Duoset Murine Lcn-2 Elisa Kit (R&D Systems

Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.

Description: CD40, a member of the TNF receptor family, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40-Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to "immunodeficiency with hyper-IgM", a disease characterized by failure to produce IgG, IgA and IgE. The soluble form of CD40L is an 18kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L. Recombinant murine CD40L is a soluble 16.4 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.

Description: IL-15 is an immunomodulating cytokine that stimulates the proliferation of T lymphocytes and shares many biological properties with IL-2. IL-15 exerts its biological activites primarily on T cells. It is also essential in the development, survival and activation of NK cells. Increased expression of IL-15 has been implicated with rheumatoid arthritis, inflammatory bowl disease and diseases affiliated with retroviruses HIV and HTLV-I. Human IL-15 is biologically active on mouse cells as measured by the dose-dependent stimulation of the proliferation of mouse CTLL cells. Recombinant murine IL-15 is a 13.3 kDa protein consisting of 115 amino acid residues.

Description: Flt3-Ligand is a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand binds to cells expressing the tyrosine kinase receptor Flt3. Flt3-Ligand, by itself does not stimulate proliferation of early hematopoietic cells, but synergizes with other CSFs and interleukins to induce growth and differentiation. Unlike SCF, Flt3-Ligand has no activity on mast cells. Multiple isoforms of Flt3-Ligand have been identified. The predominant biologically active form is anchored to the cell surface as the extracellular domain of a transmembrane protein (209 a.a.). The membrane-bound isoform can be proteolytically cleaved to generate a biologically active soluble isoform. Recombinant murine Flt3-Ligand is a soluble 18.6 kDa protein consisting of 163 amino acid residues.

Description: FGF-acidic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant murine FGF-acidic is a 15.9 kDa protein consisting of 141 amino acid residues.

Description: IL-33 is a proinflammatory protein that shares structural and functional characteristics with the IL-1 cytokine family. It binds and signals through the IL-1RL1/ST2 receptor activating NF-kappaB and MAP kinases. IL-33 induces production of TH2 cell related cytokines, including IL-4, IL-5 and IL-13, and exerts multiple inflammation related bioactivities. Recombinant murine IL-33 is a 17.5 kDa protein containing 158 amino acid residues.

Description: Murine SF20 is a bone marrow stroma-derived growth factor. SF20 is expressed in bone marrow, spleen stroma cells, resting mononuclear cells, resting CD8+ and CD19+ cells and activated CD8+ T cells and has been shown to bind to the surface of cells expressing the receptor TSA-1 (Thymic shared Ag-1). Among its biological activities, SF20 stimulates the proliferation of FDCP2 cells (a mouse factor-dependent hemopoietic cell line) and mouse lymphoid cells. Recombinant murine SF20 is a 15.8 kDa protein containing 143 amino acid residues.

Description: RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The three known members of this family; Resistin, RELMα and RELMβ are 85-94 amino acid secreted proteins sharing a conserved C-terminal domain characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. RELMα and Resistin are secreted exclusively by adipocytes while RELMβ is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMα re still unknown. Recombinant murine RELMα is a 10.0 kDa monomeric protein containing 88 amino acid residues.

Description: IL-1α is a non-secreted proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1α and IL-1β binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant murine IL-1α is an 17.9 kDa protein containing 156 amino acid residues.

Description: IL-1β is a proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1α and IL-1β binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant murine IL-1β is a 17.5 kDa protein containing 153 amino acid residues.

Description: LIX is a CXC chemokine that signals through the CXCR2 receptor.  It is expressed in monocytes, platelets, endothelial cells, and mast cells.  LIX is a chemoattractant for neutrophils.  The two naturally occurring variants of LIX; LIX 1-78 (GCP-2) and LIX 9-78 (GCP-2), contain 78 and 70 amino acid residues, respectively.  LIX contains the four conserved cysteine residues present in CXC chemokines, and also contains the ‘ELR’ motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors.  Recombinant murine LIX is a 7.6 kDa protein consisting of amino acid residues 9-78 of the full length LIX protein (70 amino acids).

Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant murine Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the naturally occurring chemically modified Cys residue.

Description: MIP-3β is a CC chemokine that is expressed in the thymus, lymph nodes and in activated bone marrow stromal cells and signals through the CCR7 receptor. MIP-3β is a chemoattractant for T and B lymphocytes and myeloid progenitor cells. Human MIP-3β is active on murine cells. Recombinant murine MIP-3β is a 9.2 kDa protein containing 83 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

Description: The MCP proteins belong to the CC chemokine family, and signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated T cells, basophils, NK cells, and immature dendritic cells. The MCP family cross reacts across species. Recombinant murine JE is a 13.8 kDa protein containing 125 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.

Description: Both MIP-1 α and MIP-1 β are structurally and functionally related CC chemokines. They participate in the host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells e.g. macrophages, lymphocytes and NK cells. While both MIP-1 α and MIP-1 β exert similar effects on monocytes their effect on lymphocytes differ; with MIP-1 α selectively attracting CD8+ lymphocytes and MIP-1 β selectively attracting CD4+ lymphocytes. Additionally, MIP-1 α and MIP-1 β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1 α and MIP-1 β are active on human and murine hematopoietic cells. Recombinant murine MIP-1 α is a 7.8 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.