59786 Results for: "Ig\u0142y+do+strzykawek&pageNo=50&view=list"

Test kits for quick, semi-quantitative analysis in situ, without the expense of transporting samples to the laboratory. Simple step by step illustrated instructions mean the kits can be used without special chemical training.

Expand 2 Items

L(+)-Lysine monohydrochloride, granular USP

Supplier: Spectrum Chemical

Form: Granular
Use: excipient, biochemistry.

Expand 1 Items

Adapter for 50ml Conical Tubes with Skirted Bottom 1 * 8 items

Supplier: EPPENDORF

Adapter for 50ml Conical Tubes with Skirted Bottom 1 * 8 items

Expand 1 Items

ELECTRON DIGITAL THERMOMETER 1 * 1 items

Supplier: Amarell

ELECTRON DIGITAL THERMOMETER 1 * 1 items

Expand 1 Items

RACK WORK GRAY FOR 15ML AND 50ML TUBES 1 * 1 items

Supplier: GLW

RACK WORK GRAY FOR 15ML AND 50ML TUBES 1 * 1 items

Expand 1 Items

COLD LABORATORY THERMOMETER DIN 1 * 1 items

Supplier: Amarell

COLD LABORATORY THERMOMETER DIN 1 * 1 items

Expand 1 Items

EDTA disodium salt dihydrate, Sigma-Aldrich®

Supplier: Merck

EDTA disodium salt dihydrate, Sigma-Aldrich®

Expand 1 Items

Human recombinant IL25 (from cells)

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.

Expand 1 Items

Human recombinant zinc-alpha-2-Glycoprotein (fromE. coli)

Supplier: ProSci Inc.

Zinc-alpha-2-glycoprotein (ZAG), first identified in the 1960s, derives its name from its precipitation from human plasma upon the addition of zinc salts. ZAG has since been found in secretory epithelial cells and in a range of body fluids. ZAG is identical to a lipid mobilizing factor isolated from the urine of patients with cancer cachexia and stimulates lipolysis in in vitro and in vivo experiments. Due to its expression in, and secretion from adipocytes, ZAG is considered an adipokine. Recently the clinical significance of ZAG has been clarified. ZAG expression in adipocytes is inversely related to fat mass, thus it is intimately involved in the maintenance of body weight in mice and humans. Epidemiological studies have uncovered an association between ZAG and plasma cholesterol. The non-synonymous single nucleotide polymorphism rs4215 in ZAG is associated with plasma cholesterol and obesity. Structurally ZAG possesses a class I major histocompatibility complex (MHC) protein fold. It is distinct from other members of this protein family in that it is soluble, rather than being anchored to plasma membranes, and it associates with prolactin inducible protein rather than beta2-microglobulin. Similar to peptide antigen-presenting class I MHC molecules, ZAG possesses an open apical groove between its alpha1 and alpha2 domain helices.