Recombinant Human FSP27 protein is a Human Full Length protein, in the 2 to 238 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, ELISA, WB, MS.
M K H H H H H H A S E Y A M K S L S L L Y P K S L S R H V S V R T S V V T Q Q L L S E P S P K A P R A R P C R V S T A D R S V R K G I M A Y S L E D L L L K V R D T L M L A D K P F F L V L E E D G T T V E T E E Y F Q A L A G D T V F M V L Q K G Q K W Q P P S E Q G T R H P L S L S H K P A K K I D V A R V T F D L Y K L N P Q D F I G C L N V K A T F Y D T Y S L S Y D L H C C G A K R I M K E A F R W A L F S M Q A T G H V L L G T S C Y L Q Q L L D A T E E G Q P P K G K A S S L I P T C L K I L Q
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
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).
FSP27, CIDEC, Lipid transferase CIDEC, Cell death activator CIDE-3, Cell death-inducing DFFA-like effector protein C, Fat-specific protein FSP27 homolog
Recombinant Human FSP27 protein is a Human Full Length protein, in the 2 to 238 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, ELISA, WB, MS.
pH: 4
Constituents: 0.25% Sodium Acetate Buffer, 0.15% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab188449 was purifed using Ni-NTA chromatography.
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).
Belongs to the CIDE family.
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.
Previously labelled as CIDE C.
FSP27 also known as CIDEC (cell death-inducing DFFA-like effector C) is a protein involved in lipid droplet formation and is composed of about 238 amino acids with a mass of approximately 27 kDa. Researchers observe its expression predominantly in adipose tissue. As an important component FSP27 contributes to the regulation and accumulation of lipids within cells particularly in white adipose tissue where it facilitates triglyceride storage.
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.
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.
FSP27 has strong associations with obesity and type 2 diabetes. This protein's function in lipid storage and energy regulation links it with metabolic syndrome development. When dysregulated it may contribute to excess adipose tissue growth leading to obesity and impaired metabolic pathways advancing insulin resistance seen in type 2 diabetes. It interacts notably with proteins such as adiponectin which is known to influence glucose regulation and fatty acid breakdown further connecting FSP27 to metabolic disruptions.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
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
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com