381434 Results for: "single-use assemblies"

Supplier: BioVendor

FGF-23 is a secreted, nonglycosylated monomeric protein belonging to the FGF family. Full-lenght FGF-23 is a phosphaturic hormone which blocks neural phosphate reabsorbtion. Upon processing, biologically inactive N- and C- terminal fragments are generated. Defects in FGF-23 is associated with autosomal dominant hypophosphatemic rickets. The FGF-23 gene encodes a member of the fibroblast growth factor family that is mutant in autosomal dominant hypophosphatemic rickets (ADHR). Tumor-induced osteomalacia is one of the paraneoplastic disorders characterized by hypophosphatemia caused by renal phosphate wasting. The fact that removal of responsible tumors normalizes phosphate metabolism is evidence that a humoral phosphaturic factor, sometimes called phosphatonin, is the basis of tumor-induced osteomalacia. Thus, overproduction of FGF-23 causes tumor-induced osteomalacia, whereas mutations in the FGF-23 gene result in autosomal hypophosphatemic rickets possibly by preventing proteolytic cleavage, which enhances the biologic activity of FGF-23. The mutations in FGF-23 found in ADHR lie within 3 nucleotides of each other in the proprotein convertase cleavage site. Jonsson et al. (2003) showed that FGF-23 is readily detectable in the plasma or serum of healthy persons and can be markedly elevated in those with oncogenic osteomalacia or X-linked hypophosphatemia, suggesting that this growth factor has a role in phosphate homeostasis.

Supplier: Prosci

Recognizes a protein of 55kDa, which is identified as fascin-1. Its actin binding ability is regulated by phosphorylation. Antibody to fascin-1 is a very sensitive marker for Reed-Sternberg cells and variants in nodular sclerosis, mixed cellularity, and lymphocyte depletion Hodgkin's disease. It is uniformly negative in lymphoid cells, plasma cells, and myeloid cells. Fascin-1 is also expressed in dendritic cells. This marker may be helpful to distinguish between Hodgkin lymphoma and non-Hodgkin lymphoma in difficult cases. Also, the lack of expression of fascin-1 in the neoplastic follicles in follicular lymphoma may be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased. Antibody to fascin-1 has been suggested as a prognostic marker in neuroendocrine neoplasms of the lung as well as in ovarian cancer. Fascin-1 expression may be induced by Epstein-Barr virus (EBV) infection of B cells with the possibility that viral induction of fascin in lymphoid or other cell types must also be considered in EBV-positive cases.

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: Prosci

It recognizes an intra-cytoplasmic antigen, which shows a very high degree of specificity for plasma cells. This antigen is present in normal as well as neoplastic plasma cells. Plasma cells, which are large lymphocytes derived from an antigen-specific B cell, secrete antibodies and are responsible for humoral immunity. Plasma cells differentiate from B cells upon stimulation by CD4+ lymphocytes. The B cell acts as an antigen-presenting cell (APC), consuming an offending pathogen, which is taken up by the B cell by phagocytosis and broken down within proteosomes. Plasma cells contain basophilic cytoplasm; their nucleus contains heterochromatin organized in a characteristic cartwheel arrangement. This mAb superbly recognizes normal and neoplastic plasma cells in routine formalin-fixed, paraffin-embedded tissue sections. It is of potential value in identifying myeloma or plasmacytoma in bone marrow or other tissues. It also helps differentiate lympho-plasmacytoid lymphoma from lymphocytic and follicular lymphoma.

Supplier: Labconco

Cell logic Class II, Type B2 Biosafety Cabinets (BSCs) offer comprehensive personnel, product and environmental protection from hazardous particulates, including risk group agents requiring BSL 1-4 containment. Type B2 BSCs, sometimes referred to as 100% exhaust or total exhaust BSCs require a dedicated exhaust system and remote blower for each cabinet. Cell Logics are designed to meet the specific needs of cell research. Models feature a modified sash to accommodate a microscope and/or a temperature-controlled work area on the work surface to maintain cell viability. All models ensure the highest standard of safety and performance.

Supplier: Biosensis

Alpha synuclein is an abundant 140 amino acid neuronal protein, expressed primarily at presynaptic terminals in the central nervous system. Alpha synuclein has been associated with several neurodegenerative diseases. A point mutation in the gene coding for the alpha-synuclein protein was the first discovery linking this protein to a rare familial form of Parkinson's disease (PD). Subsequently, other mutations in the alpha-synuclein gene have been identified in familial PD. The aggregated proteinaceous inclusions called Lewy bodies found in PD and cortical Lewy body dementia (LBD) were discovered to be predominantly alpha-synuclein. Aberrant aggregation of alpha-synuclein has been detected in an increasing number of neurodegenerative diseases, collectively known as synucleopathies. Alpha-synuclein exists physiologically in both soluble and membrane-bound states, in unstructured and alpha-helical conformations, respectively. The physiological function of alpha-synuclein appears to require its translocation between these subcellular compartments and interconversion between the 2 conformations. Abnormal processing of alpha-synuclein is predicted to lead to pathological changes in its binding properties and function.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. MMPs contain the motif His-Glu-X-X-His (X represents any amino acid) that binds zinc in the catalytic site, as well as another zinc molecule and two calcium molecules structurally. They fall within the matrixin subfamily and are EC designated 3.4.24.x. This group also contains astacin, reprolysin, and serralysin, as well as other more divergent metalloproteinases. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown.

