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47520 výsledků pro "Fire Assay Crucible"

47520 výsledků pro: "Fire Assay Crucible"

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[EN]HUMAN IL-36 BETA/IL-1F8 ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]HUMAN IL-36 BETA/IL-1F8 ELISA KIT 1 * 96 Tests

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[EN]RAT IL-22 RA2/IL-22BP ELISA KIT 1 * 48 Tests

Supplier: ANTIBODIES.COM

[EN]RAT IL-22 RA2/IL-22BP ELISA KIT 1 * 48 Tests

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[EN]HUMAN IL-22 RA2/IL-22BP ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]HUMAN IL-22 RA2/IL-22BP ELISA KIT 1 * 96 Tests

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[EN]HUMAN IL-18R BETA/IL-18RAP ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]HUMAN IL-18R BETA/IL-18RAP ELISA KIT 1 * 96 Tests

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[EN]MOUSE ANTI-SARS-COV-2 S RBD IGM ELIS 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]MOUSE ANTI-SARS-COV-2 S RBD IGM ELIS 1 * 96 Tests

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[EN]ANTI-SARS-COV-2 S RBD IGG ELISA 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]ANTI-SARS-COV-2 S RBD IGG ELISA 1 * 96 Tests

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[EN]ANTI-SARS-COV-2 S RBD IGA ELISA 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]ANTI-SARS-COV-2 S RBD IGA ELISA 1 * 96 Tests

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Microplate readers, Varioskan™ LUX

Microplate readers, Varioskan™ LUX

Supplier: THERMO LABSYSTEMS LIFE SCIENCE

Varioskan™ LUX comes equipped with a range of measurement technologies including absorbance, fluorescence intensity and FRET as standard, and with optional luminescence, AlphaScreen and time-resolved fluorescence (TRF) modules. The instrument selects the measurement wavelength using filters or monochromators, depending on which is optimal for each measurement technology.

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WIDE RANGE MOUSE INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

WIDE RANGE MOUSE INSULIN ELISA KIT 1 * 96 KS

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[EN]HUMAN VON HIPPEL LINDAU/VHL ELISA KI 1 * 48 Tests

Supplier: ANTIBODIES.COM

[EN]HUMAN VON HIPPEL LINDAU/VHL ELISA KI 1 * 48 Tests

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[EN]HUMAN IL-36 GAMMA/IL-1F9 ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]HUMAN IL-36 GAMMA/IL-1F9 ELISA KIT 1 * 96 Tests

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[EN]MOUSE IL-12/IL-23 P40 ELISA KIT 1 * 960 Tests

Supplier: ANTIBODIES.COM

[EN]MOUSE IL-12/IL-23 P40 ELISA KIT 1 * 960 Tests

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[EN]MOUSE ANTI-SARS-COV-2 S RBD IGG ELIS 1 * 96 Tests

Supplier: ANTIBODIES.COM

[EN]MOUSE ANTI-SARS-COV-2 S RBD IGG ELIS 1 * 96 Tests

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WIDE RANGE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

WIDE RANGE RAT INSULIN ELISA KIT 1 * 96 KS

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ULTRA SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

ULTRA SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

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HIGH SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

HIGH SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

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Mouse recombinant CXCL12 (from E. coli)

Supplier: ProSci Inc.

Mouse Cxcl12 is a secreted and highly conserved protein which belongs to the intercrine alpha (chemokine CxC) family.CXCL12 is widely expressed in various organs including brain, kidney, skeletal muscle, heart, liver, and lymphoid organs. Cxcl12 activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. It also binds to atypical chemokine receptor ACKR3 which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Cxcl12 has several critical functions during embryonic development such as B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Cxcl12 plays an important role in acting as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. It stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. It also plays a protective role after myocardial infarction, induces down-regulation and internalization of ACKR3 expressed in various cells and stimulates the proliferation of bone marrow-derived b progenitor cells in the presence of IL-7 as well as growth of the stromal cell-dependent B-cell clone DW34 cells.

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[EN]MALTOPENTAOSE 1 * 50 mg

Supplier: MEGAZYME

[EN]MALTOPENTAOSE 1 * 50 mg

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Mouse recombinant IL36 alpha (from E. coli)

Supplier: ProSci Inc.

Mouse Interleukin-36 alpha(Il-36a)is a member of the IL-1 family.IL¬1 alpha,IL¬1 beta and IL-18 are potent inflammatory cytokines whose activities are dependent on heterodimeric receptors of the IL-1R superfamily, and which are regulated by soluble antagonists. Il36a is expressed in many cells, including monocytes, B cells, and T cells, immune system and fetal brains. Il36a is a cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. It is a part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. It seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. It Induces the production of proinflammatory cytokines, including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23 in bone marrow-derived dendritic cells (BMDCs). Moreover, it is involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II and can induce the production of IFN-gamma, IL-4 and IL-17 by cultured CD4+ T cells and splenocytes. Il36a may play a role in proinflammatory effects in the lung: induces the expression of CXCL1 and CXCL2 in the lung, and the expression of TNF-alpha, IL-36c, IL-1A, IL-1B, CXCL1 and CXCL2 in isolated splenic CD11c+ alveolar macrophages. It may be involved in T cell maturation by stimulating the surface expression of CD40 and modestly CD80 and CD86 in splenic CD11c+ cells and CD4+ T cell proliferation.

