381460 Results for: "single-use assemblies"

Supplier: Rockland Immunochemical

Signal transducer and activator of transcription 3 (Stat3) belongs to a family of cytoplasmic transcription factors that can be activated by phosphorylation by its cell surface receptor. Stat3 plays a key role in many cellular processes such as cell growth and apoptosis. It also mediates cellular responses to interleukins, KITLG/SCF,EGF, IFN-alpha and other growth factors and may mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Stat3 forms a homodimer or a heterodimer with a related family member (e.g. STAT1). Activation occurs through phosphorylation of tyrosine 705 and serine 727. Phosphorylation of Stat3 at Tyr705 induces Stat3 dimerization and nuclear translocation. Serine phosphorylation is important for stable DNA-binding of Stat3 homodimers and maximal transcriptional activity. Stat3 can have a dual role in cancer, it has been found that Stat3 protein can promote oncogenesis and have a tumor suppressor role depending upon the mutational background of the tumor.

Supplier: Rockland Immunochemical

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy. Anti-Histone H3 are ideal for researchers interested in Chromatin Modifiers, Chromatin Research, Histones and Modified Histones, and Epigenetics Research.

Supplier: Rockland Immunochemical

Histone modifications mediate changes in gene expression by altering chromatin structure or by serving as a platform to recruit other proteins. LSD1 is a recently discovered amine oxidase that catalyzes the lysine-specific demethylation of histone proteins via an FAD-dependent oxidative reaction. Methylation on histone H3-K9 is thought to play an important role in heterochromatin formation, while methylation on arginine and some lysine residues (such as H3-K4) is associated with active transcription. LSD1 associates with various proteins, including HDAC1/2, CoREST, and BHC80, that act to regulate LSD1 activity in vivo, and in a histone H3-K4-specific methylase complex that is involved in transcriptional regulation. Experiments have shown that CoREST, a SANT domain-containing corepressor acts to enhance LSD1 activity, while BHC80, a PHD domain-containing protein, inhibits CoREST/LSD1 activity in vitro. LSD1-mediated histone demethylation thus may have significant effects on gene expression.

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

There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Supplier: Rockland Immunochemical

The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.

Supplier: Prosci

Myogenin is a member of the MyoD family of myogenic basic helix-loop-helix (bHLH) transcription factors that also includes MyoD, Myf-5, and MRF4 (also known as herculinor Myf-6). MyoD family members are expressed exclusively in skeletal muscle and play a key role in activating myogenesis by binding to enhancer sequences of muscle-specific genes. The regulatory domain of MyoD is approximately 70 amino acids in length and includes both a basic DNA binding motif and a bHLH dimerization motif. MyoD family members share about 80% amino acid homology in their bHLH motifs. Myogenin antibody labels the nuclei of myoblasts in developing muscle tissue, and is expressed in tumor cell nuclei of rhabdomyosarcoma and some leiomyosarcomas. Positive nuclear staining may occur in Wilms’ tumor.

Supplier: Prosci

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). [UniProt]

Supplier: Prosci

ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

Supplier: Genetex

Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor form of all caspases is composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a2b2 tetramer to form the active enzyme. Gene for Caspase 3 also known as Yama, CPP32, and apopain codes for a 32-kDa protein. Caspase 3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other Caspase 3 substrates include DNA-PK, actin, GAS2, and procaspase-6, etc. Caspase 3 is activated by cleavage events at Asp-28/Ser-29 (between N-terminal pro-domain) and Asp-175/Ser-176 (between large and small subunits) to generate a large subunit of 17-kDa and a small subunit of 12-kDa.

Supplier: Prosci

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. PSME3 is the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring.The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.

Supplier: TCI America

CAS Number: 3829-86-5 MDL Number: MFCD00150061 Molecular Formula: C12H8N2 Molecular Weight: 216.67 Purity/Analysis Method: 99.0% (T) Form: Crystal

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) Alkaline Phosphatase antibody generated in rabbit detects specifically monkey IgG heavy and light chains. Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. IgG binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsinization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present. This alkaline phosphatase conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform western blots, ELISAs, and more general immunoassays. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment.

Supplier: SLICE, INC.

Sturdy and flexible, this versatile tool kit shows craftsmanship in every stitch. Sixteen pockets of varying widths carry all your tools and a zipped pocket holds small loose items. Straps adjust to keep roll up secure. Coated for weather resistance and double stitched for maximum strength.

