5g

Hydromorphone Hydrochloride (CII), USP

Hydroxocobalamin

Hydroxocobalamin Acetate

Hydroxocobalamin, USP

Hydroxy Naphthol Blue, Solid Dilution (This regent is deposited on crystals of sodium chloride), Reagent, ACS

Hydroxychloroquine Sulfate

Hydroxymethylferrocene

Hydroxyurea

Hypoxanthine

Idebenone

Interferon-beta (IFN-β), acting via STAT1 and STAT2, is known to upregulate and downregulate a wide variety of genes, most of which are involved in the antiviral immune response. It is a member of Type I IFNs, which include IFN-α, -β, τ, and –ω. IFN-β plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses.

Interleukin-11 is a pleiotropic cytokine that was originally detected in the conditioned medium of an IL-1α-stimulated primate bone marrow stromal cell line (PU-34) as a mitogen for the IL-6-responsive mouse plasmacytoma cell line T11. IL-11 has multiple effects on both hematopoietic and non-hematopoietic cells. Many of the biological effects described for IL-11 overlap with those for IL-6. In vitro, IL-11 can synergize with IL-3, IL-4 and SCF to shorten the G0 period of early hematopoietic progenitors. IL-11 also enhances the IL-3-dependent megakaryocyte colony formation. IL-11 has been found to stimulate the T cell-dependent development of specific immunoglobulin-secreting B cells.

Interleukin 12 (IL-12), also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF. These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and mouse IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the mouse system.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-8 (IL-8), also known as CXCL8, GCP-1 and NAP-1, is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells. It is secreted by monocytes, macrophages and endothelial cells. IL-8 signals through CXCR1 and CXCR2 to chemoattract neutrophils, basophils, and T cells. IL-8 is also a potent promoter of angiogenesis. Other functions of this protein, such as involvement in bronchiolitis pathogenesis, have also been reported.

Imidazole-4-carboxaldehyde

Iminostilbene

Imipramine Hydrochloride

Imipramine Hydrochloride, USP

Indium(III) Chloride, Anhydrous [for General Organic Chemistry]

Indole-3-acetamide

Indole-3-butyric Acid

Indole-3-carboxaldehyde

Indophenol Blue

Indoprofen

Inosine 5′-Monophosphate Disodium Salt, Hydrate

Inositol Hexaphosphate Calcium Salt

Inulin

Iodomesitylene Diacetate

Iodosobenzene

Iohexol

TAFA-2 also named FAM19A2 belongs to the TAFA family of chemokine­like proteins. Like other members of the FAM19/TAFA family, with the exception of TAFA5, mature TAFA1 to 4 contain 10 regularly spaced cysteine residues. Human TAFA2 is 97% aa identical to mouse TAFA2. TAFA2 expression can be detected in the central nervous system (CNS), colon, heart, lung, spleen, kidney, and thymus, but its expression in the CNS is 50­ to 1000­fold higher than in other tissues. Within the CNS, TAFA2 expression is highest in the occipital and frontal cortex (3­ to 10­fold more abundantly expressed than in other cortical regions) and medulla. The biological functions of TAFA family members remain to be determined, but there are a few tentative hypotheses.

Ipratropium Bromide, USP

Iridium, 325 Mesh, Powder

Iridium(III) Chloride, Hydrate

Iron(II) Acetate

Isobutyl 4-Hydroxybenzoate, [for Biochemical Research]

Isocytosine

Isoindoline

Isopropyl 1-Thio-beta-D-galactopyranoside

Isopropyl 4-Hydroxybenzoate, [for Biochemical Research]

Isopropyl Methanesulfonate

Isopropyl-beta-D-thiogalactoside, High Purity

Isopropyl-beta-D-thiogalactoside, High Purity

Isopropyltriphenylphosphonium Iodide