Human CHKA protein (Recombinant) (N-His) (STJP010900)

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STJP010900
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human CHKA-N-His protein was developed from e. coli and has a target region of N-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: CHKA
Gene ID: 1119
Uniprot ID: CHKA_HUMAN
Immunogen Region: Asp138-Leu376
Immunogen: Homo sapiens (Human)
Function Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth. Isoform 1: This isoform plays a key role in lipolysis of lipid droplets following glucose deprivation. In response to glucose deprivation, phosphorylated by AMPK, promoting localization to lipid droplets. Phosphorylation is followed by acetylation by KAT5, leading to dissociation of the homodimer into a monomer. Monomeric CHKA isoform 1 is converted into a tyrosine-protein kinase, which phosphorylates lipid droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of lipid droplets.
Protein Name Choline Kinase Alpha
Ck
Chetk-Alpha
Ethanolamine Kinase
Ek
Database Links Reactome: R-HSA-1483191
Reactome: R-HSA-1483213
Cellular Localisation Cytoplasm
Cytosol
Isoform 1: Lipid Droplet
Isoform 1 Localizes To Lipid Droplets Following Phosphorylation By Ampk
Alternative Protein Names Choline Kinase Alpha protein
Ck protein
Chetk-Alpha protein
Ethanolamine Kinase protein
Ek protein
CHKA protein
CHK protein
CKI protein

Information sourced from Uniprot.org

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