ARF1 antibody
Cat.#: 3322-1
Rabbit Monoclonal Antibody
Clone ID: EPR443
Swiss Prot: P84077
Mol Weight: 21kDa
Size: 100ul
Description
ARF1 (small GTP-binding ADP-ribosylation factor 1) is a member of the ARF family, which contains five other ARF proteins (1). ARF1 functions in various membrane trafficking events in the ER-Golgi system and in the maintenance of organelle structure. Inactive ARF1 (ARF1-GDP) localizes in the cytoplasm, while the active form (ARF1-GTP) localizes in the membrane (2-3). Active ARF1 is also localized to the Golgi complex by regulating the assembly of coat proteins onto membranes and mediating traffic in the ER-Golgi. ARF1 activates phospholipase D and phosphatidylinositol 4-phosphate 5-kinase and recruits COPI to membranes (4-5).
Recommended Applications
WB, IHC, ICC
Applications and Recommended Dilution Factors
WB: 1:1,000-10,000
IHC: 1:100 - 250
ICC: 1:50 - 100
Species Reactivity
Human, Mouse, Rat
Mouse cross reactivity tested by western blot and IHC
Rat cross reactivity tested by western blot only
Products Data
Western blot analysis on (A) fetal kidney, (B) fetal brain, and (C) MCF-7 lysates using anti-ARF1 RabMAb (cat. #3322-1).
Immunohistochemical analysis of paraffin-embedded human breast ductal carcinoma tissue using anti-ARF1 RabMAb (cat. #3322-1).
Immunohistochemical analysis of paraffin-embedded human colonic adenocarcinoma tissue using anti-ARF1 RabMAb (cat. #3322-1).
Specificity
A synthetic peptide corresponding to residues in human ARF1 was used as an immunogen.
Storage Condition and Buffer
Store at -20 °C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Alternative Names
ARF1 antibody, - antibody, ADP-ribosylation factor 1 antibody, antibody
Description References
1. Bobak et al. Proc. Nat. Acad. Sci. 86: 6101-6105, 1989.
2. Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, R. A., and Rothman, J. E. (1991) Cell 67, 239
3. Yang, C. Z., Heimberg, H., D\'Souza-Schorey, C., Mueckler, M. M., and Stahl, P. D. (1998) J. Biol. Chem. 273, 4006
4. Bonifacino, J.S., and J. Lippincott-Schwartz. 2003. Nat. Rev. Mol. Cell Biol. 4:409
5. Nie, Z., D.S. Hirsch, and P.A. Randazzo. 2003. Arf and its many interactors. Curr. Opin. Cell Biol. 15:396