Proteins & Peptides

ELK1 is a member of the ETS oncogene family of transcription factors (1). ELK1 protein interacts with promoter of the c-fos proto-oncogene and has been shown to be involved in the Ras-Raf-MAPK signaling cascade (1). Immature phosphorylation of transcription factor ELK-1 is implicated in premature aging syndrome and insulin resistance. Expression studies have revealed that elevated expression of ELK1-like protein in human esophageal can result in squamous cell carcinoma (2). ELK1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, and Neurobiology research.

ELK1 is a member of the ETS oncogene family of transcription factors (1). ELK1 protein interacts with promoter of the c-fos proto-oncogene and has been shown to be involved in the Ras-Raf-MAPK signaling cascade (1). Immature phosphorylation of transcription factor ELK-1 is implicated in premature aging syndrome and insulin resistance. Expression studies have revealed that elevated expression of ELK1-like protein in human esophageal can result in squamous cell carcinoma (2). ELK1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, and Neurobiology research.

ENPP2 functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids which evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. It also may induce parturition (1). ENPP2 stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas (2). ENPP2 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, and Inflammation research.

ENPP2 functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids which evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. It also may induce parturition (1). ENPP2 stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas (2). ENPP2 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, and Inflammation research.

EPHA8 is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family in which EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats (1). EPHA8 receptors play a role in axonal pathfinding during development of the mammalian nervous system (2). EPHA8 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Angiogenesis, Cancer, Cardiovascular Disease, Neurobiology, and Receptor Tyrosine Kinases research.

EPHA8 is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family in which EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats (1). EPHA8 receptors play a role in axonal pathfinding during development of the mammalian nervous system (2). EPHA8 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Angiogenesis, Cancer, Cardiovascular Disease, Neurobiology, and Receptor Tyrosine Kinases research.

ERK1 is a protein serine/threonine kinase that is a member of the extracellular signal-regulated kinases (ERKs) which are activated in response to numerous growth factors and cytokines (1). Activation of ERK1 requires both tyrosine and threonine phosphorylation that is mediated by MEK. ERK1 is ubiquitously distributed in tissues with the highest expression in heart, brain and spinal cord. Activated ERK1 translocates into the nucleus where it phosphorylates various transcription factors (e.g., Elk-1, c-Myc, c-Jun, c-Fos, and C/EBP beta). ERK1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, Neurobiology, and Ser/Thr Kinases research.

ERK1 is a protein serine/threonine kinase that is a member of the extracellular signal-regulated kinases (ERKs) which are activated in response to numerous growth factors and cytokines (1). Activation of ERK1 requires both tyrosine and threonine phosphorylation that is mediated by MEK. ERK1 is ubiquitously distributed in tissues with the highest expression in heart, brain and spinal cord. Activated ERK1 translocates into the nucleus where it phosphorylates various transcription factors (e.g., Elk-1, c-Myc, c-Jun, c-Fos, and C/EBP beta). ERK1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, Neurobiology, and Ser/Thr Kinases research.

FADD or Fas-Associated protein with Death Domain is an adaptor molecule that mediates death signaling by the Fas-receptor, tumor necrosis factor receptor and TRAIL-receptor. FADD binds to these receptors via the C-terminus Death Domain which then unmasks the N-terminal effector domain of FADD thereby allowing it to recruit caspase-8 and activate the cysteine protease cascade leading to apoptosis (1). Cells lacking FADD are defective in intracellular double-stranded RNA (dsRNA)-activated gene expression, including production of type I (alpha/beta) interferons and are thus very susceptible to viral infection (2). FADD Protein is ideal for investigators involved in Signaling Proteins, Adaptor Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, and NfkB Pathway research.