This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2.
Proliferating Cell Nuclear Antigen (PCNA) is a protein only expresse in nomal proliferate cells and cancer cells. It is central to both DNA replication and repair. One of the well-established functions for PCNA is its role as the processivity factor for DNA polymerase delta and epsilon. PCNA tethers the polymerase catalytic unit to the DNA template for rapid and processive DNA synthesis. Two forms of PCNA exist in cells: (i) a detergent-insoluble trimeric form stably associated with the replicating forks during S phase and (ii) a soluble form in quiescent cells in G1 and G2 phases. PCNA forms a toroidal trimer in S phase with replication factor-C (RF-C) and DNA in an ATP-dependent manner and enables the loading of DNA polymerase delta and epsilon onto the complex. The close association of PCNA with kinase complexes involved in cell cycle machinery indicates that PCNA has a regulatory role in cell cycle progression. PCNA also participates in the processing of branched intermediates that arise during the lagging strand DNA synthesis.
Neuroendocrine convertase 1, also known as Prohormone convertase 1, Proprotein convertase 1, PCSK1 and NEC1, is anenzyme which belongs to thepeptidase S8 family and Furin subfamily. PCSK1 is an enzyme that performs the proteolytic cleavage of prohormones to their intermediate (or sometimes completely cleaved) forms. It is present only in neuroendocrine cells such as brain, pituitary and adrenal, and most often cleaves after a pair of basic residues within prohormones but can occasionally cleave after a single arginine. It binds to a protein known as proSAAS, which also represents its endogenous inhibitor. PCSK1 is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. PCSK1 substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin. Defects in PCSK1 are the cause of proprotein convertase 1 deficiency (PC1 deficiency). PC1 deficiency is characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small-intestinal absorptive dysfunction. It is due to impaired processing of prohormones.
Human Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesized as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER ; the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2); and play a role in the neural development.
Recombinant Human Proprotein Convertase Subtilisin/Kexin Type 9/PCSK9 (D374Y) is a gain of function mutant of human PCSK9 protein. Human PCSK9 is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesized as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER, the pro domain and mature chain are secreted together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and it plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the neural development.
Human Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesized as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER , the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the neural development.
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