endogenous protein levels of human AKT1. AKT1 Antibody detects AKT1 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. Anti-AKT1 Antibody is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

Supplier: Rockland Immunochemical

BRSK1 was initially identified as a mammalian homolog to the fission yeast S. pombe Cdr2, a mitosis-regulatory kinase and also shows significant homology to the C. elegans neuronal cell polarity regulator SAD1. BRSK1 is unbiquitously expressed, with highest levels of expression in the brain and testes. Similar to its yeast homolog, BRSK1 is thought to be involved in stress-induced cell cycle arrest. Overexpression of this protein leads to the G2/M arrest in HeLa S2 cells and UV-induced G2/M arrest could be partially abrogated by reduced expression of BRSK1 through the use of siRNA, indicating its role in DNA damage checkpoint function. More recently, it has been shown that both BRSK1 and the related protein BRSK2 are required for mammalian neuronal polarization. While BRSK1- and BRSK2-null mice were viable, double-mutant mice died within two hours of birth. Neurons from these mice showed uniformly-sized neurites as opposed to the normal long axon and multiple shorter dendrites. These neurites also displayed both axonal and dendritic markers. At least two isoforms of BRSK1 are known to exist.

Supplier: Rockland Immunochemical

Avian Influenza Neuraminidase Antibody detects internal portion of the protein. Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. Although it has been known that cleavage site and glycosylation patterns of the HA protein play important roles in determining the pathogenicity of H5 avian influenza viruses, it has only recently been shown that an additional glycosylation site within the globular head of the NA protein also contributes to the high virulence of the H5N1 virus. Anti-Avian Influenza Neuraminidase antibodies are ideal for investigators involved in infectious disease reseach.

Supplier: Prosci

A-Raf, B-Raf and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway. Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497 and Ser499. p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338 and the Src family phosphorylates Tyr341 to induce c-Raf activity (3, 4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf. Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6, 7). While A-Raf, B-Raf and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428 and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8, 9). The B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301 and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to

Supplier: Rockland Immunochemical

The nuclear factor NF-kB plays key roles in development and immunity. ABIN3 (A20-binding inhibitor of NF-kB activation 3), also known as TNFAIP3-interacting protein 3 (TNIP3), is a novel negative feedback regulator of LPS-induced NF-kB activation. ABIN3 is a 39 kDa protein that negatively regulates NF-kB activation in response to TNF and LPS. ABIN3 is highly expressed in brain, thymus, lymph node, lung and fetal liver, with low expression in kidney, bone marrow. Through its interaction with A20, ABIN3 interferes with TRAF2-mediated transactivation signals and NF-kB inhibition is mediated by the ABIN-homology domain 2. ABIN3 has been found to be induced by Listeria infection and can be slightly downregulated by dexamethasone. Enhanced expression of ABIN3 in monocytes is associated with sepsis. Thus, ABIN3 is an IL-10-induced gene product capable of attenuating NF-kB in human macrophages yet is inoperative in mice and represents a basis for species-specific differences in IL-10 actions. At least four isoforms of ABIN3 are known to exist.

Supplier: Rockland Immunochemical

CCR5 antibody detects a G coupled -protein receptor. Human immunodeficiency virus (HIV) and related virus require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b and CCR8 in the chemokine receptor family, and four new human molecules GPR15, STRL33, GPR1 and V28 were recently identified as HIV coreceptors. Among them, CCR5 (CC-CKR-5) is a principal coreceptor for macrophage- and dual-tropic HIV-1 strains fusion and entry of human white blood cells. CCR5 is required for the infection by HIV-1, HIV-2, and SIV. The beta-chemokines RANTES, MIP-alpha and MIP-beta are the ligands for CCR5 and prevent infection by M-tropic HIV-1. CXC5 associates with the surface CD4-gp120 of HIV complex and leads to membrane fusion and virus entry of target cells. The amino-terminal domain and the extracellular loops of CCR5 serve as HIV biding sites. CCR5 messenger RNA is expressed in lymphoid organs and monocytes. Anti-CCR5 antibodies are ideal for investigators involved in Cytokines and Growth Factors and Infectious Disease research.