Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Rab1A (D3X9S) Rabbit mAb (BSA and Azide Free) #42627
Filter:
- WB
- IF
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 22 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
This product is the carrier free version of product #13075. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.
For standard formulation of this product see product #13075
For standard formulation of this product see product #13075
Storage
Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.
Specificity / Sensitivity
Rab1A (D3X9S) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total Rab1A protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys191 of human Rab1A protein.
Background
Ras-related protein Rab1A (Rab1A) is a member of the Ras superfamily of cellular G proteins that function in protein transport and membrane restructuring (1). Early immunofluorescence studies determined that Rab1A localizes to a region between the endoplasmic reticulum (ER) and the Golgi complex, and in early Golgi compartments (2). Rab1A binds and recruits the COPII complex tethering factor p115 to a cis-SNARE complex associated with COPII-coated, budding vesicles on the endoplasmic reticulum (3). A Rab1 effector complex containing several proteins, including the cis-Golgi tethering protein GM130 and the stacking protein GRASP65, is essential for targeting and fusion of COPII-coated vesicles with the Golgi complex (4). Rab1A also interacts with the golgin tethering and docking proteins giantin (GOLGB1) and golgin-84 to regulate Golgi structure formation and function (5,6). Thus, Rab1A plays an important role in mediating the export of newly synthesized target proteins from ER to the Golgi. As with other Rab proteins, Rab1A function requires an intrinsic GTPase cycling activity facilitated by associated GEF and GAP factors (7-9). In addition to mediating ER to Golgi transport, Rab1A is also involved in autophagy during early autophagosome formation (10,11).
- Zerial, M. and McBride, H. (2001) Nat Rev Mol Cell Biol 2, 107-17.
- Saraste, J. et al. (1995) J Cell Sci 108 ( Pt 4), 1541-52.
- Allan, B.B. et al. (2000) Science 289, 444-8.
- Moyer, B.D. et al. (2001) Traffic 2, 268-76.
- Koreishi, M. et al. (2013) PLoS One 8, e59821.
- Satoh, A. et al. (2003) Traffic 4, 153-61.
- Nuoffer, C. et al. (1994) J Cell Biol 125, 225-37.
- Pind, S.N. et al. (1994) J Cell Biol 125, 239-52.
- Haas, A.K. et al. (2007) J Cell Sci 120, 2997-3010.
- Huang, J. et al. (2011) Autophagy 7, 17-26.
- Lipatova, Z. et al. (2013) Mol Biol Cell , .
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For Research Use Only. Not for Use in Diagnostic Procedures.
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