381450 Results for: "single-use assemblies"

Supplier: Rockland Immunochemical

Interleukin-32 (IL-32) was initially identified as a transcript (NK4) that is selectively expressed in lymphocytes and NK cells and whose expression is increased following activation by IL-2. It was later re-isolated from an IL-18-treated lung carcinoma cell line and re-named IL-32. IL-32 is unusual in that it does not share sequence homology with known cytokine families and is highly expressed in immune tissues, existing in at least four differentially spliced isoforms. Because treatment of human monocytic and mouse macrophage cells with IL-32 induces several proinflammatory cytokines such as TNF-a, IL-8 and MIP-2, and because it is also induced in human peripheral lymphocyte cells after mitogen stimulation and in epithelial cells by IFN-gamma, it has been suggested that IL-32 may play a role in autoimmune and inflammatory diseases such as rheumatoid arthritis.

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: BioVendor

Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species. A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.

Supplier: Rockland Immunochemical

A novel cytokine, designated IL-TIF for IL-10 related T cell-derived inducible factor and IL-22, was recently identified. The receptor for IL-22 (IL-22R, also termed CRF2-9 and IL-TIF-R1 chain) is a new member of the class II cytokine receptor family. IL-22R forms a complex with IL-10 receptor beta chain and mediates IL-22 signaling. IL-22 and its receptor activate JAK-STAT signaling pathway. IL22R is expressed in normal liver and kidney and their cell lines HepG2 and TK-10. A soluble form of IL-22 receptor, also termed IL-22 binding protein (IL-22BP) and IL-22 receptor-alpha 2 (IL-22RA2), was identified very recently. IL-22BP prevents binding of IL-22 to the functional cell surface IL-22R complex and neutralizes IL-22 activity. LPS induces IL-22 expression, which indicates the role of IL-22 in inflammatory response.

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: Prosci

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system, causing a hyperpolarization of the membrane through the opening of a Cl- channel associated with the GABAA-Receptor (GABAA-R) subtype. GABAA-Rs are important therapeutic targets for a range of sedative, anxiolytic, and hypnotic agents and are implicated in several diseases including epilepsy, anxiety, depression, and substance abuse. The GABAA-R is a multimeric subunit complex. To date six alphas, four betas and four gammas, plus alternative splicing variants of some of these subunits, have been identified. Injection in oocytes or mammalian cell lines of cRNA coding for alpha and beta subunits results in the expression of functional GABAA-Rs sensitive to GABA. However, coexpression of a gamma subunit is required for benzodiazepine modulation. The various effects of the benzodiazepines in brain may also be mediated via different alpha subunits of the receptor. Lastly, phosphorylation of beta subunits of the receptor has been shown to modulate GABAA-R function.

Supplier: Prosci

Chek1 is a protein kinase that inhibits mitotic entry after DNA damage, required for the DNA damage checkpoint and is strongly similar to murine Chek1. Checkpoint pathways control the order and timing of cell cycle transitions and ensure that critical events, such as DNA replication and chromosome segregation, are completed with high fidelity. The mouse and human proteins share 90% sequence identity through the protein kinase domains. The sequence of the 476-amino acid human Chek1 protein is 29%, 40%, and 44% identical to those of the fission yeast Chek1, C. elegans Chek1, and Drosophila 'grapes' (Grp) proteins, respectively. Chek1 is expressed ubiquitously as an approximately 2.4-kb mRNA, with the most abundant expression in thymus, testis, small intestine, and colon. The protein has altered mobility when isolated from cells treated with ionizing radiation, indicating that Chek1 is modified in response to DNA damage. In vitro, Chek1 directly phosphorylates a regulator of CDC2 tyrosine phosphorylation, CDC25C. In response to DNA damage, Chek1 phosphorylates and inhibits CDC25C, thus preventing activation of the CDC2-Cyclin-B complex and mitotic entry

Supplier: Biosensis

BDNF belongs to the neurotrophin family and promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. It is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family.

