Although underappreciated, the Golgi apparatus is indispensable to normal cellular function by ensuring proteins are properly folded and sorted, and to direct diverse functions including autophagy. Disruptions to proper Golgi function can lead to many disease states, including diabetes, cancer, and neurodegenerative disorders such as Alzheimer's disease. The study of vesicular markers, including Golgi markers, is critical to our understanding of this amazing organelle's function in keeping the cell and organism healthy. Clarifying the mechanisms by which proteins are properly folded, sorted, quality controlled, and transported will prove important as more effective therapies are developed against a diverse array of human diseases.

We have previously explored the function of organelle markers USO1, GOLGA2, and GOLM1 but not how the corresponding antibodies can be applied in research. Organelle marker antibodies are common tools in cell biology research. They can be used with immunofluorescence technology to observe the morphological structure of organelles and understanding the subcellular localization of proteins. In turn, they help to explore the biological functions/role of organelle proteins in normal or disease models. These markers can also be used in Western blot (WB) experiments examining organelle extracts: as a positive control to determine whether the organelle is successfully extracted.

You can see some examples of ABclonal Technology's Golgi marker antibodies below. These are only a handful of the huge selection of targets that you can use to supplement your cutting-edge research!

Organelle marker antibodies are common tools in cell biology research. They can be used with immunofluorescence technology to observe the morphological structure of intracellular membrane-bound organelles and for understanding the subcellular localization of proteins. In turn, they help to explore the biological functions/role of organelle proteins in normal or disease models. These markers can also be used in Western blot (WB) experiments examining organelle extracts, as well as providing a positive control to determine whether the organelle is successfully extracted.

We focus today on the endoplasmic reticulum (ER) markers. The ER is a network of membrane-bound organelles that are the initial destination for proteins that are targeted for other organelles, the plasma membrane, or are to be secreted outside the cell. Proper ER function includes accepting the nascent protein as it is being translated by ribosomes, and ensuring that the protein is properly folded so it does not lead to accumulation of unusable cellular cargo. Disruptions in ER or the unfolded protein response can lead to cell death or various disease states such as cancer or neurodegenerative disorders. 

ABclonal provides many antibody products for the study of ER and Golgi markers, as well as exosome markers. Please read our blog on the vesicular transport system and its role in cellular homeostasis, and check out some of our ER marker antibodies below. We are honored to be part of your journey to better understanding vesicular transport and the fight against human diseases!

Endoplasmic Reticulum Marker

The endoplasmic reticulum is a membrane-bound organelle that is critical to the proper sorting and folding of proteins. Improperly folded proteins are normally allowed to refold into their functional conformation, and if not possible to repair, these unfolded proteins are directed to be degraded to prevent damage to the cell. The P4HB gene encodes a protein disulfide isomerase (PDI) that catalyzes both the formation of disulfide bonds, which form between cysteine residues to stabilize protein structure, and isomerization between or within molecules of secreted proteins. To achieve the natural conformation, this process takes place in the endoplasmic reticulum, so P4HB is often used as an ER marker. Studies on the oxidative folding mechanism indicate that molecular oxygen can oxidize the ER protein Ero1, and Ero1 can oxidize PDI through a disulfide bond. After this activity, PDI catalyzes the folding of proteins to form disulfide bonds.

Although underappreciated, the Golgi apparatus is indispensable to normal cellular function by ensuring proteins are properly folded and sorted, and to direct diverse functions including autophagy. Disruptions to proper Golgi function can lead to many disease states, including diabetes, cancer, and neurodegenerative disorders such as Alzheimer's disease.

Part of the Golgi protein family, USO1 protein (also known as vesicle docking protein p115) is a peripheral membrane protein that can be used as a Golgi marker. It cycles between the cytoplasm and the Golgi apparatus during interphase. The position of the USO1 protein is regulated by phosphorylation -- dephosphorylated proteins bind to the Golgi membrane and dissociate from the membrane when phosphorylated. This regulated transportation plays an important role in protein localization, secretion, and signal transduction. USO1 protein acts as a vesicle anchor by interacting with the target membrane and keeping the vesicles close to the target membrane. In addition, the USO1 protein interacts with GOLGA2 (GM130) and Giantin to promote endoplasmic reticulum-Golgi transportation. A large part of Golgi-related research is in understanding how to maintain proper Golgi function to prevent and treat human diseases.

AIFM1, also known as Apoptosis Inducing Factor (AIF), is a widely expressed flavoprotein that plays an important role in caspase-independent apoptosis. AIF normally exists in the mitochondrial intermembrane space.