JIP4/SPAG9 (D72F4) XP® Rabbit mAb #5519
- WB
- IP
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 190 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
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 |
| Immunohistochemistry (Paraffin) | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:50 |
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
For a carrier free (BSA and azide free) version of this product see product #49354.
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
There are four known JIPs, JIP1-4, of which JIP1 and JIP2 share extensive sequence homology and domain structure. JIP1 and JIP2 are mainly expressed in neurons, testis and in β pancreatic cells, where they have been implicated in cellular responses to metabolic stress, the development of diabetes, and post-traumatic brain damage (5-7). Although architecturally distinct from JIP1 and JIP2, JIP3 and JIP4 share some overlapping functions and are more broadly expressed. JIP4, encoded by the SPAG9 (sperm-associated antigen-9) gene, is a homooligomer that binds to and coordinates the activation of numerous components of the stress-activated kinase cascade including MEK4, MEKK3, p38α MAPK, and JNK1-3 (1,3). However, unlike the other JIP members, JIP4 does not appear to activate JNK directly, instead favoring stimulation of p38 MAPK signaling events in response to cellular stress (3,8).
In addition to mediating stress responses, JIP4 (or its splice variant, JLP) has also been shown to interact with ARF6 and PIKfyve, thus regulating microtubule-based endosomal trafficking (9,10). There are extensive reports indicating that JIP4 is phosphorylated in response to stress (UV damage etc.) but it is unclear what effect, if any, this has on its function, localization, or binding properties (11-14).
- Jagadish, N. et al. (2005) Biochem J 389, 73-82.
- Bouwmeester, T. et al. (2004) Nat Cell Biol 6, 97-105.
- Kelkar, N. et al. (2005) Mol Cell Biol 25, 2733-43.
- Hsu, C.H. et al. (2010) Neurodegener Dis 7, 68-75.
- Willoughby, E.A. et al. (2003) J Biol Chem 278, 10731-6.
- Koushika, S.P. (2008) Bioessays 30, 10-4.
- Beeler, N. et al. (2009) Brain Res Bull 80, 274-81.
- Brancho, D. et al. (2003) Genes Dev 17, 1969-78.
- Ikonomov, O.C. et al. (2009) J Biol Chem 284, 3750-61.
- Montagnac, G. et al. (2009) Curr Biol 19, 184-95.
- Olsen, J.V. et al. (2006) Cell 127, 635-48.
- Molina, H. et al. (2007) Proc Natl Acad Sci U S A 104, 2199-204.
- Matsuoka, S. et al. (2007) Science 316, 1160-6.
- Dephoure, N. et al. (2008) Proc Natl Acad Sci U S A 105, 10762-7.
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