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illustra™ MicroSpin™ S-300 HR columns

illustra™ MicroSpin™ S-300 HR columns

Supplier: Cytiva

illustra™ MicroSpin™ S-300 HR columns designed for rapid purification of PCR products (>100 bp) from unincorporated primers (<20-mers) and nucleotides using spin-column chromatography.

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Human recombinant IL-15 R alpha & IL-15 fusion (from Cells)

Supplier: ProSci Inc.

Interleukin-15 receptor subunit alpha, also known as Il15ra, is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits (Common gamma chain, or gamma c) to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells. Human Il15ra shares 45% amino acid sequence homology with the mouse form of the receptor. Eight isoforms of IL-15 R alpha mRNA have been identified, resulting from alternative splicing events involving different exons.Interleukin 15 (IL-15) is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL15 receptor (IL-15RA) with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each other's activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs.

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RNA-Solv® reagent

RNA-Solv® reagent

Supplier: OMEGA BIO-TEK

RNA-Solv® Reagent is a one reagent system for the isolation of total RNA from cells and tissues. The reagent, a single-phase solution consisting of phenol and guanidine isothiocyanate, is a modification of the single-step RNA isolation method developed by Chomczynski and Sacchi. The sample is homogenised and lysed in RNA-Solv® Reagent, which maintains the integrity of the RNA while disrupting and denaturing endogenous RNases and other cellular components. Extraction of the lysate with chloroform further denatures proteins and separates the mixture into an organic and an aqueous phase. RNA remains exclusively in the aqueous phase, and is subsequently recovered by isopropanol.

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Human recombinant IL20 (fromE. coli)

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.

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Human recombinant Galectin 8 (from E. coli)

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.

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Human recombinant Fc gamma RIIa (from cells)

Supplier: ProSci Inc.

Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Human Fc gamma Rs are divided into three classes designated Fc gamma RI (CD64), Fc gamma RII (CD32), and Fc gamma RIII (CD16), which generate multiple isoforms, are recognized. The activating­ type receptor either has or associates non­covalently with an accessory subunit that has an immunoreceptor tyrosine­based activation motif (ITAM) in its cytoplasmic domain. Fc gamma RI binds IgG with high affinity and functions during early immune responses, whereas Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. Three genes for human Fc gamma RII (A, B, and C) and one for mouse (Fc gamma RIIB), encoding type I transmembrane proteins with ITAM motifs (Fc gamma RII A and C) or ITIM motifs (Fc gamma RIIB) in their cytoplasmic domains, have been identified. Human CD32, also known as Low affinity immunoglobulin gamma Fc region receptor II-a (IgG Fc receptor II-a), Fc gamma RII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcR gamma , CD32a (Fc gamma RII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fc gamma RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors.

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Human recombinant Galectin 3 (from E. coli)

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.

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illustra™ ProbeQuant™ G-50 micro columns

illustra™ ProbeQuant™ G-50 micro columns

Supplier: Cytiva

ProbeQuant™ G-50 micro columns use spin column chromatography to provide a fast and reliable method for purifying labelled probes from unincorporated labelled nucleotides. In addition, a portion of the eluted DNA can be counted in a scintillation counter and compared to an unpurified sample to give an approximation of percent incorporation. The columns are designed for use in a microcentrifuge, come prepacked with Sephadex™ G-50 DNA grade and are pre-equilibrated in STE, which means that they are ready to use. They can accommodate samples ranging in volume from 25 μl to 50 μl.

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Genomic DNA extraction from dried blood spots, Extracta™ DBS

Genomic DNA extraction from dried blood spots, Extracta™ DBS

Supplier: Quantabio

Extracta™ DBS is a ready to use DNA extraction reagent for rapid and efficient recovery of PCR-ready DNA from dried blood spots (DBS) on Guthrie cards or Whatman® 903 filter/TFN or 226 from Ahlstrom Munksjö paper. This patented single-solution process produces DNA eluates that are substantially free of PCR inhibitors and compatible with a variety of end-point PCR, real-time PCR and Next Generation Sequencing (NGS) or Sanger Sequencing reagents. Application of Extracta DBS with PerfeCTa® qPCR ToughMix® or PerfeCTa MultiPlex qPCR ToughMix® enables accurate and reproducible quantification of DNA sequences in blood using TaqMan® hydrolysis probe real-time qPCR.

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RNAspin Mini Kits

RNAspin Mini Kits

Supplier: Cytiva

RNAspin Mini RNA Isolation Kit is a complete RNA purification kit designed for rapid extraction of high-quality total RNA from a wide range of sample types.

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Microscope documentation cameras

Supplier: LEICA MICROSYSTEMS

Leica (brightfield) colour cameras provide outstanding colour fidelity due to state-of-the-art colour interpolation algorithms performed in the camera head. Leica fluorescence cameras provide high sensor sensitivity allowing short exposure times and, therefore, preventing photo bleaching, so actively protecting cells from any photo damage.

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