Other Proteins

The PI3K comprises of a 110 kDa catalytic subunit and an 85 kDa regulatory subunit. A number of isoforms of the 110 kDa catalytic subunit and the 85 kDa regulatory subunit exist in cells. p85α modulates the interaction between PI3K and platelet-derived growth factor receptor (1). Furthermore, estrogen receptor isoform ER-alpha binds in a ligand-dependent manner to the p85-alpha regulatory subunit of PI3K. Stimulation with estrogen increases ER-alpha-associated PI3K activity, leading to the activation of protein kinase B/AKT and endothelial nitric oxide synthase (eNOS) (2). PI3K (p85 alpha) Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and WNT Signaling research.

Phosphatidylinositol 3-kinase (PI3K) is a lipid kinase that phosphorylates the inositol ring of phosphatidylinositol and related lipid products at the 3-prime position. PI3K p85 subunit which is the regulatory subunit of PI3K and consists of 2 closely related proteins, p85-alpha and p85-beta (1). The activation of PI3K signaling in influenza A virus-infected cells is important for efficient virus replication (2). PI3K signaling in T cells can lead to organ-specific autoimmunity and the class IA PI3K-deficient mice manifest the cardinal features of human primary Sjogren’s syndrome-like disease (3). PI3k (p85 beta) Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Inflammation, Invasion/Metastasis, Lipid Kinases, Metabolic Disorder, Neurobiology, NfkB Pathway, and WNT Signaling research.

PIP5K3 (also known as phosphatidylinositol-3-phosphate 5-kinase type III or PIPKIII) encodes an enzyme that phosphorylates the D-5 position in PtdIns and phosphatidylinositol-3-phosphate (PtdIns3P) to make PtdIns5P and PtdIns (3,5)biphosphate. PIP5K3 belongs to a large family of lipid kinases that alter the phosphorylation status of intracellular phosphatidylinositol but also have protein kinase activity (1). PIP5K3 regulate cytoskeletal functions, membrane trafficking, and receptor signaling by recruiting protein complexes to cell- and endosomal-membranes. The inhibition of PIP5K3 renders the late endosome/lysosome compartment refractory to fusion with autophagosomes and multivesicular bodies (2). PIP5K3 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Inflammation, Invasion/Metastasis, Lipid Kinases, Metabolic Disorder, Neurobiology, NfkB Pathway, and WNT Signalin

POR is a flavoprotein that donates electrons to all microsomal P450 enzymes, including the steroidogenic enzymes P450c17, P450c21, and CYP51A1. POR encodes an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain which binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes (1). POR has been linked with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome (2). POR Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cancer, and Metabolic Disorder research.

PP2A is one of the four major Ser/Thr phosphatases which are implicated in the negative control of cell growth and division and encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A (1). PP2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B which is encoded by a diverse set of genes. The interaction was independent of ATP or magnesium ion and the inclusion of PTPA altered the substrate specificity of PP2A, with enhanced phosphotyrosine phosphatase activity and decreased phosphoserine phosphatase activity (2). PP2Aβ Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Metabolic Disorder, Phosphatases, Ser/Thr Kinases, and WNT Signaling research.

PP2B is a key regulator of the anaphase-promoting factor which is an excellent substrate for protein phosphatase. PP2B is involved in bovine ocular tissues and is postulated to be involved in the immunologic privilege of the cornea, in retinal signal transduction, and in the toxic effects of immunosuppressants on the eye. PP2B acts as an inhibitory constraint on I-LTP that is relieved by PKA, and that this inhibitory constraint acts as a gate to regulate the synaptic induction of L-LTP (1). PP2B plays a role in the transition from short- to long-term memory and also regulates bone formation through an effect on osteoblast differentiation (2). PP2B Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Metabolic Disorder, Phosphatases, and Ser/Thr Kinases research.

PRKAR1A or the cAMP-dependent protein kinase regulatory subunit type I alpha, is part of the type 1 PKA holoenzyme. PRKAR1A is found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids (1). Mutations in PRKAR1A gene cause Carney complex (CNC) and PRKAR1A can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2 (2). A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). PRKAR1A Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cardiovascular Disease, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway research.

PRKAR1B is the type I-beta regulatory subunit of cyclic AMP-dependent protein kinase A (PKA) which is an essential enzyme in the cAMP signaling pathway. PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP. PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. PKA undergoes a dramatic conformational change upon complex formation with the catalytic subunit (1). PRKAR1B subunits can dimerize through an N-terminal motif and this dimerization is necessary for binding to PKA anchoring proteins (AKAPs) and targeting of PKA to its site of action. PRKAR1B Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cardiovascular Disease, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway research.

PRMT5 is a protein arginine methyltransferase and part of a 20S methyltransferase complex that modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins (1). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. MEP50 associates with PRMT5 in the 20S arginine methyltransferase complex in HeLa cells (2). Antibodies directed against MEP50 can reduce the arginine methyltransferase activity of the immunopurified complex toward Sm substrates. PRMT5-mediated transcriptional repression of reporter gene is dependent on MEP50. PRMT5 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.