Rab11A Antibody (Rabbit mAb) [N14G1]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:500-1:1000 IF1:50

Application
WB, IF

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
24 kDa 24 kDa,36 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human brain tissue; Mouse brain tissue; Mouse spleen tissue; Rat brain tissue; Rat spleen tissue; A431 cells; C6 cells; A549 cells; HeLa cells; HCT 116 cells; LNCaP cells; Neuro-2a cells; 4T1 cells; EL4 cells; Jurkat cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Rab11A Antibody (Rabbit mAb) [N14G1] detects endogenous levels of total Rab11A protein.

Clone
N14G1

Synonym(s)
RAB11, RAB11A, Ras-related protein Rab-11A, Rab-11, YL8

Background
Rab11A belongs to the Rab11 subfamily of small GTPases within the Ras superfamily, alongside the closely related isoforms Rab11B and Rab25, and like other Rab proteins is anchored to membranes through C-terminal prenylation while cycling between an active, GTP-bound conformation and an inactive, GDP-bound conformation. This nucleotide-dependent switch is structurally centered on two mobile regions, switch 1 and switch 2, whose conformation differs sharply depending on which nucleotide is bound and which together form the principal surface recognized by downstream effector proteins. Rab11A localizes to recycling endosomes as well as the trans-Golgi network and post-Golgi vesicles, and once loaded with GTP it recruits a dedicated family of effectors, the Rab11-family interacting proteins, or FIPs, through a highly conserved carboxy-terminal Rab-binding domain shared across all FIP family members. Crystal structure analysis of active, GTP-bound Rab11A in complex with the Rab-binding domain of FIP2 reveals that the FIP2 domain forms a central alpha-helical coiled-coil, and this coiled-coil homodimerizes to generate two symmetrical binding interfaces, producing a heterotetrameric assembly of two FIP molecules bound to two Rab11 molecules rather than a simple one-to-one complex; within each interface, Rab11's switch 1 region is embedded directly between the two FIP2 helices, while the more flexible switch 2 region makes only peripheral contact with the effector, showing that switch 1 provides the dominant, structurally rigid anchor point for FIP recognition. FIP proteins divide into two structurally and functionally distinct classes based on additional domains flanking this shared Rab-binding domain: class I FIPs, including Rip11 and FIP2, carry N-terminal C2 or EF-hand domains that confer calcium and phospholipid sensitivity and direct most recycling cargo to docking sites at the phospholipid-enriched plasma membrane, while class II FIPs, including FIP3 and FIP4, instead bind the GTPase Arf6 and are recruited to the cleavage furrow and midbody during cytokinesis to supply endosomal membrane material for cell division. Through these FIP effectors, Rab11A additionally couples to motor proteins including myosin V, kinesin, and dynein, positioning the GTPase as the organizing hub that links cargo-laden recycling endosomes to the cytoskeletal transport machinery required to deliver receptors such as transferrin receptor and integrins back to the plasma membrane.

Background

Rab11A belongs to the Rab11 subfamily of small GTPases within the Ras superfamily, alongside the closely related isoforms Rab11B and Rab25, and like other Rab proteins is anchored to membranes through C-terminal prenylation while cycling between an active, GTP-bound conformation and an inactive, GDP-bound conformation. This nucleotide-dependent switch is structurally centered on two mobile regions, switch 1 and switch 2, whose conformation differs sharply depending on which nucleotide is bound and which together form the principal surface recognized by downstream effector proteins. Rab11A localizes to recycling endosomes as well as the trans-Golgi network and post-Golgi vesicles, and once loaded with GTP it recruits a dedicated family of effectors, the Rab11-family interacting proteins, or FIPs, through a highly conserved carboxy-terminal Rab-binding domain shared across all FIP family members. Crystal structure analysis of active, GTP-bound Rab11A in complex with the Rab-binding domain of FIP2 reveals that the FIP2 domain forms a central alpha-helical coiled-coil, and this coiled-coil homodimerizes to generate two symmetrical binding interfaces, producing a heterotetrameric assembly of two FIP molecules bound to two Rab11 molecules rather than a simple one-to-one complex; within each interface, Rab11's switch 1 region is embedded directly between the two FIP2 helices, while the more flexible switch 2 region makes only peripheral contact with the effector, showing that switch 1 provides the dominant, structurally rigid anchor point for FIP recognition. FIP proteins divide into two structurally and functionally distinct classes based on additional domains flanking this shared Rab-binding domain: class I FIPs, including Rip11 and FIP2, carry N-terminal C2 or EF-hand domains that confer calcium and phospholipid sensitivity and direct most recycling cargo to docking sites at the phospholipid-enriched plasma membrane, while class II FIPs, including FIP3 and FIP4, instead bind the GTPase Arf6 and are recruited to the cleavage furrow and midbody during cytokinesis to supply endosomal membrane material for cell division. Through these FIP effectors, Rab11A additionally couples to motor proteins including myosin V, kinesin, and dynein, positioning the GTPase as the organizing hub that links cargo-laden recycling endosomes to the cytoskeletal transport machinery required to deliver receptors such as transferrin receptor and integrins back to the plasma membrane.

References
https://pubmed.ncbi.nlm.nih.gov/19754446/ https://pubmed.ncbi.nlm.nih.gov/32744247/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%