ARL8B Antibody #56085
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 21 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
ARL8B Antibody recognizes endogenous levels of total ARL8B protein. This antibody does not cross-react with ARL8A.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala137 of human ARL8B protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The small GTPases of the Arf and Rab families have critical roles in cytoskeletal organization and membrane/vesicular transport (1,2). The related ADP-ribosylation factor-like (ARL) family member ARL8, including two paralogs ARL8A and ARL8B, has emerged as an important regulator of lysosomal transport to the cell periphery (3,4). Lysosome positioning is a critical determinant of a number of physiological processes including plasma membrane repair, cell migration, antigen presentation, and response to nutrient availability. Membrane association of ARL8B is regulated by the BLOC-one related complex (BORC), a multi-subunit complex under the control of the mTOR pathway (5,6). Effectors of GTP-bound ARL8B include PLEKHM2/SKIP and the Vps41 subunit of the HOPS complex (7). Studies have found that ARL8B may be a critical factor for NK-mediated cytotoxicity by driving polarization of lytic granules toward the immune synapse (8). In addition, ARL8B has been shown to act as a negative regulator of autophagy (9). Knockdown of ARL8B resulted in increased fusion of autophagosomes with lysosomes. Furthermore, ARL8B depleted cells had reduced levels of pathogenic substrates associated with neurodegenerative diseases.
- Donaldson, J.G. and Jackson, C.L. (2011) Nat Rev Mol Cell Biol 12, 362-75.
- Kjos, I. et al. (2018) Biochim Biophys Acta Mol Cell Res 1865, 1397-1409.
- Hofmann, I. and Munro, S. (2006) J Cell Sci 119, 1494-503.
- Bagshaw, R.D. et al. (2006) Biochem Biophys Res Commun 344, 1186-91.
- Pu, J. et al. (2015) Dev Cell 33, 176-88.
- Filipek, P.A. et al. (2017) J Cell Biol 216, 4199-215.
- Khatter, D. et al. (2015) J Cell Sci 128, 1746-61.
- Tuli, A. et al. (2013) Mol Biol Cell 24, 3721-35.
- Korolchuk, V.I. et al. (2011) Nat Cell Biol 13, 453-60.
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