Recombinant Human SAR1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
M G S S H H H H H H S S G L V P R G S H M S F I F E W I Y N G F S S V L Q F L G L Y K K S G K L V F L G L D N A G K T T L L H M L K D D R L G Q H V P T L H P T S E E L T I A G M T F T T F D L G G H E Q A R R V W K N Y L P A I N G I V F L V D C A D H S R L V E S K V E L N A L M T D E T I S N V P I L I L G N K I D R T D A I S E E K L R E I F G L Y G Q T T G K G N V T L K E L N A R P M E V F M C S V L K R Q G Y G E G F R W L S Q Y I D
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Small GTPase that cycles between an active GTP-bound and an inactive GDP-bound state and mainly functions in vesicle-mediated endoplasmic reticulum (ER) to Golgi transport. The active GTP-bound form inserts into the endoplasmic reticulum membrane where it recruits the remainder of the coat protein complex II/COPII. The coat protein complex II assembling and polymerizing on endoplasmic reticulum membrane is responsible for both the sorting of cargos and the deformation and budding of membranes into vesicles destined to the Golgi (PubMed:23433038, PubMed:32358066, PubMed:36369712). The GTPase activity of SAR1 by controlling the timing of COPII budding regulates the size of the formed vesicles and is important for cargo selection depending on their size (PubMed:32358066). Together with SEC16A, forms the organized scaffold defining endoplasmic reticulum exit sites (ERES), some specific domains of the endoplasmic reticulum where COPII vesicles form (PubMed:17005010). In addition to its role in vesicle trafficking, can also function as a leucine sensor regulating TORC1 signaling and more indirectly cellular metabolism, growth and survival. In absence of leucine, interacts with the GATOR2 complex via MIOS and inhibits TORC1 signaling. The binding of leucine abrogates the interaction with GATOR2 and the inhibition of the TORC1 signaling. This function is completely independent of the GTPase activity of SAR1B (PubMed:34290409).
SAR1, SARA, SARA1, SAR1A, Small COPII coat GTPase SAR1A, COPII-associated small GTPase, Secretion-associated Ras-related GTPase 1A
Recombinant Human SAR1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab87626 is purified using conventional chromatography techniques.
Small GTPase that cycles between an active GTP-bound and an inactive GDP-bound state and mainly functions in vesicle-mediated endoplasmic reticulum (ER) to Golgi transport. The active GTP-bound form inserts into the endoplasmic reticulum membrane where it recruits the remainder of the coat protein complex II/COPII. The coat protein complex II assembling and polymerizing on endoplasmic reticulum membrane is responsible for both the sorting of cargos and the deformation and budding of membranes into vesicles destined to the Golgi (PubMed:23433038, PubMed:32358066, PubMed:36369712). The GTPase activity of SAR1 by controlling the timing of COPII budding regulates the size of the formed vesicles and is important for cargo selection depending on their size (PubMed:32358066). Together with SEC16A, forms the organized scaffold defining endoplasmic reticulum exit sites (ERES), some specific domains of the endoplasmic reticulum where COPII vesicles form (PubMed:17005010). In addition to its role in vesicle trafficking, can also function as a leucine sensor regulating TORC1 signaling and more indirectly cellular metabolism, growth and survival. In absence of leucine, interacts with the GATOR2 complex via MIOS and inhibits TORC1 signaling. The binding of leucine abrogates the interaction with GATOR2 and the inhibition of the TORC1 signaling. This function is completely independent of the GTPase activity of SAR1B (PubMed:34290409).
Belongs to the small GTPase superfamily. SAR1 family.
SAR1 also known as SAR1A or SAR1B is a small GTPase belonging to the Ras superfamily. It plays an integral role in protein transport by regulating the formation of transport vesicles from the endoplasmic reticulum (ER). SAR1 has a molecular mass of about 21 kDa. It is ubiquitously expressed with significant levels observed in tissues involved in high protein synthesis activities such as liver and pancreas. Mechanically it switches between GDP-bound inactive and GTP-bound active states which is essential for its function in vesicle formation.
SAR1 is an important component in the coat protein complex II (COPII) which is vital for ER-to-Golgi transport. Within this complex SAR1 assists in the initiation of vesicle budding by recruiting other COPII components such as Sec23/Sec24 and Sec13/Sec31. This assembly is important for maintaining efficient secretory pathways and cellular homeostasis. The COPII complex with SAR1 ensures the proper sorting and packaging of proteins destined for the Golgi apparatus.
SAR1 plays an essential role in the secretory pathway facilitating intracellular protein trafficking. This pathway is vital for transporting proteins from the ER to the Golgi impacting processes such as cell signaling and membrane composition. SAR1 interacts with other proteins including Sec23 and Sec24 to ensure proper vesicle formation and function. These interactions highlight SAR1's role within the broader exocytic pathway signifying its importance in maintaining cellular function.
SAR1 mutations have been linked to lipid absorption disorders such as chylomicron retention disease (CMRD) and Anderson's disease. These conditions result from defective protein trafficking leading to impaired chylomicron secretion. In CMRD SAR1 dysfunction affects the related APOB protein contributing to the accumulation of fat in enterocytes and subsequent clinical symptoms. Understanding SAR1's function in these diseases may offer insights into therapeutic strategies targeting protein transport mechanisms.
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