Recombinant Human FSP27 protein
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(1 Publication)
Recombinant Human FSP27 protein is a Human Full Length protein, in the 2 to 238 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, ELISA, WB, Mass Spec.
View Alternative Names
FSP27, CIDEC, Lipid transferase CIDEC, Cell death activator CIDE-3, Cell death-inducing DFFA-like effector protein C, Fat-specific protein FSP27 homolog
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human FSP27 protein (AB188449)
14% SDS-PAGE analysis of ab188449.
Lane 1 : Reduced and boiled sample, 2.5 μg
Lane 2 : Non-reduced and non-boiled sample, 2.5 μg
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
FSP27 plays a critical role in lipid metabolism and energy homeostasis. It localizes on the surface of lipid droplets where it interacts with other structural proteins to maintain the stability and size of these lipid storage structures within adipocytes. While it does not form a traditional protein complex its function integrates with the overall architecture of lipid droplets to ensure efficient fat storage and energy balance in the body.
Pathways
FSP27 significantly impacts the regulation of lipid metabolism and energy homeostasis pathways. It associates with the perilipin family of proteins which also manage lipid droplet dynamics important to adipocyte function. The protein interacts with pathways like the insulin signaling pathway and the PPARγ signaling pathway important for maintaining metabolic homeostasis and regulating adipocyte differentiation. These interactions ensure proper energy storage and expenditure balance playing a vital role in metabolic health.
Specifications
Form
Liquid
Additional notes
ab188449 was purifed using Ni-NTA chromatography.
General info
Function
Lipid transferase specifically expressed in white adipose tissue, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed : 18334488, PubMed : 19843876, PubMed : 20049731, PubMed : 23399566, PubMed : 30361435). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed : 18334488, PubMed : 19843876, PubMed : 20049731, PubMed : 23399566). Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by undergoing liquid-liquid phase separation (LLPS) and promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (PubMed : 18334488, PubMed : 19843876, PubMed : 20049731, PubMed : 23399566). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (PubMed : 18334488, PubMed : 19843876, PubMed : 20049731, PubMed : 23399566). Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (PubMed : 23399566). May also act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH (By similarity). When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (PubMed : 12429024).
Sequence similarities
Belongs to the CIDE family.
Post-translational modifications
Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life (about 15 minutes in 3T3-L1 cells). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation.
Subcellular localisation
Nucleus
Target data
Publications (1)
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Journal of the American Heart Association 8:e011431 PubMed31433737
2019
Applications
Unspecified application
Species
Unspecified reactive species
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