Other Proteins

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.

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.

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.

FANCL or Fanconi anemia complementation group L is a member of the Fanconi anemia complementation group. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. FANCL is crucial in the FA pathway as the catalytic subunit required for monoubiquitination of FANCD2 (1). UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2 (2). FANCL Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.

FKBP1A is a member of the immunophilin protein family which plays a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP1A is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and Rapamycin. FKBP1A interacts with various type I receptors, including the TGF-beta type I receptor and competitive binding assays show that the type I receptor may be a natural ligand for FKBP1A (1). FKBP1A-deficient mice have normal skeletal muscle but show severe dilated cardiomyopathy and ventricular septal defects that mimic a human congenital heart disorder (2). FKBP1A Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Cardiovascular Disease, Inflammation, Neurobiology, and NfkB Pathway research.

FOS is a member of the FOS gene family that consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. FOS gene encodes a leucine zipper protein that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation (1). In some cases, expression of the FOS gene has also been associated with apoptotic cell death. FOS overexpression leads to decreased phosphorylation and dimerization of STAT1, which in turn downregulates p21 gene expression (2). This regulatory pathway may enhance the proliferation of lymphocytes in rheumatoid arthritis patients. FOS 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.

FRS3 or fibroblast growth factor receptor substrate 3 is a peripheral plasma membrane protein that is a substrate for the fibroblast growth factor receptor. During FGF or NGF stimulation, FRS3 becomes tyrosine phosphorylated and then serves as a platform for the recruitment of multiple signaling proteins for activation of the Ras-MAP kinase signaling cascade (1). FRS3 is mainly expressed in fibroblast and myoblast cell lines and undergo robust tyrosine phosphorylation in response to several mitogenic ligands. Through interaction with Rho family of small GTPases, FRS3 has been implicated in the reorganization of the actin cytoskeleton and subsequent morphological changes in various cells (2). FRS3 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and ERK/MAPK Pathway research.

GRB2 is an adaptor protein that is the homolog of the Sem5 gene of C. elegans and Drk gene of Drosophila. GRB2 protein contains one SH2 domain and two SH3 domains and plays a role in growth factor-mediated signal transduction. GRB2 forms a complex with activated EGFR and the RAS-specific guanine nucleotide exchange factor SOS1 thereby mediating the growth factor-induced activation of RAS (1). GRB2 has been implicated in growth factor regulation of the cytoskeleton and DNA synthesis. DAB2 also binds to GRB2 and competes with SOS for GRB2 binding. GRB2 interacts with the hepatitis C virus nonstructural 5A (NS5A) protein and inhibits the activation of ERK1 and ERK2 by EGF (2). GRB2 Protein is ideal for investigators involved in Signaling Proteins, Adaptor Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, JAK/STAT Pathway, and Neurobiology research.