10g

Methylene Chloride-d2, 99.9 Atom Percent D

Metoclopramide Hydrochloride, Monohydrate, USP

Midazolam (CIV), USP

Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine, existing as a homotrimer in vivo. MIF was originally identified as a T cell derived factor responsible for the inhibition of macrophage migration. However, recently MIF has received much more attention because of its possible roles in angiogenesis and cancer development. MIF is over-expressed in various cancers, including pancreatic, breast, colon, brain, prostate, skin, and lung. The intratumoral expression of MIF is strongly correlated with angiogenic growth factor expression, such as the expression of Interleukin 8 (IL-8) and Vascular Endothelial Growth Factor (VEGF), and with risk of recurrence after resection.

CCL18, is a novel CC chemokine that is highly homologous to MIP-1α (61% amino acid sequence identity). CCL18 cDNA encodes an 89 aa residue precursor protein with a 20 aa putative signal peptide that is cleaved to generate a 69 aa residue mature protein which lacks potential glycosylation sites. In vitro, CCL18 mRNA expression is induced in alternatively activated macrophages by Th2 cytokines such as IL-4, IL-10 and IL-13, and inhibited by IFN-γ. CCL18 mRNA is also expressed by GM-CSF/IL-4-induced monocyte-derived dendritic cells. In vivo, CCL18 is highly expressed in lung and placenta but is not expressed in epidermal Langerhans cells. Recombinant CCL18 has been shown to chemoattract naive T cells, but not monocytes or neutrophils.

Myoglobin, a member of the globin family of proteins, is a cytosolic oxygen-binding protein that regulates the storage and diffusion of oxygen within myocytes. The largest expression of myoglobin is in skeletal and cardiac muscle. Myoglobin exhibits various functions in relation to the muscular oxygen supply, such as oxygen storage, facilitated diffusion, and myoglobin-mediated oxidative phosphorylation. Myoglobin is the primary oxygen-carrying pigment of muscle tissues. High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with a particularly high abundance of myoglobin. Myoglobin is found in Type I, Type II A and Type II B muscle; however several studies indicate myoglobinis not found in smooth muscle.

N-(tert-Butyldimethylsilyl)-N-methyltrifluoroacetamide

Molecular Formula : C12 H19 N O

Molecular Formula : C12 H11 N O

Molecular Formula : C12 H11 N O3

Molecular Formula : C9 H9 N O4

Molecular Formula : C8 H15 N O6

Molecular Formula : C5H9NO3

N-Acetyl-DL-phenylalanine

Molecular Formula : C8 H15 N O3

Molecular Formula : C5H9NO3

Molecular Formula : C11 H16 N4 O4

Molecular Formula : C7H11NO5

Molecular Formula : C7H11NO3

Molecular Formula : C13 H14 N2 O3

Molecular Formula : C11 H13 N O4

Molecular Formula : C3H6N2OS

Molecular Formula : C17H30ClN

N-Carbobenzoxy-L-threonine

N-CBZ-L-phenylalanine p-Nitrophenyl Ester

N-Methoxy-N-methylacetamide

N-Methylnicotinamide

N-Vanillylnonanamide, [=Capsaicin (Synthetic)]

N,N-Dimethylformamide-d7, 99.5 Atom Percent D

Neutrophil Activating Peptide 2 (NAP-2) is proteolytically processed carboxyl-terminal fragments of platelet basic protein (PBP) which is found in the alpha-granules of human platelets. NAP-2 is a member of the CXC chemokines. Similar to other ELR domain containing CXC chemokines such as IL-8 and the GRO proteins, NAP-2 has been shown to bind CXCR-2 and to chemoattract and activate neutrophils. Although CTAP-III, β-TG and PBP represent amino-terminal extended variants of NAP-2 and possess the same CXC chemokine domains, these proteins do not exhibit NAP-2 activity. Recently, it has been shown that the additional amino-terminal residues of CTAP-III masks the critical ELR receptor binding domain that is exposed on NAP-2 and may account for lack of NAP-2 activity.

Neutral Red

Neutral Red, Reagent, ACS

NGF Receptor, also known as Gp80-LNGFR, p75 ICD, CD271 and TNFRSF16, is a type I transmembrane protein belonging to the TNF receptor family. It is expressed by both neuronal and non-neuronal cells. Signaling through NGF Receptor has been shown to regulate gene expression, cell migration and death. A truncated NGF Receptor containing only the extracellular domain has been detected in plasma, amniotic fluid and urine, and acts as a potent NGF antagonist.

Nifedipine

Nile Blue A

Nizatidine

Noggin, also known as NOG, is a homodimeric glycoprotein that bindsto and modulates the activity of TGF-beta family ligands. It is expressed in condensing cartilage and immature chondrocytes. Noggin antagonizes bone morphogenetic protein (BMP) activities by blocking epitopes on BMPs needed for binding to their receptors. Noggin has been shown to be involved in many developmental processes, such as neural tube formation and joint formation. During development, Noggin diffuses through extracellular matrices and forms morphogenic gradients, regulating cellular responses dependent on the local concentration of the signaling molecule.

Neurotrophin-4 (NT-4), also known as NT-5, is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-3. Human NT-4 shares 48 – 52% aa sequence identity with human β-NGF, BDNF, and NT-3. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds. NT-4 is expressed highest levels in prostate, lower levels in thymus, placenta, and skeletal muscle. NT-4 binds and induces receptor dimerization and activation of TrkB. NT-4 can signal through TrkB receptors and promotes the survival of peripheral sensory sympathetic neurons.

Nuclear Fast Red

Molecular Formula : C9H10O

Octafluorocyclopentene

Ofloxacin

Orotic Acid Sodium Salt

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, including IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and share a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. On the other hand, OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.