Results for Other Proteins ( 57807 )
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The secreted cytokine RANKL (Receptor Activator of Nuclear factor kappa-B Ligand) is critically involved in osteoclastic differentiation and activation and in the regulation of specific immunity. RANKL exists as a homotrimer, is glycosylated, and occurs in 3 forms: cell-bound RANKL, which is expressed by osteoblast lineage cells, soluble RANKL (sRANKL), which is expressed by activated T lymphocytes, and a truncated ectodomain form derived from the cell-bound RANK Ligand, which is enzymatically processed by TACE (TNF-alpha converting enzyme (TACE; ADAM-17)). All three forms stimulate their specific receptor, RANK, which is located on osteoclastic and dendritic cells. RANKL binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. RANKL augments the ability of dendritic cells to stimulate naive T-cell proliferation. It may be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. It may also play
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Epidermal Growth Factor (EGF) is a growth factor that stimulates the proliferation of epithelial and epidermal cells. EGF family members are characterized by three intramolecular disulfide bonds and can bind to four different receptor tyrosine kinases known as EGFR/ErbB1, ErbB2, ErbB3, and ErbB4. Recombinant mouse EGF is a non-glycosylated protein, containing 54 amino acids, including 3 intra-molecular disulfide-bonds, with a molecular weight of 6.2 kDa.
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Epidermal Growth Factor (EGF) is a growth factor that stimulates the proliferation of epithelial and epidermal cells. EGF family members are characterized by three intramolecular disulfide bonds and can bind to four different receptor tyrosine kinases known as EGFR/ErbB1, ErbB2, ErbB3, and ErbB4. Recombinant mouse EGF is a non-glycosylated protein, containing 54 amino acids, including 3 intra-molecular disulfide-bonds, with a molecular weight of 6.2 kDa.
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Epstein-Barr Virus Induced Gene-3 (EBI3), is a secreted glycoprotein belonging to the hematopoietin receptor family and is related to the p40 subunit of IL-12. EBI3 was identified by its induced expression in B-lymphocytes in response to Epstein-Barr virus infection. EBI3 forms heterodimers with p28 to form IL-27 and with p35 to form IL-35. Both IL-27 and IL-35 have anti-inflammatory and regulatory activity. Recombinant mouse EBI3 is a non-glycosylated protein, containing 207 amino acids, with a molecular weight of 22.9 kDa.
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AATK or apoptosis-associated tyrosine kinase contains a tyrosine kinase domain at the N-terminus and a proline-rich domain at the C-terminus. AATK is induced during apoptosis, and expression of this protein is a necessary pre-requisite for the induction of growth arrest and/or apoptosis of myeloid precursor cells (1). AATK is highly detected in brain, lung, kidney, and pancreas (2). AATK is also shown to produce neuronal differentiation in a neuroblastoma cell line. AATK Protein is ideal for investigators involved in Signaling Proteins , Cellular Proteins, Apoptosis/Autophagy, Cancer, and Cytoplasmic Tyrosine Kinase research.
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DNMT1 has a role in the establishment and regulation of tissue-specific patterns of methylated cytosine residues. Aberrant methylation patterns are associated with certain human tumors and developmental abnormalities (1). DNMT1 enzyme is crucial for stable expression and function in vivo (2). DNMT1 is essential for maintenance of DNA methylation and the interaction of DNMT1 with the replication machinery is not strictly necessary for maintenance of DNA methylation, but improves its efficiency. DNMT1 is necessary and sufficient to maintain global methylation and aberrant CpG island methylation in human cancer cells. DNMT1 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.
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KDM4B or lysine (K)-specific demethylase 4B, which is also known as JMJD2B, contains a JmjN domain, a JmjC domain, a JD2H domain, 2 TUDOR domains, and a bipartite nuclear localization signal that overlaps the C-terminal part of the second TUDOR domain. KDM4B plays an essential role in human carcinogenesis through positive regulation of cyclin-dependent kinase 6 (1). KDM4B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development (2). KDM4B is regulated by both ERa and HIF-1a, drives breast cancer cell proliferation in normoxia and hypoxia, and epigenetically regulates the expression of cell cycle genes such as CCND1, CCNA1, and WEE1. KDM4B Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.
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KDM5B is a lysine (K)-specific demethylase 5B which is highly expressed in testis and shows the lowest expression in skeletal muscle (1). KDM5B is a histone H3 lysine 4 (H3K4) demethylase up-regulated in prostate cancer and associated with androgen receptor where it regulated its transcriptional activity in reporter gene assays (2). Overexpression of KDM5B in HeLa cells results in loss of tri-, di-, and monomethyl H3K4, but does not alter the methylation status of H3K9 or H3K36. A KDM5B containing highly conserved putative DNA/chromatin binding motif is specifically up-regulated in breast cancer. KDM5B Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.
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LC20 is the myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads (1). LC20 protein binds calcium and is activated by myosin light chain kinase. Two transcript variants encoding different isoforms have been found for LC20 and the deduced 172-amino acid protein is highly conserved, with only 3 differences between the human and chicken proteins. Light chain phosphorylation causes the folded monomeric form of myosin to extend and assemble into filaments. This observation established the involvement of the LC20 in conformational transitions of smooth muscle myosin (2). LC20 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, and Cardiovascular Disease research.