S100A6 (D3H3W) Rabbit mAb #13162
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 10 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cation in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4).
S100A6 (calcyclin) is involved in a number of cellular processes, including exocytosis (5) and cell cycle regulation (6). In addition, S100A6 interacts with a number of proteins such as SIP, GAPDH, and annexins in a calcium-dependent fashion (7,8). Research studies demonstrate that a down regulation of corresponding S100A6 gene expression causes a decrease in cell proliferation (6).
- Heizmann, C.W. et al. (2002) Front Biosci 7, d1356-68.
- Donato, R. (2003) Microsc Res Tech 60, 540-51.
- Marenholz, I. et al. (2004) Biochem Biophys Res Commun 322, 1111-22.
- Santamaria-Kisiel, L. et al. (2006) Biochem J 396, 201-14.
- Okazaki, K. et al. (1994) J Biol Chem 269, 6149-52.
- Breen, E.C. and Tang, K. (2003) J Cell Biochem 88, 848-54.
- Nowotny, M. et al. (2003) J Biol Chem 278, 26923-8.
- Filipek, A. and Wojda, U. (1996) Biochem J 320 ( Pt 2), 585-7.
- Bao, L. et al. (2012) FEBS J 279, 4576-88.
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