Proteins & Peptides

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.

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.

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.

Activating transcription factor (ATF)-2, also designated CRE-BP1, is a member of the ATF/cyclic AMP-responsive element binding protein family of transcription factors. ATF2 has two unique characteristics: it mediates the adenovirus E1A-induced trans-activation and forms a heterodimer with c-Jun (1). ATF2 is a target of the JNK signal transduction pathway (2). ATF2 is phosphorylated by JNK on two closely spaced threonine residues within the NH2-terminal activation domain. The replacement of these phosphorylation sites with alanine inhibited the transcriptional activity of ATF2. Furthermore, p38 MAPK can also phosphorylate ATF2. ATF2 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Angiogenesis, Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, Metabolic Disorder, Neurobiology, NfkB Pathway, and p38 Pathway research.

Activating transcription factor (ATF)-2, also designated CRE-BP1, is a member of the ATF/cyclic AMP-responsive element binding protein family of transcription factors. ATF2 has two unique characteristics: it mediates the adenovirus E1A-induced trans-activation and forms a heterodimer with c-Jun (1). ATF2 is a target of the JNK signal transduction pathway (2). ATF2 is phosphorylated by JNK on two closely spaced threonine residues within the NH2-terminal activation domain. The replacement of these phosphorylation sites with alanine inhibited the transcriptional activity of ATF2. Furthermore, p38 MAPK can also phosphorylate ATF2. ATF2 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, 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, Cardiovascular Disease, Cellular Stress, Inflammation, Metabolic Disorder, Neurobiology, NfkB Pathway, and p38 Pathway research.