Supplier: Genetex

Four distinct colony-stimulating factors (CSFs) that promote survival, proliferation and differentiation of bone marrow precursor cells have been well characterized: granulocyte macrophage CSF (GMCSF), granulocyte CSF (GCSF), macrophage CSF (MCSF), and Interleukin-3 (IL-3, Multi CSF). Both GMCSF and IL-3 are multipotential growth factors, stimulating proliferation of progenitor cells from more than one hematopoietic lineage. In contrast, GCSF and MCSF are lineage restricted hematopoietic growth factors, stimulating final mitotic divisions and the terminal cellular maturation of the partially differentiated hematopoietic progenitors. Macrophage CSF, also known as CSF1, is produced by monocytes, fibroblasts and endothelial cells. It stimulates the formation of macrophage colonies, enhances antibody-dependent, cell-mediated cytotoxicity by monocytes and macrophages, and inhibits bone resorption by osetoclasts. Natural human MCSF is a dimeric glycoprotein of 70-90 kD molecular weight, existing in multiple glycosylation forms. It binds to a 165 kD glycoprotein of the receptor tyrosine kinase subclass III, a family that includes the receptors for platelet derived growth factor (PDGF) and stem cell factor (SCF).

Supplier: Rockland Immunochemical

SHOC2 protein participates in protein binding / transferase activity in the fibroblast growth factor receptor signaling pathway and Ras protein signal transduction. It is a widely expressed protein composed almost entirely of leucine-rich repeats (LRR), with a lysine-rich sequence at the amino terminus and cytoplasmically localized. SHOC2 acts as a positive modulator of the RAS-MAPK signaling cascade, which is elicited by EGL-15 and LET-23 and mediated by LET-60. SHOC2 together with protein phosphatase 1c (PP1c) forms a highly specific M-Ras effector complex and is essential for activation of the MAPK pathway by growth factors. Furthermore, in tumor cells with Ras gene mutations, inhibition of SHOC2 expression inhibits MAPK, but not PI3K activity. The SHOC2-PP1c holoenzyme provides an attractive therapeutic target for inhibition of the MAPK pathway in cancer. Recent studies show that aberrantly acquired N-myristoylation of SHOC2 causes human disease Noonan-like syndrome with loose anagen hair.

Supplier: Rockland Immunochemical

Norrie disease is an X-linked genetic disorder characterized by progressive atrophy of the eyes, mental disturbances and deafness. The gene responsible for this disease was initially identified through positional cloning. Norrin, the gene product, encodes a small secreted, cysteine-rich protein that is thought to act as a ligand for the Wnt-receptor/beta-catenin signal pathway despite having sequence homology with the Wnt family of proteins. Mice lacking this gene have abnormal blood vessel growth in the vitreous and a disorganized retina; transgenic ectopic expression of Norrin restores normal retinal vasculature. Recent evidence shows that Norrin can attenuate tPA and uPA-mediated death of transformed rat retinal ganglion cells (RGC-5) by activating the Wnt/beta-catenin pathway and regulating the phosphorylation of LRP-1, a cell surface receptor for tPA and uPA, suggesting the Norrin may function in vivo by regulating kinases which may alter the phosphorylation of LRP-1.

Supplier: Rockland Immunochemical

Antigen stimulation of immune cells triggers Ca++ entry t hrough 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. This antibody is predicted to have no cross-reactivity to ORAI1 or ORAI2. Larger molecular weight bands are sometimes seen in SDS-PAGE; these may represent post-translationally modified ORAI 3.

Supplier: Rockland Immunochemical

IL-16 was initially identified as a chemotactic cytokine, but is now known to possess a wide range of activities. Later studies have more fully characterized IL-16 as an immunomodulatory cytokine that contributes to the regulatory process of CD4+ T cell recruitment and activation at sites of inflammation in association with asthma and several autoimmune diseases. The precursor of IL-16 (pro-IL-16) is thought to be cleaved towards the C-terminal region by Caspase-3, releasing a 20 kDa active form that binds to and signals through CD4. Besides acting as a chemotactic cytokine, IL-16 is thought to also be involved in the regulation of T cell proliferation and multiple infectious, immune-mediated, and autoimmune inflammatory disorders including irritable bowel syndrome, systemic lupus erythematosus, and neurodegenerative disorders. At least two isoforms of IL-16 are known to exist; the longer isoform (also known as NIL-16) is detected only in neurons of the cerebellum and hippocampus.

