Human Recombinant RAB1B protein, hFc Tag (V2LY-0526-LY6432)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
hFc Tag
Protein Construction
This product is Human Recombinant RAB1B protein, hFc Tag consist of Amino Acid: 1-199 and predicts a molecular mass of 50.4 kDa.
Molecule Mass
50.4 kDa
Sequence
Amino Acid: 1-199
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
RAB1B, member RAS oncogene family
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).
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).
Biological Process
Biological Process autophagosome assemblyManual Assertion Based On ExperimentIBA:GO_Central
Biological Process endoplasmic reticulum to Golgi vesicle-mediated transportManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process Golgi organizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process intracellular protein transportManual Assertion Based On ExperimentIBA:GO_Central
Biological Process positive regulation of glycoprotein metabolic processManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process regulation of autophagosome assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process virion assemblyManual Assertion Based On ExperimentIGI:UniProtKB
Cellular Location
Cytoplasm
Membrane
Preautophagosomal structure membrane
Cytoplasm, perinuclear region
Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments (PubMed:11389151).
In the GDP-form, colocalizes with GDI in the cytoplasm (PubMed:11389151).
Co-localizes with MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (By similarity).
PTM
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.
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For research use only. Not intended for any clinical use.

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