Recombinant Human RAB1B protein (Fc Chimera)
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Recombinant Human RAB1B protein (Fc Chimera) is a Human Fragment protein, in the 1 to 199 aa range, expressed in HEK 293 cells, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
Ras-related protein Rab-1B, RAB1B
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human RAB1B protein (Fc Chimera) (AB276657)
SDS-PAGE analysis of ab276657
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RAB1B plays a role in maintaining cellular homeostasis and protein secretion. It is an important component of the protein transport machinery participating in vesicle coat complex formation. It regulates the movement between the ER and Golgi working closely with other Rab proteins and their effectors to keep the flow of materials steady. The localization and activity of RAB1B influence processes important for cell growth and differentiation.
Pathways
RAB1B operates significantly in the secretory and trafficking pathways. It connects with the Golgi apparatus and ER pathways participating in sorting and cellular signaling. RAB1B interacts with other proteins such as COPII and Golgi SNARE proteins to facilitate transport vesicle movement. These proteins and pathways ensure precise and organized intracellular cargo traffic impacting multiple cellular processes directly tied to the secretory pathway.
Specifications
Form
Lyophilized
General info
Function
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed : 20545908, PubMed : 9437002, PubMed : 23236136). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed : 9437002). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (PubMed : 20545908). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (By similarity). Required to modulate the compacted morphology of the Golgi (PubMed : 26209634). Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity).
Sequence similarities
Belongs to the small GTPase superfamily. Rab family.
Post-translational modifications
Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1).. (Microbial infection) AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB1B constitutively active. It is later de-AMPylated by L.pneumophila SidD, releasing RAB1B from bacterial phagosomes.. (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI) (PubMed:21822290, PubMed:22307087). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB (PubMed:22158903, PubMed:22307087).. (Microbial infection) Glycosylated by S.typhimurium protein Ssek3: arginine GlcNAcylation prevents GTPase activity, thereby disrupting vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment.
Target data
Product promise
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