Other Proteins

IRAK3 or interleukin-1 receptor-associated kinase 3 is a member of the interleukin-1 receptor-associated kinase protein family which is essential components of the Toll/IL-R immune signal transduction pathways. IRAK3 is primarily expressed in monocytes and macrophages and functions as a negative regulator of Toll-like receptor signaling (1). IRAKM mediates critical aspects of innate immunity that result in an immunocompromised state during sepsis (2). Mutations in IRAK3 are associated with a susceptibility to asthma. IRAK3 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Inflammation, NfkB Pathway, p38 Pathway, and Ser/Thr Kinases research.

IRS1 is the substrate for the insulin tyrosine kinase receptor and is found in a variety of insulin-responsive cells and tissues. IRS1 protein has no intrinsic enzymatic activity but acts as a docking protein, via the SH2 domains, for mediating the insulin downstream signaling events. IRS1 has been shown to associate with the 14-3-3 family of proteins and this could play a role in the regulation of insulin sensitivity by interrupting the association between the insulin receptor and IRS1 (1). IRS1 may be associated with colorectal cancer and diet and related factors may affect the risk by modifying plasma insulin levels. Thus, the inter-individual variation in insulin signaling mediated by IRS1 may play a plausible role in the development of colorectal cancer (2). IRS1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Cancer, Cellular Stress, and ERK/MAPK Pathway research.

IRS1 is the substrate for the insulin tyrosine kinase receptor and is found in a variety of insulin-responsive cells and tissues. IRS1 protein has no intrinsic enzymatic activity but acts as a docking protein, via the SH2 domains, for mediating the insulin downstream signaling events. IRS1 has been shown to associate with the 14-3-3 family of proteins and this could play a role in the regulation of insulin sensitivity by interrupting the association between the insulin receptor and IRS1 (1). IRS1 may be associated with colorectal cancer and diet and related factors may affect the risk by modifying plasma insulin levels. Thus, the inter-individual variation in insulin signaling mediated by IRS1 may play a plausible role in the development of colorectal cancer (2). IRS1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Cancer, Cellular Stress, and ERK/MAPK Pathway research.

KAT3A has intrinsic histone acetyltransferase activity that acts as a scaffold to stabilize additional protein interactions with the transcription complex and acetylates both histone and non-histone proteins. KAT3A (CREBBP) expressed as a nuclear protein that binds to cAMP-response element binding protein (CREB) and involved in the transcriptional coactivation of many different transcription factors. KAT3A plays a main role in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition (1). KAT3A also plays a critical role in the transmission of inductive signals from cell surface receptors to the transcriptional apparatus (2). KAT3A Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway resea

KAT3B (also known as EP300) encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein that functions as a histone acetyltransferase. KAT3B regulates transcription via chromatin remodeling and is important in the processes of cell proliferation and differentiation. KAT3B binding is a highly accurate process and can be used for identifying enhancers and their associated activities (1). KAT3B is also useful in the study of the role of tissue-specific enhancers in human biology and diseases on a genome wide scale. Defects in KAT3B gene are a cause of Rubinstein-Taybi syndrome that play a important role in epithelial cancer and act as a classic tumor suppressor gene (2). KAT3B Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway

KAT8 (MYST1) or MYST histone acetyltransferase 1 is a signaling protein that belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein which play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. MYST1 have a chromodomain that involved in protein-protein interactions and targeting transcriptional regulators to chromatin (1). MYST histone acetyltransferase 1 is also involved in ATM function (2). KAT8 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway research.

KAT9 (also known as ELP3) is the catalytic subunit of the histone acetyltransferase (HAT) elongator complex, which contributes to transcript elongation and also regulates the maturation of projection neurons. The knockdown of KAT9 by antisense morpholinos in zebrafish embryos resulted in dose-dependent shortening and abnormal branching of motor neurons with no concomitant morphologic abnormalities (1). KAT9 knockdown also impairs paternal DNA demethylation as indicated by reporter binding, immunostaining, and bisulfite sequencing (2). KAT9 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway research.

KDM1A or lysine (K)-specific demethylase 1A is a nuclear protein containing a SWIRM domain, a FAD-binding motif, and an amine oxidase domain that is a component of several histone deacetylase complexes and act as a histone demethylase. (1) H3K4 histone demethylase activity of KDM1A is partly responsible for the repressive activity of TAL1 and restricts TAL1 function in hematopoiesis (1). KDM1A plays an essential role for CoREST in demethylation of H3K4 both in vitro and in vivo (2). KDM1A Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.

KDM2A or lysine (K)-specific demethylase 2A is a member of the F-box protein family that are components of the modular E3 ubiquitin protein ligases called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination (1). KDM2A belongs to the Fbls class and, in addition to the presence of an F-box, contains at least six highly degenerated leucine-rich repeats which play a role in epigenetic silencing. The demethylase activity of the JmjC domain-containing proteins is conserved from yeast to human (2). KDM2A Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.