Golgin-97 (D8P2K) Rabbit mAb #13192
- WB
- IP
- IF
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 97 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunofluorescence (Immunocytochemistry) | 1:100 - 1:400 |
Storage
Protocol
Specificity / Sensitivity
Golgin-97 (D8P2K) Rabbit mAb recognizes endogenous levels of total golgin-97 protein.
Species Reactivity:
Human, Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu663 of human golgin-97 protein.
Background
The Golgi-associated protein golgin A1 (GOLGA1, golgin-97) was first isolated as a Golgi complex autoantigen associated with the autoimmune disorder Sjogren's syndrome (1). The golgin-97 protein contains a carboxy-terminal GRIP domain and is a commonly used trans-Golgi network (TGN) marker. All four known mammalian GRIP domain-containing proteins (golgin-97, golgin-245, GCC88, and GCC185) are found in the TGN, share extensive alpha-helical structure, and form homodimers (2). While all four golgin proteins localize to the TGN, they exhibit different membrane-binding abilities and are found in distinct TGN regions (3). Golgin-97 and golgin-245 are targeted to the TGN through an interaction between their GRIP domains and the Arl1 protein switch II region (4). Overexpression studies and siRNA assays with GRIP domain-containing proteins suggest that these proteins help to maintain TGN integrity and function by controlling localization of TGN resident proteins (5). By using a Shiga toxin B fragment (STxB)-based in vitro transport assay and an E-cadherin transport model system, golgin-97 and its effector Arl1-GTP were shown to play a role in trans-Golgi endosomal trafficking (6,7). Research studies also suggest that golgin-97 may play a role in poxvirus morphogenesis and maturation (8,9).
- Griffith, K.J. et al. (1997) Arthritis Rheum 40, 1693-702.
- Luke, M.R. et al. (2005) Biochem J 388, 835-41.
- Derby, M.C. et al. (2004) J Cell Sci 117, 5865-74.
- Lu, L. and Hong, W. (2003) Mol Biol Cell 14, 3767-81.
- Yoshino, A. et al. (2003) J Cell Sci 116, 4441-54.
- Lu, L. et al. (2004) Mol Biol Cell 15, 4426-43.
- Lock, J.G. et al. (2005) Traffic 6, 1142-56.
- Alzhanova, D. and Hruby, D.E. (2006) J Virol 80, 11520-7.
- Alzhanova, D. and Hruby, D.E. (2007) Virology 362, 421-7.
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