Other Proteins

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.

KDM5C or lysine (K)-specific demethylase 5C is a member of the SMCY homolog family that encodes a protein with one ARID domain, one JmjC domain, one JmjN domain and two PHD-type zinc fingers. KDM5C is mainly expressed in brain and skeletal muscle. KDM5C is involved in the regulation of transcription and chromatin remodeling that cause X-linked mental retardation (1). KDM5C is also essential for spermatogenesis and expression of male-specific minor histocompatibility antigens (2). KDM5C Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.

LOXL1 is a member of the lysyl oxidase gene family which is essential to the biogenesis of connective tissue. LOXL1 encodes an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. LOXL1 is responsible for catalyzing the oxidative deamination of lysine residues of tropoelastin and this deamination causes spontaneous cross-linking and formation of elastin polymer fibers (1). LOXL1 serves both as a crosslinking enzyme and an element of the scaffold to ensure spatially defined deposition of elastin (2). LOXL1 Protein is ideal for investigators involved in Signaling Proteins, Lysyl Oxidase Proteins, Cancer, and Metabolic Disorder research.

LOXL2 is a member of the lysyl oxidase gene family which is essential for the biogenesis of connective tissue. LOXL2 encodes an extracellular copper-dependent amine oxidase that catalyzes the first step in the formation of crosslinks in collagens and elastin. LOXL2 may play an important role in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family (1). LOXL2 may mediate fibroblast activation through enzymatic crosslinking of fibrillar collagen and local matrix tension, resulting in activation of TGFb1 signaling (2). LOXL2 Protein is ideal for investigators involved in Signaling Proteins, Lysyl Oxidase Proteins, Cancer, and Metabolic Disorder research.

LOXL3 is a member of the lysyl oxidase gene family. This family is essential to the biogenesis of connective tissue. The lysyl oxidase gene family encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin (1). LOXL3 is highly expressed in central nervous system, uterus, heart, and leukocyte (1). LOXL3 plays an important role in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis. LOXL3 Protein is ideal for investigators involved in Signaling Proteins, Lysyl Oxidase Proteins, Cancer, and Metabolic Disorder research.

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.