Proteins & Peptides

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.

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.

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.

KDM4A or lysine (K)-specific demethylase 4A is a member of the Jumonji domain 2 (JMJD2) family that encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. KDM4A functions in euchromatin to remove histone methylation marks that are associated with active transcription (1). KDM4A also act as a trimethylation-specific demethylase those converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor (2). KDM4A Protein is ideal for investigators involved in Cancer, Cell Cycle, and Inflammation research.

KDM4A or lysine (K)-specific demethylase 4A is a member of the Jumonji domain 2 (JMJD2) family that encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. KDM4A functions in euchromatin to remove histone methylation marks that are associated with active transcription (1). KDM4A also act as a trimethylation-specific demethylase those converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor (2). KDM4A Protein is ideal for investigators involved in Cancer, Cell Cycle, and Inflammation research.

KDM4C or lysine-specific demethylase 4C functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form (1). KDM4C is a member of the Jumonji domain 2 (JMJD2) family and contains one JmjC domain, one JmjN domain, two PHD-type zinc fingers, and two Tudor domains. KDM4C may contribute to tumor development and inhibition of KDM4C expression leads to decreased cell proliferation. KDM4C has been shown to play an important role in the development and/or progression of various types of cancer, including esophageal squamous cell carcinoma(2). KDM4C Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.

KDM4C or lysine-specific demethylase 4C functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form (1). KDM4C is a member of the Jumonji domain 2 (JMJD2) family and contains one JmjC domain, one JmjN domain, two PHD-type zinc fingers, and two Tudor domains. KDM4C may contribute to tumor development and inhibition of KDM4C expression leads to decreased cell proliferation. KDM4C has been shown to play an important role in the development and/or progression of various types of cancer, including esophageal squamous cell carcinoma(2). KDM4C Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.