Other Proteins

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multi-subunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.

ALK7 is a type I receptor for the TGFB family of signaling molecules in which type I receptors phosphorylate cytoplasmic SMAD transcription factors, which then translocate to the nucleus and interact directly with DNA or in complex with other transcription factors (1). Alk7 was expressed in all insulin, glucagon, and somatostatin -positive cells of the pancreas (2). GDF3 regulates adipose tissue homeostasis and energy balance under nutrient overload, in part, by signaling through ALK7 and Alk7 showed reduced fat accumulation and partial resistance to diet-induced obesity, similar to Gdf3. ALK7 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Angiogenesis, Cancer, Cardiovascular Disease, JAK/STAT Pathway, Neurobiology, and Ser/Thr Kinase research.

Annexin 5 is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin 5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel activity and a potential role in cellular signal transduction, inflammation, growth and differentiation. In vitro studies have shown that Annexin 5 is a cellular protein which plays a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with prothrombin (1). Through affinity assays Annexin 5 has been localized on cells that expressed phosphatidylserine on the cell surface, a feature found in apoptosis as well as other forms of cell death (2). Annexin 5 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cancer, and Neurobiology research.

ARAF belongs to the RAF subfamily of the Ser/Thr protein kinase family, and maybe involved in cell growth and development. ARAF play a critical role in cell growth and development (1).The N-terminal regulatory domain of ARAF interacted with the putative mitochondrial proteins TOM and TIM44. ARAF is expressed predominantly in urogenital tissues (2). The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus. ARAF Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Cancer research.

ARAF belongs to the RAF subfamily of the Ser/Thr protein kinase family, and maybe involved in cell growth and development. ARAF play a critical role in cell growth and development (1).The N-terminal regulatory domain of ARAF interacted with the putative mitochondrial proteins TOM and TIM44. ARAF is expressed predominantly in urogenital tissues (2). The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus. ARAF Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Cancer research.

ATF1 is a class of transcription factor that stimulates gene expression of several cell growth-related genes through protein kinase A-related cAMP response elements. ATF1 can physically associate with BRCA1 in vitro, in yeast, and in human cells and BRCA1 is implicated in the transcriptional activation of ATF1 target genes, some of which are involved in the transcriptional response to DNA damage (1). Mitogen- and stress-activated protein kinase 1 (MSK1) and MSK2 play a role in the stress-induced phosphorylation of ATF1 in primary embryonic fibroblasts. However, mitogen-induced phosphorylation of ATF1 is greatly reduced (2). ATF1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Angiogenesis, Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, Metabolic Disorder, Neurobiology, NfkB Pathway, and p38 Pathway research.

ATG13 is a protein that is part of the autophagy complex which is the major route by which cytoplasmic contents are delivered to the lysosome for degradation. ATG13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. In mammals, ATG13 interacts with ATG1 (ULK1/2) and FIP200 to form the autophagy. ATG101 can also bind to ATG13 protein and is important for the stability and basal phosphorylation of ATG13 and ULK1 (1). mTOR can suppress the autophagy process through direct regulation of the ULK1-Atg13-FIP200 complex where mTOR has been shown to phosphorylate ATG13 (2). ATG13 Protein is ideal for investigators involved in Signaling Proteins, Apoptosis Proteins, Angiogenesis, Angiogenesis, Apoptosis/Autophagy, Apoptosis/Autophagy, Cardiovascular Disease, Cardiovascular Disease, Cellular Stress, Cellular Stress, Inflammation, Inflammation, Metabolic Disorder, Metabolic Disorder, Neurobiology, Neurobiology, NfkB Pathway, NfkB Pathway, p38 Pathway, and