You searched for: Proteins and Peptides

Supplier: STEMCELL Technologies

Ciliary neurotrophic factor (CNTF) is a neurotrophic factor that belongs to the four-helix bundle cytokine family and is structurally related to interleukin 6 (IL-6), interleukin 11 (IL-11), leukemia inhibitory factor (LIF), and oncostatin M (OSM). CNTF binds to its receptor CNFTRα and induces formation of a heterodimer of the signal transducing IL-6 receptor gp130 and LIF receptor (LIFR)-β, which triggers JAK/STAT, ERK, and PI3K signaling cascades (Schuster et al.). CNTF plays an important role in neurogenesis and the differentiation of neural stem cells and has been suggested to possess a therapeutic role in treating neurological disorders (Ding et al.; Oppenheim et al.). CNTF has also been shown to protect rod photoreceptors from light-induced damage and have therapeutic effects on retinal degenerative diseases caused by genetic defect or damage induced by toxins, autoantibodies, or strong light (Pernet et al.; Rhee et al.). Another therapeutic role of CNTF has been reported in protecting oligodendrocytes from death induced by apoptosis (Louis et al.). Additionally, CNTF is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into astrocytes (Krencik and Zhang). This product is animal component-free.

Supplier: STEMCELL Technologies

Interleukin 11 (IL-11) is a pleiotropic cytokine with effects on various tissues including the bone marrow, brain, and intestinal mucosa (Du andamp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. IL-11 induces the proliferation of hematopoietic stem cells (Lemoli et al.) and megakaryocytic progenitor cells (Bruno et al.), the maturation of megakaryocytes (Burstein et al.), and the production of platelets (Neben et al.). IL-11 is produced by a variety of cell types including hematopoietic cells, mesenchymal cells, epithelial cells, and neuronal cells. It was first cloned from a cDNA library of the human bone marrow-derived stromal cell line KM-102 (Kawashima et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 was the first pharmacologic agent approved for the treatment of chemotherapy-induced thrombocytopenia. IL-11 also plays a role in cancer progression by inducing the proliferation of epithelial cancer cells and the survival of metastatic cells at distant organs. Recently, IL-11 has gained interest for its role in the pathogenesis of diseases in dysregulated mucosal homeostasis associated with STAT3 upregulation, including gastrointestinal cancers (Putoczki et al.).

Supplier: STEMCELL Technologies

Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 T cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils and basophils) and monocytic lineages in vivo. It has been tested for mobilization of hematopoietic progenitor cells and for treating chemotherapy-induced neutropenia in patients. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

Supplier: Adipogen

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerization of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

Supplier: Adipogen

Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important homeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens. IL-2 promotes T cell proliferation and particularly naive T cells. IL-2 signaling on activated T cells is effected through a quaternary high-affinity receptor complex consisting of IL-2, IL-2Ralpha (CD25), IL-2Rbeta and IL-2Rgamma. Naive T cells are relatively insensitive to IL-2 as they only express small amounts of IL-2Rbeta and IL-2Rgamma. They only acquire sensitivity after CD25 expression, which captures the cytokine and presents it to the IL-2Rbeta and IL-2Rgamma receptors. IL-2 Superkine (Fc) is an artificial variant of IL-2 containing mutations at positions L80F / R81D / L85V / I 86V / I92F. These mutations are located in the molecule's core that acts to stabilize the structure and to give it a receptor-binding conformation mimicking native IL-2 bound to CD25. These mutations effectively eliminate the functional requirement of IL-2 for CD25 expression and elicit proliferation of T cells. Compared to IL-2, the IL-2 superkine induces superior expansion of cytotoxic T cells, leading to improved antitumour responses in vivo, and elicits proportionally less toxicity by lowering the expansion of Tregulatory cells and reducing pulmonary oedema.

Supplier: STEMCELL Technologies

Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the TRKB kinase receptor, and activates AKT and ERK pathways (Mattson et al.). It is expressed in hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, as well as homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman). This product is animal component-free.

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilization of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Mouse G-CSF was first purified from cultures of the WEHI-3B myelomonocytic leukemia cell line as the inducer of the terminal differentiation of WEHI-3B and other myeloid leukemia cell lines (Nicola et al.). It was later cloned in monkey COS cells from a cDNA library prepared with mRNA derived from mouse fibrosarcoma NFSA cells that produce G-CSF constitutively (Tsuchiya et al.). Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

Supplier: STEMCELL Technologies

Flt3/Flk-2 (Fms-like tyrosine kinase 3/fetal liver kinase-2) Ligand is a hematopoietic cytokine that plays an important role as a co-stimulatory factor in the proliferation, differentiation, and survival of hematopoietic stem and progenitor cells and the development of the immune system (Hannum et al.). Flt3/Flk-2 Ligand, together with stem cell factor and thrombopoietin, is commonly used to promote expansion of primitive CD34+ hematopoietic cells in culture. In combination with myeloid cytokines such as GM-CSF, G-CSF, or M-CSF, Flt3/Flk-2 Ligand enhances the growth and numbers of clonogenic myeloid progenitor cells. In synergy with the interleukins IL-3, IL-4, IL-7, IL-11, IL-12, IL-15, and GM-CSF and TNF-α, Flt3/Flk-2 Ligand regulates the development of various lymphoid progenitor cells, including dendritic cell, B cell, T cell, and NK cell progenitors. In contrast, Flt3/Flk-2 Ligand has no significant effect on erythropoiesis or megakaryopoiesis (Drexler and Quentmeier; Wodnar-Filipowicz). Flt3/Flk-2 Ligand exists as membrane-bound and soluble isoforms. Both isoforms are biologically active and signal through the class III tyrosine kinase receptor (Flt3/Flk-2, CD135; Rosnet et al.). Flt3/Flk-2 Ligand is produced by a variety of cell types, including uncommitted and committed hematopoietic cells and stromal fibroblasts, whereas expression of the Flt3/Flk-2 receptor is restricted to CD34+ hematopoietic stem and progenitor cells. Flt3/Flk-2 receptor is also expressed on leukemic cells and outside the hematopoietic system in the brain, placenta, and testis (Drexler and Quentmeier; Hannum et al.). This product is animal component-free.

Supplier: New England Biolabs (NEB)

NEBExpress GamS nuclease inhibitor is a recombinant protein that inhibits Exonuclease V (RecBCD) activity and stabilizes linear DNA templates in E. coli based in vitro protein synthesis reactions.

Supplier: Abnova

Human DPYSL2 full-length ORF recombinant protein with GST-tag at N-terminal.