research use only
Cat.No.: F4153
| Dilution |
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| Application |
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| WB |
| Reactivity |
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| Human, Mouse, Rat |
| Source |
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| Rabbit Monoclonal Antibody |
| Storage Buffer |
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| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
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| -20°C (avoid freeze-thaw cycles), 2 years |
| Predicted MW |
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| 125 kDa |
| Specificity |
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| Phospho-Jak2 (Tyr1007/1008) Antibody [L12G1] detects endogenous levels of total Jak2 protein only when it is phosphorylated at Tyr1007/1008. |
| Clone |
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| L12G1 |
| Synonym(s) |
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| Tyrosine-protein kinase JAK2; Janus kinase 2 (JAK-2); JAK2 |
| Background |
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| Phospho-Jak2 (Tyr1007/1008) represents the critical activation loop phosphorylation within the Janus kinase 2 (Jak2), a non-receptor tyrosine kinase of the Jak family that associates constitutively with cytokine receptors spanning class I and type II families to transduce signals for hematopoiesis, immune regulation, and growth. Jak2 comprises FERM, SH2, and pseudokinase (JH2) domains that maintain autoinhibition until ligand-induced dimerization, with the Tyr1007/1008 motif in the JH1 kinase domain undergoing trans-autophosphorylation to unlock catalytic competency. Ligand binding, such as erythropoietin to EPOR or interferon-γ to IFNGR, clusters receptors, relieving JH2 inhibition and enabling sequential Tyr1007/1008 phosphorylation that amplifies Jak2 activity over 100-fold, recruiting SH2-domain proteins like STAT1/3/5 for tyrosine phosphorylation, dimerization, and nuclear translocation to drive transcription of target genes including SOCS feedback inhibitors, IRF1, and BCL-XL. This cascades through the Jak2-STAT axis with PI3K-Akt and MAPK branches via receptor docking sites, while negative regulation by PTPN6/SHP1 dephosphorylates the loop and SOCS3 binds phosphorylated Tyr221 to attenuate signaling duration. Phospho-Tyr1007/1008 governs erythroid maturation, Th1 differentiation, and megakaryocyte development, positioning it as a direct pharmacodynamic marker for researchers assessing cytokine pathway fidelity in primary hematopoietic cultures or dissecting hypersensitivity in CRISPR-edited cell lines. Dysregulation through the V617F mutation causes constitutive activation in myeloproliferative neoplasms like polycythemia vera. |
| References |
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