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: BioVendor

A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa. Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiogenic factor selectively binding to VEGF receptor –2/KDR.

Supplier: Rockland Immunochemical

Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.

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 R232 variant is the most common variant in the human population, found at a frequency of 57.9% in the 1000 Genome Project.{38697} The SNP variant H232 (Item No. 22815) is found at a 13.7% frequency. 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: SenseAnywhere

The SenseAnywhere 0 - 10 V input module digitizes analogue products with a 0 - 10 V output, ensuring high-precision measurements for variables like CO₂ and dust particles. Integrated electronics with a SAB interface allow individual module calibration. Its hot-swappable feature ensures continuous, accurate monitoring without data loss.

Supplier: SenseAnywhere

The SenseAnywhere 4 - 20 mA input module transforms analogue devices with a 4 - 20 mA output into digital, accurately measuring parameters like CO₂ and dust in cleanrooms. With a SAB interface and integrated electronics, it needs self-calibration only. Its hot-swappable design guarantees continuous, loss-free data collection.

Supplier: Rockland Immunochemical

Immunity-related GTPases (IRG) (also known as p47 GTPases) are a family of GTPase proteins found in vertebrates, which play critical roles in mediating innate resistance to intracellular pathogens. IRG genes have been found in a number of mammals and lower species including mice, rats, zebrafish and humans. Most of the mouse genes contain interferon-stimulated response elements which mediate transcriptional activation by IFNs. In humans, only two IRG genes have been found: human IRGC encodes a full-length IRG protein that, like the mouse homologue, is constitutively expressed in testis, while human IRGM encodes a considerably truncated protein that is constitutively expressed in cultured cells including some macrophage cell lines. As the two human genes IRGC and IRGM are not subject to IFN control, it has been suggested that the host resistance mechanism supported by IRG proteins in the mouse is lacking in humans.

Supplier: Prosci

The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). It has been shown that phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons (Chung et al., 2004).

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: TECNIPLAST USA, INC.

The 1290D Mouse/Rat/Hamster Cage can comfortably house eight mice or four rats of standard size, and is available in polycarbonate or polysulfone materials. Preferred by mice over rats.

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) Biotin 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 biotin conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform western blot, ELISA, Immunohistochemistry, 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: Rockland Immunochemical

Junctional complexes between the plasma membrane (PM) and endoplasmic/sarcoplasmic reticulum (ER/SR) are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. Junctophilins (JPs) are important components of the junctional complexes. JPs are composed of a carboxy-terminal hydrophobic segment spanning the ER/SR membrane and a remaining cytoplasmic domain that shows specific affinity for the PM. Four JPs have been identified as tissue-specific subtypes derived from different genes: JPH1 is expressed in skeletal muscle, JPH2 is detected throughout all muscle cell types, and JPH3 and JPH4 are predominantly expressed in the brain. In the CNS, both JPH3 and JPH4 are expressed throughout neural sites and contribute to the subsurface cistern formation in neurons. Mice lacking both JPH3 and JPH4 subtypes exhibit serious symptoms such as impaired learning and memory and are accompanied by abnormal nervous functions.

Supplier: Rockland Immunochemical

TACE Antibody detects TNF-alpha. Tumor-necrosis factor-alpha is a proinflammatory cytokine and contributes to a variety of inflammatory disease responses and programmed cell death. TNF-alpha; is synthesized as a 26K type II membrane-bound precursor that is cleaved by a convertase to generate secreted 17K mature TNF-alpha;. TNF-alpha; converting enzyme (TACE) protein was recently purified and the human and mouse TACE cDNAs were cloned by several groups separately. TACE is a membrane-bound metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease). TACE also processes other cell surface proteins, including TNF receptor, TGFalpha, the L-selectin adhesion molecule, and alpha-cleavage of amyloid protein precursor (APP). TACE mRNA is expressed in a variety of human and murine tissues. TACE was selected as one of the few targets in cytokine activation by the Eighth International Conference of the Inflammation Research Association. Anti-TACE antibodies are ideal for investigators involved in Apoptosis and Cytokines and Growth factor research.

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.