42439 Results for: "2,5-dimethylbenzothiazole"

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Rockland Immunochemical

CD44 was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). CD44 is a receptor for hyaluronic acid (HA), an integral component of the extracellular matrix. CD44 mediates cell-cell and cell-matrix interactions through its affinity for HA, and can also interact with ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). The multiple protein isoforms are encoded by a single gene by alternative splicing and are further modified by a range of post-translational modifications. CD44 function is controlled by these posttranslational modifications. The major physiological role of CD44 is to maintain organ and tissue structure via cell-cell and cell-matrix adhesion, but certain variant isoforms can also mediate lymphocyte activation and homing, and the presentation of chemical factors and hormones. CD44 participates in a wide variety of cellular functions including lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. CD44 is a multi-structural and multi-functional cell surface molecule involved in cell proliferation, cell differentiation, cell migration, angiogenesis, presentation of cytokines, chemokines, and growth factors to the corresponding receptors, and docking of proteases at the cell membrane, as well as in signaling for cell survival. All these biological properties are essential to the physiological activities of normal cells, but they are also associated with the pathologic activities of cancer cells. CD44, particularly its variants, may be useful as a diagnostic or prognostic marker of malignancy and, in at least some human cancers, it may be a potential target for cancer therapy.

Supplier: Biotium

EvaGreen® Dye and high-performance dye-based qPCR master mixes containing EvaGreen® qPCR dye, Cheetah™ HotStart Taq Polymerase, and Forget-Me-Not™ tracking dye. Available with 2-color tracking or pre-mixed with low or high ROX.

Supplier: Rockland Immunochemical

RB1 (RB Transcriptional Corepressor 1) is a protein coding gene. The protein encoded by this gene is a negative regulator of the cell cycle and was the first tumor suppressor gene found. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The active, hypo-phosphorylated form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. RB1 is directly involved in heterochromatin formation by maintaining overall chromatin structure and the constitutive heterochromatin, by stabilizing histone methylation. Retinoblastoma recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 Lys-20 trimethylation and inhibits the intrinsic kinase activity of TAF1. It mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein, or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1s activity. RB1 may be associated with diseases such as retinoblastoma, small cell cancer of the lung, bladder cancer, and osteogenic sarcoma. Anti-Retinoblastoma K860 Me1 Antibody is useful for researchers interested in cancer, transcription factor, epigenetics, and enzyme antibody research.

Supplier: Prosci

Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of some cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of some cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.

Supplier: Prosci

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX19B is a DEAD box protein, which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding activities. This protein is recruited to the cytoplasmic fibrils of the nuclear pore complex, where it participates in the export of mRNA from the nucleus.DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding activities. This protein is recruited to the cytoplasmic fibrils of the nuclear pore complex, where it participates in the export of mRNA from the nucleus. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Supplier: Zymo Research

The Quick-RNA™ viral kit is a quick, purification system for viral RNA from plasma, serum, cell culture media, cellular suspensions, urine, blood, saliva and any other biological samples stored in DNA/RNA Shield™.

Supplier: MP Biomedicals

MPurify Your Nucleic Acid: Obtain Superior Yield, Exceptional Purity, and Automated Performance in a Flexible, Convenient and Affordable Manner!

Supplier: Genetex

BRCA1 (breast and ovarian cancer susceptibility protein 1) is a RING finger protein containing a BRCT domain. BRCA1 exists as a heterodimer with 22 possible isoforms. The full length protein has a reported molecular weight of 208 kD. BRCA1 localizes to the mitotic spindle microtubules, centriole walls, pericentriolar fibers at centrosomes. Unphosphorylated BRCA1 localizes on chromosomes from metaphase through telophase; phosphorylated BRCA1 resides in inner chromosomal structure, centrosome, cleavage furrow during prophase through telophase, and relocalizes to the perinuclear region when cells are subjected to IR or UV radiation in S phase. BRCA1 acts as a tumor suppressor and can function as a secreted growth inhibitory protein, participate in transcription coupled repair of oxidative DNA damage, X-chromosome inactivation, and can function as a E3 ubiquitin ligase. BRCA1 can be transcriptionally downregulated by Ets-2, Brg-1, and Hmga-1. BRCA1 can be modified by glycosylation, ubiquitination and phosphorylation by CDK4, ATM/ATR, cdk2, and hChk2. The BRCA1 protein has been reported to interact with RNA polymerase II holoenzyme and BARD1. BRCA1 contains at least two nuclear localization signals and is proposed to be a tumor suppressor protein. It is a serine phosphoprotein that undergoes hyperphosphorylation during late G1 and S phases of the cell cycle and is transiently dephosphorylated early after M phase. BRCA1 protein alters in a qualitative and quantitative manner during cell cycle progression. The amount of BRCA1 protein is highest during S phase and remains elevated toward G2 / M, before it declines in early G1 phase. Inherited loss of BRCA1 function confers an increased susceptibility for both breast and ovarian cancer.

Supplier: Avantor

You be the detective!

Supplier: G-Biosciences

G-Biosciences' GET™ Plasmid Miniprep kit isolates high quality plasmid DNA from 1-5 mL E

Supplier: Enzo Life Sciences

Quick, easy kit for purifying DNA from PCR, gels and labeling reactions for a variety of downstream applications.

