R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Phospho-Jak2 (Ser523) (F8E8U) Rabbit mAb #15446
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 125 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-Jak2 (Ser523) (F8E8U) Rabbit mAb recognizes endogenous levels of Jak2 protein only when phosphorylated at Ser523.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser523 of human Jak2 protein.
Background
Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.
The JH2 domain of Jak2 has been shown to autophosphorylate two negative regulatory sites on Jak2, Ser523 and Tyr570. In the absence of cytokine stimulation, Jak2 is constitutively phosphorylated on Ser523, effectively inhibiting its activity (6,7). Mutation in the JH2 domain can lead to an increase in Jak2 activity, resulting in myeloproliferative neoplasms (MPNs) (8).
The JH2 domain of Jak2 has been shown to autophosphorylate two negative regulatory sites on Jak2, Ser523 and Tyr570. In the absence of cytokine stimulation, Jak2 is constitutively phosphorylated on Ser523, effectively inhibiting its activity (6,7). Mutation in the JH2 domain can lead to an increase in Jak2 activity, resulting in myeloproliferative neoplasms (MPNs) (8).
- Leonard, W.J. and O'Shea, J.J. (1998) Annu Rev Immunol 16, 293-322.
- Darnell, J.E. (1997) Science 277, 1630-5.
- VanderKuur, J. et al. (1995) J Biol Chem 270, 7587-93.
- Argetsinger, L.S. et al. (1995) J Biol Chem 270, 14685-92.
- Zhu, T. et al. (1998) J Biol Chem 273, 10682-9.
- Ishida-Takahashi, R. et al. (2006) Mol Cell Biol 26, 4063-73.
- Mazurkiewicz-Munoz, A.M. et al. (2006) Mol Cell Biol 26, 4052-62.
- Ungureanu, D. et al. (2011) Nat Struct Mol Biol 18, 971-6.
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