GTP-binding protein SAR1B is a small GTPase that plays a crucial role in the transport of proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. This protein is part of the COPII coat complex, which is essential for the formation of transport vesicles. The SAR1B protein is encoded by the SAR1B gene and is involved in various cellular processes, including lipid metabolism and protein trafficking.
SAR1B functions as a homodimer and is activated by the guanine nucleotide exchange factor PREB. Upon activation, SAR1B binds to GTP, which induces a conformational change that allows it to interact with other components of the COPII coat complex. This interaction is critical for the budding of transport vesicles from the ER membrane.
The primary role of SAR1B is to facilitate the transport of proteins from the ER to the Golgi apparatus. This process is vital for the proper functioning of the secretory pathway, which is responsible for the synthesis, modification, and sorting of proteins destined for various cellular locations.
Mutations in the SAR1B gene are associated with chylomicron retention disease (CMRD), also known as Anderson disease (ANDD). This rare genetic disorder is characterized by the inability to properly secrete chylomicrons, leading to fat malabsorption and various gastrointestinal symptoms. Patients with CMRD typically present with failure to thrive, diarrhea, and steatorrhea (fatty stools).
Mouse anti-human SAR1B antibodies are monoclonal antibodies developed to specifically target the SAR1B protein in human samples. These antibodies are widely used in various scientific applications, including Western blotting, immunohistochemistry, and immunocytochemistry. They are valuable tools for researchers studying the function and regulation of SAR1B, as well as its role in diseases such as CMRD.