Supplier: Rockland Immunochemical

TRIM30 belongs to a family of the tripartite motif (TRIM) proteins involved in the regulation of cell proliferation, differentiation, development, oncogenesis, apoptosis and antiviral responses. The TRIM protein family is an expanding family of RING ('really interesting new gene') proteins, also known as RBCC proteins as they contain an RBCC motif, which comprises a RING domain, one or two B-boxes and a predicted coiled-coil region. Studies have shown that some TRIM family members are critical to innate immunity; TRIM5, TRIM19 and TRIM25, for example, have been shown to restrict viral infection. A recent study shows that TRIM30 functions as a negative modulator of the TLR signaling pathway, by targeting TAB2 and TAB3, and contributes to the inhibition of TLR-mediated NF-kB activation. The importance of TRIM30 in the attenuation or termination of NF-kB activation suggests that targeting of TAB2 and TAB3 by TRIM30alpha may be a mechanism for modulating many types of immune responses.

Supplier: Prosci

MECT1 (also known as MucoEpidermoid Carcinoma Translocated 1, Transducer of regulated cAMP response element-binding protein 1, TORC1, and Transducer of CREB protein 1) is a nuclear protein that functions as a transcriptional coactivator for CREB1, which activates transcription through both consensus and variant cAMP response element (CRE) sites. MECT1does not appear to modulate CREB1 DNA-binding activity but enhances the interaction of CREB1 with TAF4/TAFII-130. MECT1 translocates with MAML2 (MasterMind-Like Protein 2) to yield a fusion oncogene: t(11;19) (q21;p13). This translocation occurs in mucoepidermoid carcinomas, benign Warthin tumors and clear cell hidradenomas. The novel fusion product that results disrupts the Notch signaling pathway. The fusion protein consists of the N-terminus of MECT1 joined to the C-terminus of MAML2. The reciprocal fusion protein consisting of the N-terminus of MAML2 joined to the C-terminus of MECT1 has been detected in a small number of mucoepidermoid carcinomas. Multiple isoforms have been reported for the MECT1 protein.

Supplier: Prosci

Recognizes a protein of 42-46kDa, identified as MAGE-1. This mAb does not cross-react with MAGE-2, -3, -4, -6 -9, -10, -or -12 protein. Human malignant neoplasms carry rejection antigens that are recognized by the patients' autologous, tumor directed and specific, cytolytic, CD8+ T lymphocyte clones (CTL). The MAGE family of genes codes an important group of antigens. It was identified that melanomas and primary glial brain tumors express common melanoma associated antigens (MAAs). Because MAGE-1 is expressed on a significant proportion of human neoplasms of various histological types (melanoma, brain tumors of glial origin, neuroblastoma, non-small cell lung cancer, breast, gastric, colorectal, ovarian, renal cell carcinomas) and not on normal tissues, the encoded antigen may serve as a marker of early detection and target for cancer immunotherapy.

Supplier: Rockland Immunochemical

PTPRF or leukocyte common antigen-related protein (LAR) is a widely expressed protein tyrosine phosphatase with an extracellular receptor region that resembles a cell adhesion molecule. PTPRF removes phosphate group from β-catenin, an event that may subsequently facilitate cell-cell adhesion and ensure the stability of the cadherin complex. This phosphatase has also been implicated in various cellular processes such as neurite growth, nerve regeneration, actin remodeling and regulation of insulin function (1,2,3,4). Anti-PTPRF (C-terminal) antibody is specific for the extracellular and cytoplasmic subunits of human PTPRF (approx. 210, 150 and 85 kDa). Detection of the PTPRF bands by immunoblotting is specifically inhibited by the immunizing peptide. Anti-PTPRF is ideal for researchers interested in Cell adhesion Cadherin-mediated cell adhesion pathways, PAK pathways, insulin resistance and ureterocele.

Supplier: Rockland Immunochemical

p53DINP1 antibody detects human p53DINP1. 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 gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress. Anti-p53DINP1 antibodies are ideal for investigators involved in Apoptosis and Cancer research.

Supplier: Rockland Immunochemical

West Nile Virus (WNV) is a member of the Flaviviridae, a plus-stranded virus family that includes St. Louis encephalitis virus, yellow fever virus, and Dengue virus. WNV was initially isolated in 1937 in the West Nile region of Uganda and has become prevalent in Africa, Asia, and Europe. It has rapidly spread across the United States with cases being observed in every continental state. Virus particles consist of a dense core made up of the core/capsid protein encapsulating the RNA genome surrounded by a membrane envelope embedded with envelope and matrix proteins which play a major role for WNV entry into target cells. The viral core protein is thought to contribute to the WNV-associated inflammation via apoptosis induced though the caspase-9 pathway as delivery of core gene delivery into the striatum of mouse brain and skeletal muscle resulted in cell death and inflammation.