Supplier: Prosci

Interleukin-23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12 (1-5). Although p19 is expressed by activated macrophages, dendritic cells, T cells, and endothelial cells, only activated macrophages and dendritic cells express p40 concurrently to produce IL-23. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 Rbeta1) and the IL-23-specific receptor subunit (IL-23 R). IL-23 has biological activities that are similar to, but distinct from IL-12. Both IL-12 and IL-23 induce proliferation and IFN-gamma production by human T cells. While IL-12 acts on both naie and memory human T cells, the effects of IL-23 is restricted to memory T cells. In mouse, IL-23 but not IL-12, has also been shown to induce memory T cells to secret IL-17, a potent proinflammatory cytokine. IL-12 and IL-23 can induce IL-12 production from mouse splenic DC of both the CD8-and CD8+ subtypes, however only IL-23 can act directly on CD8+ DC to mediate immunogenic presentation of poorly immunogenic tumor/self peptide.

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. Anti-myogenin 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: SenseAnywhere

Discover the SenseAnywhere StarterKit with the AiroSensor 20-20-41 and Magnetic Door Contact Set for efficient open door monitoring in refrigerators and freezers. This kit includes an Indoor AccessPoint for secure data transfer, AssetTagging for easy sensor management, and five credits for optimal system functionality.

Supplier: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is significant for researchers involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic and cardiovascular diseases.

Supplier: Prosci

It recognizes a polypeptide of 6.5kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Rockland Immunochemical

Anti-Monkey IgG (gamma chain) DyLight™680 conjugated antibody generated in goat detects specifically monkey IgG (gamma chain). 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. This DyLight™680 conjugated anti-Monkey IgG gamma chain secondary antibody is ideal for investigators who routinely perform ELISA, Sandwich ELISA, titration assays, western-blot, immunoprecipitation 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

NLRP3(NLR FAMILY, PYRIN DOMAIN-CONTAINING 3),also known as CIAS1, CRYOPYRIN, NALP3 or PYPAF1, is a protein that in humans is encoded by the NLRP3 (NOD-like receptor family, pryin domain containing 3) gene. The NLRP3 gene encodes a pyrin-like protein expressed predominantly in peripheral blood leukocytes. And the NLRP3 gene is mapped on 1q44. NLRP3 interacts with apoptosis-associated speck-like protein containing a CARD (ASC). The encoded protein may play a role in the regulation of inflammation and apoptosis. Mutation of the NALP3 nucleotide-binding domain reduced ATP binding, CASP1 activation, IL1B production, cell death, macromolecular complex formation, self-association, and association with ASC. Consistent with an essential role for Nlrp3 inflammasomes in antifungal immunity, Gross et al.showed that Nlrp3-deficient mice are hypersusceptible to C. albicans infection. Activation of the NLRP3 inflammasome in response to virus or to RNA was dependent upon lysosomal maturation and reactive oxygen species production in human cells. The NLRP3 inflammasome senses obesity-associated danger signals and contributes to obesity-induced inflammation and insulin resistance. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) DyLight™ 800 Conjugated 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 DyLight™800 conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform immunofluorescence, flow cytometry, 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.The emission spectra for this DyLight™ conjugate match the principle output wavelengths of most common fluorescence instrumentation.

