PLCXD3 Human
Escherichia Coli.
PI-PLC X domain-containing protein 3, phosphatidylinositol-specific phospholipase C X domain containing 3, phosphatidylinositol-specific phospholipase C, X domain containing 3
Greater than 85.0% as determined by SDS-PAGE.
Description
PLCXD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a.) and having a molecular mass of 38.7 kDa.
PLCXD3 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Product Specs
PI-PLC X domain-containing protein 3, phosphatidylinositol-specific phospholipase C X domain containing 3, phosphatidylinositol-specific phospholipase C, X domain containing 3
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MGSMASSQGK NELKLADWMA TLPESMHSIP LTNLAIPGSH DSFSFYIDEA SPVGPEQPET VQNFVSVFGT VAKKLMRKWL ATQTMNFTGQ LGAGIRYFDL RISTKPRDPD NELYFAHGLF SAKVNEGLEE INAFLTDHHK EVVFLDFNHF YGMQKYHHEK LVQMLKDIYG NKMCPAIFAQ EVSLKYLWEK DYQVLVFYHS PVALEVPFLW PGQMMPAPWA NTTDPEKLIQ FLQASITERR KKGSFFISQV VLTPKASTVV KGVASGLRET ITERALPAMM QWVRTQKPGE SGINIVTADF VELGDFISTV IKLNYVFDEG EANT
Product Science Overview
Phosphatidylinositol-specific phospholipase C (PI-PLC) is an enzyme that plays a crucial role in cellular signaling by hydrolyzing phosphatidylinositol into diacylglycerol (DAG) and inositol trisphosphate (IP3). The X domain of PI-PLC is essential for its catalytic activity and interaction with other cellular components.
PI-PLC enzymes are classified into several isoforms based on their structure and function. The X domain is a conserved region found in various PI-PLC isoforms, including the human recombinant form. This domain is responsible for the enzyme’s ability to bind and hydrolyze phosphatidylinositol.
The X domain of PI-PLC is characterized by its ability to interact with phospholipid membranes and catalyze the cleavage of phosphatidylinositol. This activity is crucial for the generation of second messengers, such as DAG and IP3, which are involved in various cellular processes, including cell growth, differentiation, and apoptosis.
The primary function of the PI-PLC X domain is to hydrolyze phosphatidylinositol into DAG and IP3. DAG acts as a secondary messenger that activates protein kinase C (PKC), while IP3 triggers the release of calcium ions from intracellular stores. These signaling molecules play a vital role in regulating various cellular functions, including metabolism, gene expression, and cell proliferation.
The PI-PLC X domain operates by binding to the phosphatidylinositol substrate and catalyzing its hydrolysis through an intramolecular nucleophilic attack. This reaction results in the formation of DAG and IP3, which then participate in downstream signaling pathways. The X domain’s structure allows it to interact with other proteins and lipids, facilitating its role in cellular signaling.
The activity of the PI-PLC X domain is regulated by various factors, including phosphorylation, interaction with other proteins, and changes in cellular calcium levels. These regulatory mechanisms ensure that the enzyme’s activity is tightly controlled, preventing aberrant signaling that could lead to pathological conditions.
