10g

Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine that was previously called monocyte-specific chemokine 3 (MCP-3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature form, it is classified within the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, within a large cluster containing many other CC chemokines and is most closely related to CCL2. CCL7 can signal through the CCR1, CCR2 and CCR3 receptors.

Mecobalamin, JP

Methyl 4-(Bromomethyl)benzoate

Methyl Alcohol-d4, 99.8 Atom Percent D

Methyl N,N-Dimethylanthranilate

Methyl-beta-cyclodextrin

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

N-Acetyl-DL-phenylalanine

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

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.

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, 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.

p-Naphtholbenzein

Palladium on Charcoal, 5 Percent, Catalyst, Powder

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L1 binds to its receptor, PD-1, found on activated T cells, B cells, and myeloid cells, to modulate activation or inhibition.

Platelet-Derived Growth Factor-AA (PDGF-AA) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In chemical terms, platelet-derived growth factor is a dimeric glycoprotein composed of two A (-AA) or two B (-BB) chains or a combination of the two (-AB). The dimeric isoforms PDGF­AA, AB and BB are differentially expressed in various cell types, and their effects are mediated through two distinct receptors termed α and β. Differences exist in isoform binding to each receptor. Ingeneral, PDGF isoforms are potent mitogens for connective tissue cells including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial andendothelial cells. In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells. PDGF-AA plays a significant role in blood vessel formation (angiogenesis).

Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in an animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, and PDGF-AB. It is involved in many biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).

Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, PDGF-AB. It is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor (PDGF) is a potent mitogen for a wide range of cell types including fibroblasts, smooth muscle, connective tissue, bone and cartilage cells, and some blood cells. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. The PDGF family consists of proteins derived from four genes (PDGF -A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB).

PDGF-DD, also known as platelet-derived growth factor D, IEGF and SCDGFB, is asecreted growth factor belonging to the PDGF/VEGFfamily. It is highly expressed in the heart, pancreas, adrenal glands and ovary. PDGF-DD forms functional homodimers that bind and induce PDGF Rβ homodimers and PDGF Rα/β heterodimers that promote intracellular signaling. This plays an important role in the regulation of cell differentiation, migration and survival. It has also been reported that PDGF-DD can induce monocyte and macrophage recruitment, increase interstitial pressure and facilitate wound healing.