62585 Results for: "Barium+iodide+hydrate&pageNo=50&view=easy"

Supplier: CUSTOM MADE CHEMICALS LAB

COMPONENT 4 MIX 1 * 10 mL

Supplier: VACUUBRAND

In-Line Isolation Valve VV 25 1 * 1 items

Supplier: HAMILTON BONADUZ

calibrate with certificate 1 * 1 items

Supplier: THERMO NATIONAL SCIENTIFIC

SEPCAP INJECTOR CLEAR VIAL NATURAL POLYETHELYNE CAP 1 * 1.000 items

Supplier: Socorex Isba

SPRING MICRO TIP 50µL. 200µL. 1 * 1 items

Supplier: PHENOMENEX

HPLC COLUMN, AERIS 3.6 UM WIDEPORE XB-C18, 150X4,6 MM, 200A 1 * 1 items

Supplier: DWK Life Sciences

Tube screw 125x16mm, GPI 15-415, borosilicate. 1 * 1 items

Supplier: ProSci Inc.

The Galectin family of proteins (with specificity for Nacetyllactosamine containing glycoproteins) consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members that share structural similarities in their carbohydrate recognition domains (CRD) have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins (1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain, and the tandem repeat Galectins (4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

Supplier: ProSci Inc.

Interleukin-20 (IL-20) is a member of the IL-10 family of regulatory cytokines that includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences but they are dissimilar in their biological functions. IL-20 exhibits approximately 28% amino acid identity with IL-10 and 76% amino acid identity with mouse IL-20. There are two heterodimeric receptor complexes for IL-20. The first is composed of IL-20 R alpha and IL-20 R beta . The second is composed of IL-22 R and IL-20 R beta . Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24, the IL-20 R alpha/IL-20 R beta complex is shared with both IL-19 and IL-24. IL-20 has been shown to initiate transduction cascades involving STAT3 and stimulates the induction of pro-inflammatory genes including TNF- alpha and MCP-1. Initial functional studies using transgenic mice suggest that IL-20 has the ability to regulate skin development. The over-expression of both human and mouse forms of IL-20 results in keratinocyte hyper-proliferation, abnormal epidermal differentiation, and neonatal lethality. In humans, IL-20 and its receptors are up-regulated in psoriatic skin, and polymorphisms in the IL-20 gene have been associated with plaque-type psoriasis. IL-20 may also have a role in hematopoiesis. It enhances the proliferation of multi-potential progenitors in vitro and increases their numbers and cell cycling status in IL-20 transgenic mice. IL-20 is also shown to suppress COX-2 and PGE2 and acts as an inhibitor of angiogenesis in model systems.

Supplier: STEMCELL Technologies

Use sclerostin to alter bone remodeling homeostasis, where it inhibits bone formation in vivo and in vitro, likely through Wnt/β-catenin signaling cascades (Ellies et al.; Lin et al.). Sclerostin is a member of the cerberus/DAN family of glycoproteins whose members share a C-terminal cysteine-knot-like (CTCK) domain. Highly expressed in bone and cartilage, as well as in kidney, and liver tissues (Weivoda et al.), this osteoclast-derived BMP antagonist binds BMP6 and BMP7 with high affinity, and binds BMP2 and BMP4 with a lower affinity (Kusu et al.). Mutations in the SOST gene have been associated with sclerosteosis (Brunkow et al.), van Buchem disease (Staehling-Hampton et al.), and bone dysplasia disorders, characterized by increased bone density. This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

Supplier: STEMCELL Technologies

Modulate prostaglandin metabolism with 15-hydroxyprostaglandin dehydrogenase (15-PGDH). 15-PGDH catalyses the reversible oxidation of the 15-hydroxyl group in prostaglandins, resulting in inactivated metabolites (Ensor and Tai), it can act on a variety of prostaglandins as substrates in a NAD+ dependent manner (Cho et al.). As prostaglandins can have a range of effects on cellular processes, 15-PGDH is of considerable importance in drug development. In vitro and in vivo studies suggest 15-PGDH has tumor suppressive activity and is downregulated in certain cancers (Na et al.).15-PGDH belongs to the short-chain dehydrogenases/reductases (SDR) family; its primary structure indicates 20% homology with other SDRs, with some conserved amino acid residues (Krook et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apo M from STEMCELL comes lyophilised with ≥89% purity.

Supplier: MACHEREY-NAGEL

QUANTOFIX CHLORINE 500 TEST STRIPS 1 * 100 Tests

Supplier: Hospidex

Needle Regular point 12° Smaller tip diameter 1 * 5 items

Supplier: OMEGA BIO-TEK

Gel purification of DNA is a common technique used for the isolation of specific DNA fragments. However, most methods either fail to completely remove agarose (which can lead to problems in downstream manipulations), shear the DNA, or result in very low yields.

Supplier: OMEGA BIO-TEK

The E.Z.N.A.® SP plant DNA kit is specially designed for the rapid and reliable isolation of high quality total cellular DNA from a variety of plant species. Up to 100 mg of fresh samples or 30 mg of dry samples can be processed in less than 40 minutes. Purified DNA is suitable for most downstream applications including PCR, restriction digestions and hybridisation techniques.

Supplier: OMEGA BIO-TEK

The E.Z.N.A.® Bacterial RNA kit is designed for isolation of high-quality total RNA from variety of bacterial strains. Up to 1×10⁹ log-phase bacterial cells can be processed. This kit uses an improved lysis procedure to ensure the complete lysis of bacterial cells. Purified RNA is suitable for downstream applications such as RT-PCR and hybridisation techniques.

Supplier: ProSci Inc.

The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

Supplier: STEMCELL Technologies

Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells, however mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

Supplier: EBRO

SURFACE PROBE TPN350 500°C DIA 15MM 1 * 1 items

Supplier: Hospidex

NEEDLE REGULAR POINT 12° NORMAL TYPE 1 * 5 items

Supplier: B. Braun

MEAS.FLASK PACKED UNICO 10-50ML 1 * 10 items

Supplier: DAKLAPACK

BAG 150X200MM 50UM THICKNESS 1 * 1.000 items

Supplier: SIGMUND LINDNER

SiLibeads Typ M Kalknatron-Glaskugel, poliert, 5mm 1 * 1 kg

Supplier: Hospidex

NEEDLE BENT POINT SMALLER TIP DIAMETER 1 * 5 items

Supplier: SARSTEDT

CONTAINER STYROFOAM F/100 MONOVETTE TUBE 1 * 10 items

Supplier: HAMILTON BONADUZ

Syringe,50ul,fixed needle 100 x 0.17mm, point style 3.Hamilton. 1 * 1 items

Supplier: Palintest

IRON MR PHOT 0-5MG/L FE 250 TESTS 1 * 250 Tests

Supplier: Cytiva

For rapid buffer exchange/desalting of PCR products and other DNAs in a volume of 10 to 100 μl using spin column chromatography.

Supplier: Thermo Fisher Scientific

Applications: Complete and ready to use reagent for the isolation of genomic DNA from solid and liquid samples of animal and plant origin

Supplier: STEMCELL Technologies

Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via heterodimers of the IL-21 receptor (IL-21R) and the IL2RG encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.).