Supplier: MilliporeSigma

Sodium L-glutamate monohydrate suitable for use as excipient EMPROVE® exp FCC,NF,E 621.

Supplier: Zymo Research

Columns and filters for the purification of DNA and/or RNA from high-volume sample inputs.

Supplier: Prosci

SMAD1 belongs to the SMAD family. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. SMAD1 mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, SMAD1 can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of SMAD1 forms a complex with SMAD4, which is important for its function in the transcription regulation. SMAD1 is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation.The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed.

Supplier: Prosci

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. The ribosomal protein is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Thermo Scientific Chemicals

Sodium deoxycholate monohydrate 98%

Supplier: GILSON, INC.

This compact, ergonomic system is an easy to use and accurate solution for high throughput pipetting of 96- and 384-well plates. The PLATEMASTER's 96-channel design greatly reduces the number of pipetting steps necessary to fill a microplate when compared to using regular manual multichannel pipettes. When using this, the time it takes to fill 96-well plates is significantly reduced to approximately 10 to 20 seconds or less, and 384-wells can typically be filled in less than a minute using only four pipetting steps.

Supplier: Zymo Research

The YeaStar™ RNA Kit provides all the necessary reagents for RNA isolation from a broad spectrum of fungi including: Aspergillus fumigatus, Aspergillus nidulans, Aspergillus nivens var. aureus, Candida albicans, Pichia pastoris, Saccharomyces cerevisiae, Schizosaccharomyces pombe.

Supplier: Prosci

Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene. Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene.

Supplier: MP Biomedicals

MPure Viral Nucleic RNA Extraction Kit is used with the MPure-12 instrument for extraction of Viral RNA from human biological specimens such as serum, plasma, and other cell-free fluids.

Supplier: MP Biomedicals

MPure Tissue DNA Extraction Kit is used with the MPure-12 nucleic acid purification system for the extraction and purification of genomic DNA from a variety of animal tissues, swab samples and blood stain.

Supplier: Rockland Immunochemical

Leptin is a key player in the regulation of energy balance and body weight control. Once released into the circulation, it has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways. It acts as an appetite-regulating factor, regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones, it increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, it induces FOS and SOCS3 expression to release anorexigenic peptides. It has a modulatory role in nutrient absorption. It reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption. It acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways. It may also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. It plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 which promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38. In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses. Increases CD4+CD25- T cells proliferation and reduces autophagy during TCR (T cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation.

Supplier: MP Biomedicals

MPure Bacterial DNA Extraction Kit is used with the MPure-12 Nucleic Acid Purification System for extraction and purification of genomic DNA from both Gram-positive and Gram-negative bacteria.

Supplier: Thermo Scientific Chemicals

MDL: MFCD00150989 Beilstein Registry No.: 6113568 Notes: Loses water of crystallization at 140°C unstable above 225°C

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Rochelle salt; Seignette salt tetrahydrate; sodium potassium tartrate tetrahydrate. CAS RN 6381-59-5. Formula Weight: 282.23. Crystals, 'BAKER ANALYZED'* Reagent, 99.0-102.0%. Meets ACS specifications. Packaged in a plastic container. 2.5kg.

Supplier: Thermo Scientific Chemicals

MDL: MFCD00065606 Beilstein Registry No.: 5158059 Optical Rotation: +5.5°C (c=5 in 5N HCl)

Supplier: MilliporeSigma

Meets ACS Specifications, Meets Reagent Specifications for testing USP/NF monographs

Supplier: IBI Scientific

The DNA/RNA/Protein Extraction Kit provides an efficient method for purifying genomic DNA, total RNA, and total protein simultaneously from cultured cells, animal tissues, whole blood, and biological fluids

Supplier: Prosci

RFX5 is the fifth member of the growing family of DNA-binding proteins sharing a novel and highly characteristic DNA-binding domain called the RFX motif. RFX is a nuclear protein complex that binds to the X box of MHC-II promoters. The lack of RFX binding activity in complementation group C results from mutations in the RFX5 gene encoding the 75-kD subunit of RFX.A lack of MHC-II expression results in a severe immunodeficiency syndrome called MHC-II deficiency, or the bare lymphocyte syndrome (BLS; MIM 209920). At least 4 complementation groups have been identified in B-cell lines established from patients with BLS. The molecular defects in complementation groups B, C, and D all lead to a deficiency in RFX.A lack of MHC-II expression results in a severe immunodeficiency syndrome called MHC-II deficiency, or the bare lymphocyte syndrome (BLS; MIM 209920). At least 4 complementation groups have been identified in B-cell lines established from patients with BLS. The molecular defects in complementation groups B, C, and D all lead to a deficiency in RFX, a nuclear protein complex that binds to the X box of MHC-II promoters. The lack of RFX binding activity in complementation group C results from mutations in the RFX5 gene encoding the 75-kD subunit of RFX (Steimle et al., 1995). RFX5 is the fifth member of the growing family of DNA-binding proteins sharing a novel and highly characteristic DNA-binding domain called the RFX motif. Multiple alternatively spliced transcript variants have been found but the full-length natures of only two have been determined.