Supplier: Genetex

Syntaxin 1, also known as HPC1, is a 35 kDa integral membrane protein which along with SNAP25, and VAMP/synaptobrevin plays a role in vesicular trafficking and membrane fusion. Two Syntaxin 1 isoforms have been identified, Syntaxin 1A which is localized to nerve terminals of sensory neurons and nerve fibers reaching small blood vessels, and Syntaxin 1B which is localized to motor end plates and muscle spindles. The SNARE (soluble N-ethylmaleimide sensitive fusion protein [NSF] attachment protein [SNAPs] receptors)hypothesis of membrane fusion proposes that Syntaxin 1A and SNAP25 (target membrane SNAREs, t-SNAREs) and VAMP/synaptobrevin (vesicular SNAREs, vSNAREs) bind together to form a tripartite structure that along with soluble cytosolic proteins allows for close membrane apposition of donor and target membranes thereby facilitating membrane fusion. The interaction of Syntaxin 1A with vSNAREs is thought to be negatively regulated by the binding of Munc18 to Syntaxin 1A and this interaction is controlled by Cdk5 phosphorylation of Munc18. Syntaxin 1A can be phosphorylated by casein kinase II and phosphorylation of Syntaxin enhances its interaction with Synaptotagmin.

Supplier: BioVendor

Zymogen granule membrane protein 16 (ZG16) is a 16 kDa protein first identified by immunoscreening of a rat pancreatic cDNA expression library with a polyspecific antiserum raised against purified zymogen granule membranes (ZGM). ZG16 displays sequence homology especially in the carbohydrate recognition domain to the plant lectin jacalin, which recognizes terminal galactose attached to N-acetylgalactosamine by a β1–3 linkage. According to its sequence homology with this lectin, ZG16 was considered a secretory lectin ZG16. Sequence analyses uncovered that ZG16 is highly conserved amongst mammals but also appears in many other species. Rat ZG16 was found to be highly expressed in pancreas, colon, and duodenum, where the protein was localized in the zymogen granule of pancreas. The previous reports indicated that rat ZG16 took part in the formation of zymogen granule by mediating the digested enzymes to the zymogen granule membrane in pancreatic acinar cells. Human ZG16 was shown to be highly expressed in adult liver and moderately expressed in intestine (jejunum, ileum) and colon. Moreover, ZG16 is also weakly expressed in pedunculus cerebellaris but not in other brain’s regions. Owing to the specific expression pattern in human liver, ZG16 was evaluated in hepatocellular carcinoma (HCC), a common cancer worldwide (it was found that human ZG16 was significantly down-regulated in HCC). ZG16 protein took part also in several secretions of glycoproteins (the secretion of human ZG16 would be affected when the synthesis of glycans was inhibited with inhibitor or without glucose in cell culture).

Supplier: Biosensis

Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, epinephrine and norepinephrine. Therefore the regulation of the TH enzyme represents the central means for controlling the synthesis of these important catecholamines. FUNCTION: Plays an important role in the physiology of adrenergic neurons. CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. COFACTOR: Fe(2+) ion. ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity. PATHWAY: Catecholamine biosynthesis; first step. SUBUNIT: Homotetramer. PTM: In vitro, phosphorylation of Ser-19 increases the rate of Ser-40 phosphorylation, which results in enzyme opening and activation. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. The presence of different DNA sequences at the TH locus confers susceptibility to various disorders of the brain including manic-depression and schizophrenia. Parkinson's disease is also considered a TH deficiency as low dopamine levels are a consistent neurochemical abnormality.

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) DyLight™ 488 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 DyLight™488 conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform immunofluorescence, flow cytometry, 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. The emission spectra for this DyLight™ conjugate match the principle output wavelengths of most common fluorescence instrumentation.

Supplier: Rockland Immunochemical

Interleukin-33 (IL-33) is a recently identified member of the IL-1 family of cytokines whose other members include IL-1ab, IL-1Ra and IL-18. Its receptor has been shown to be ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling and IL-1R accessory protein (IL-1RAcP). Receptor binding of IL-33 activates NF-kB and MAP kinases and induces the expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine. Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties. Despite its predicted molecular weight, IL-33 will often run at higher molecular weight in SDS-PAGE.

Supplier: Invitrogen

Thermo Scientific Pierce Coomassie Brilliant Blue R-250 is one of the most common forms of coomassie dye, which is a key component of various colorimetric protein gel stains.

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. A repeat expansion in JPH3 is associated with Huntington disease-like 2. At least two isoforms of JPH3 are known to exist.

