45994 výsledků pro: "Fire Assay Crucible"

Supplier: ANTIBODIES.COM

[EN]MOUSE IL22 RA2/IL-22BP ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

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

Supplier: ANTIBODIES.COM

[EN]MOUSE IL-12/IL-23 P40 ELISA KIT 1 * 96 Tests

Supplier: ANTIBODIES.COM

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

Supplier: Biorbyt

ULTRA SENSITIVE MOUSE INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

HIGH SENSITIVE MOUSE INSULIN ELISA KIT 1 * 96 KS

Supplier: MILLIPORE

Plasmid Miniprep 96 kit is a quick and easy-to-use kit that produces clean and reproducible DNA in half a time than traditional methods.

Supplier: Biorbyt

WIDE RANGE MOUSE INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

ULTRA SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: Biorbyt

HIGH SENSITIVE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: ANTIBODIES.COM

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

Supplier: ANTIBODIES.COM

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

Supplier: ANTIBODIES.COM

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

Supplier: ANTIBODIES.COM

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

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.

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.

Supplier: Biorbyt

WIDE RANGE RAT INSULIN ELISA KIT 1 * 96 KS

Supplier: Cytiva

illustra™ MicroSpin™ S-400 HR columns designed for rapid purification of PCR products (>200 bp) from unincorporated primers (<32-mers) and nucleotides using spin-column chromatography.

Supplier: ProSci Inc.

tumour Necrosis Factor- alpha (TNF- alpha) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF- alpha while cells that express CD8 secrete little or no TNF- alpha. Synthesis of TNF- alpha can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumour activity of TNF- alpha has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF- alpha mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF- alpha that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumour activity and reduced systemic toxicity in mice compared with murine TNF- alpha, which binds to both murine TNF receptors. Based on these results, many TNF- alpha mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumour cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF- alpha High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo.

Supplier: ProSci Inc.

Interleukin 25 (IL-25) belongs to the Interleukin 17 (IL-17) family of proteins, which is comprised of six members (IL-17, IL-17B through IL-17F). These proteins are secreted and are structurally related by sharing a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non-covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Human interleukin-17E (IL17E), also referred to as Interleukin-25 (IL25), is a distinct member of the IL17 cytokine family comprised of at least six members sharing a conserved cysteine-knot structure but divergent at the N-terminus. IL25 is a glycoprotein secreted as dimers by innate effector eosinophils and basophils, and present at very low levels in various peripheral tissues. IL25, together with IL17B, are ligands for the cytokine receptor IL17BR, and the cross-linking induces NF-κB activation and production of the proinflammatory chemokine IL-8, as well as ERK, JNK, and p38 activation. Overexpression of IL25 gene in transgenic mice suggested that this cytokine can regulate hematopoietic and immune functions, and additionally is identified as a proinflammatory cytokine favoring Th2-type immune responses possibly by enhancing the maintenance and functions of adaptive Th2 memory cells.

Supplier: ProSci Inc.

Reacts with a protein of 57 kDa, identified as the L1 protein of human papilloma virus type 16 (HPV-16). Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on the basement membrane to provide initial virion attachment to target cells. Basement membrane is exposed only after epithelium trauma. Additionally, the alpha6 integrin complexed with either beta1 or beta4 integrin has been proposed to act as a coreceptor recognized by L1. Once attached, integrin complexed with beta4 integrin has been proposed to act as a coreceptor recognized by L1. Once attached, the virion enters the host cell via clathrin-mediated endocytosis and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2. [UniProt]

The antibody reacts very strongly with formalin-fixed, paraffin-embedded tissues containing HPV-16 or -33; very weak reactions were occasionally observed with biopsy specimens or smears containing HPV-6 or HPV-11. It cross-reacts with HPV37.

Supplier: MEGAZYME

[EN]MALTOPENTAOSE 1 * 50 mg

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.

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.

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.

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.

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: 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: 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.

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.