The PNPLA8 Polyclonal Antibody (PAC057472) is a valuable tool for researchers studying PNPLA8, a protein involved in lipid metabolism and storage. This antibody, produced in rabbits, exhibits high reactivity with human samples and is validated for use in Western blot applications. By targeting the PNPLA8 protein, this antibody allows for detection and analysis in various cell types, making it ideal for investigations in metabolism, obesity, and related disorders.PNPLA8, also known as adiponutrin, plays a crucial role in lipid droplet turnover and triglyceride metabolism. Its functions in lipid homeostasis make it a key player in the development of metabolic diseases such as obesity, fatty liver disease, and insulin resistance.
By studying the activity of PNPLA8, researchers can gain insights into the underlying mechanisms of these conditions and potentially identify new targets for therapeutic intervention.In conclusion, the PNPLA8 Polyclonal Antibody is a valuable tool for researchers interested in lipid metabolism and metabolic diseases. Its high reactivity and specificity make it suitable for various experimental applications, enabling in-depth exploration of PNPLA8 functions and its implications for human health.
IHC image of PACO57472 diluted at 1:400 and staining in paraffin-embedded human adrenal gland tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.
Immunofluorescence staining of A549 cells with PACO57472 at 1:133, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
IHC image of PACO57472 diluted at 1:400 and staining in paraffin-embedded human small intestine tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.
Background:
Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids.
PNPLA8: Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids. 2 isoforms of the human protein are produced by alternative splicing.Protein type: Membrane protein, integral; EC 3.1.1.5; Phospholipase; Motility/polarity/chemotaxisChromosomal Location of Human Ortholog: 7q31Cellular Component: endoplasmic reticulum membrane; intracellular; membrane; peroxisomal membrane; peroxisomeMolecular Function: calcium-independent phospholipase A2 activity; phospholipase A2 activityBiological Process: arachidonic acid metabolic process; arachidonic acid secretion; cell death; fatty acid metabolic process; linoleic acid metabolic process; phosphatidylethanolamine catabolic process; prostaglandin biosynthetic processDisease: Mitochondrial Myopathy With Lactic Acidosis
UniProt Protein Details:
NCBI Summary:
This gene encodes a member of the patatin-like phospholipase domain containing protein family. Members of this family are phospholipases which catalyze the cleavage of fatty acids from membrane phospholipids. The product of this gene is a calcium-independent phospholipase. Mutations in this gene have been associated with mitochondrial myopathy with lactic acidosis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2015]