Supplier: DRG International

An enzyme immunoassay test system to screen for the presence of IgG and IgM class autoantibodies against cardiolipin, phosphatidyl serine, phosphatidyl inositol, phosphatidic acid and beta-2-glycoprotein I in human serum or plasma.

Supplier: Prosci

This Epithelial Membrane Antigen / EMA antibody, also called MUC1 and Mucin-1, recognizes the full-length protein in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this mAb is APDTR in the VNTR region. It reacts with the core peptide of the EMA protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the mAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This EMA antibody reacts with both normal and malignant epithelia of various tissues including breast and colon.

Supplier: Prosci

Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including alpha and beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER alpha and beta are differentially activated by various ligands. Ligand interaction triggers a cascade of events, including dissociation from heat shock proteins, recepter dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER alpha and beta may be regulated by distinct mechanisms even though they share many functional characteristics.

Supplier: Genetex

Structural Maintenance of Chromosomes (SMC) family proteins play critical roles in various nuclear events that require structural changes of chromosomes, including mitotic chromosome organization, DNA recombination and repair and global transcriptional repression. The chromosome proteins are conserved in eukaryotes lead to mitotic chromosome segregation defects, suggesting a critical function of SMC family proteins in mitotic chromosome dynamics. SMC1 and SMC3 form a heterodimeric complex required for metaphase progression in mitotic cells. Specifically this SMC1/SMC3 complex is responsible for sister chromatid cohesion during metaphase. A number of cellular factors interact with hSMC1/hSMC3 during cell cycle. The major population of hSMC1/hSMC3 is in a compex with hRAD21 forming the human cohesion complex. Human cohesion associates with chromosomes which peaks at S phase and dissociates from chromosomes during G2/M transition. In addition, a subpopulation of hSMC1/hSMC3 associates tightly with nuclear matrix and centrosomes during interphase. A subset of hSMC1/hSMC3 is localized to spindle poles, spindles and kinetochores during mitosis when cohesin is in the cytoplasm. hSMC1/hSMC3 is required for spindle aster formation in vitro and reacts with nuclear mitotic apparatus protein in vivo.

Supplier: Genetex

The Aspergillus nidulans 'never in mitosis A' (NIMA) gene encodes a serine/threonine kinase that controls initiation of mitosis. NIMA-related kinases (NEKs) are a group of protein kinases that are homologous to NIMA. Evidence suggests that NEKs perform functions similar to those of NIMA. NEK6 encodes a NEK type protein kinase, which contains a C-terminal NIMA-like catalytic domain. The protein is believed to regulate chromatin condensation in mammalian cells via phosphorylation of histones H1 and H3, and it has been shown to phosphorylate ribosomal S6 protein kinase (S6K1) and serum and glucocorticoid induced protein kinase (SGK1), which regulate diverse cellular processes. The protein also has been shown to bind NEK9, another NIMA-related kinase which regulates chromosome alignment and segregation. At least three mRNA transcripts have been identified, 1.6-, 2.6-, and 9.5-kb. The NEK6 gene is localized to 9q33-34, a region at which the loss of heterozygosity is associated with transitional cell carcinomas. NEK6 expression has been documented in many normal human tissues, including blood, brain, heart, liver, lung, skeletal muscle, spleen and testis. ESTs have been isolated from numerous tissue libraries, especially normal cervix and amnion and cancerous bone marrow.

Supplier: Promega Corporation

Nucleic Acid Purification Kits and Reagents, Membrane Binding Solution, 100ml

Supplier: SenseAnywhere

Explore the SenseAnywhere StarterKit −200 to +200 °C for unparalleled temperature surveillance in extreme environments. Integrating the AiroSensor 20-20-43 and a PT100 Probe, it offers accurate readings for cryogenic applications. Simplified calibration, robust Indoor AccessPoint, and innovative AssetTagging ensure continuous, secure data transmission and seamless sensor management in demanding conditions.