Supplier: Rockland Immunochemical

The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6. These proteins are not activated by Cdc42/Rac binding. PAK4 was initially identified as a novel effector of Cdc42Hs. Co-expression of PAK4 and Cdc42Hs resulted in induction of filopodia and actin polymerization, showing that it is involved in cytoskeletal reorganization. Other experiments have shown PAK4 to be essential for embryonic viability and proper neuronal development. PAK4 has also been implicated in anchorage-independent growth of tumor cells and is required for activation of several cancer prosurvival pathways.

Supplier: Cayman Chemical Company

Stimulator of interferon genes (STING) is a component of the innate immune response that binds to cyclic dinucleotides, which are bacterial second messengers, leading to activation of NF-κB and transcription of immunomodulatory genes, including type I interferon (IFN). The H232 variant of STING is found at a 13.7% frequency in the 1000 Genome Project. The SNP variant R232 (Item No. 22816) is the most common variant in the human population, found at a frequency of 57.9%. Various mutations in STING either reduce or increase its activity. Gain-of-function mutations in STING, including R284M (Item No. 23594) and V155M, lead to constitutive activation and enhancement of the type I IFN response. The V155M mutation is associated with a systemic inflammatory condition, including pulmonary fibrosis and autoimmune factors. Mutations that reduce STING activity include K224R (Item No. 23593), which reduces ubiquitination of STING thereby disrupting its localization within the cell, and the double mutation G230A, R293Q (Item No. 23592), which reduces the IFN response. A T596A mutation present in the mouse strain Goldenticket leads to a complete loss of STING protein and lack of a type I IFN response to infection by Listeria.

Supplier: Rockland Immunochemical

The pro-inflammatory cytokine IL-1 induced cellular response requires IL-1 receptor complex including IL-1RI and IL-1RAcP. Recently, MyD88 was identified as an adapter molecule in the IL-1 signaling pathway. MyD88 associates with and recruits IRAK to the IL-1 receptor complex in response to IL-1 treatment and dominant negative form of MyD88 attenuates IL-1R-mediated NF-kB activation. MyD88 is also employed as a regulator molecule by IL-18 receptor and human Toll receptor, which are members in the Toll/IL-1R family of receptors. Targeted disruption of the MyD88 gene results in lose of cellular responses to IL-1 and IL-18, and MyD88-deficient mice lack responses to bacterial product LPS that employs Toll-like receptors 2 and 4 (TLR2 and TLR4) as the signaling receptors. MyD88 is a general adapter protein for the Toll/IL-1R family of receptors and plays an important role in the inflammatory response induced by cytokines IL-1 and IL-18 and endotoxin. MyD88 gene is expressed in many tissues.

Supplier: Rockland Immunochemical

PTPRF or leukocyte common antigen-related protein (LAR) is a widely expressed protein tyrosine phosphatase with an extracellular receptor region that resembles a cell adhesion molecule. PTPRF removes phosphate group from β-catenin, an event that may subsequently facilitate cell-cell adhesion and ensure the stability of the cadherin complex. This phosphatase has also been implicated in various cellular processes such as neurite growth, nerve regeneration, actin remodeling and regulation of insulin function (1,2,3,4). Anti-PTPRF (C-terminal) antibody is specific for the extracellular and cytoplasmic subunits of human PTPRF (approx. 210, 150 and 85 kDa). Detection of the PTPRF bands by immunoblotting is specifically inhibited by the immunizing peptide. Anti-PTPRF is ideal for researchers interested in Cell adhesion Cadherin-mediated cell adhesion pathways, PAK pathways, insulin resistance and ureterocele.

Supplier: Rockland Immunochemical

The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. Rapamycin inhibits TOR activity resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. Raptor (regulatory associated protein of TOR) is a TOR-binding protein essential for TOR signaling in vivo. It acts as a TOR scaffold protein whose binding by TOR substrates is necessary for effective TOR-catalyzed phosphorylation. These substrates include the ribosomal protein S6 kinase (RP S6K) and the eukaryotic initiation factor 4E binding protein 4EBP1, proteins necessary for cell growth and proliferation and responsive to nutrient and mitogen levels. Raptor binds these proteins through a common 5 amino acid TOR-signaling (TOS) motif; mutation of this motif prevents the TOR-dependent phosphorylation of these proteins.