|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rat, Non-human primate, Hamster, Human, Mouse, Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of mouse JAK2 that contains tyrosines 1007 and 1008.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 50% glycerol, 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Janus Activating Kinase 2 (JAK2) is one of a number of related tyrosine kinases involved in cytoplasmic signal transduction. In response to a varitety of cytokine or related factors (e.g., interferon, interleukins), JAKs are activated via phosphorylation at 2 adjacent tyrosine residues. The activation of JAKs can lead to the phosphorylation of STAT (signal transducers and activatiors of transcription) proteins, which dimerize and translocate to the nucleus. Once translocated to the nucleus, the STAT proteins can modify transcription of numerous genes, including interferon-stimulated genes. JAK2 is required for the IFN gamma-receptor complex initiation and JAK1 functions as an amplifier. However, active JAK1 may be required for complex responses. Some studies have suggested that the role of JAK2 might be performed by Tyk2 and JAK3, if they were positioned correctly within the IFN gamma-receptor complex.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
|Not Applicable||Not Cited||
Molecular basis for pseudokinase-dependent autoinhibition of JAK2 tyrosine kinase.
44-426G was used in western blot to propose a structural model for the autoinhibitory interaction between the JAK2 pseudokinase and kinase domains
|Shan Y,Gnanasambandan K,Ungureanu D,Kim ET,Hammar?n H,Yamashita K,Silvennoinen O,Shaw DE,Hubbard SR||Nature structural and molecular biology (21:579)||2014|
Urokinase-type plasminogen activator receptor signaling is critical in nasopharyngeal carcinoma cell growth and metastasis.
44-426G was used in western blot to show that uPAR regulates nasopharyngeal carcinoma NPC progression.
|Bao YN,Cao X,Luo DH,Sun R,Peng LX,Wang L,Yan YP,Zheng LS,Xie P,Cao Y,Liang YY,Zheng FJ,Huang BJ,Xiang YQ,Lv X,Chen QY,Chen MY,Huang PY,Guo L,Mai HQ,Guo X,Zeng YX,Qian CN||Cell cycle (Georgetown, Tex.) (13:1958)||2014|
Pharmacologic suppression of JAK1/2 by JAK1/2 inhibitor AZD1480 potently inhibits IL-6-induced experimental prostate cancer metastases formation.
44-426G was used in western blot to evaluate the effect of JAK1/2 inhibitor AZD1480 on IL-6-induced experimental prostate cancer metastases formation
|Gu L,Talati P,Vogiatzi P,Romero-Weaver AL,Abdulghani J,Liao Z,Leiby B,Hoang DT,Mirtti T,Alanen K,Zinda M,Huszar D,Nevalainen MT||Molecular cancer therapeutics (13:1246)||2014|
IL-21 and CD40L synergistically promote plasma cell differentiation through upregulation of Blimp-1 in human B cells.
44-426G was used in western blot to investigate plasma cell differentiation.
|Ding BB,Bi E,Chen H,Yu JJ,Ye BH||Journal of immunology (Baltimore, Md. : 1950) (190:1827)||2013|
IL-6 promotes head and neck tumor metastasis by inducing epithelial-mesenchymal transition via the JAK-STAT3-SNAIL signaling pathway.
44-426G was used in western blot to determine the function of IL-6 in the epithelial-mesenchymal transition in head and neck tumor cells.
|Yadav A,Kumar B,Datta J,Teknos TN,Kumar P||Molecular cancer research : MCR (9:1658)||2011|
|Not Applicable||Not Cited||
Erythropoietin prevents dialysis fluid-induced apoptosis of mesothelial cells.
44-426G was used in western blot to test if recombinant human erythropoietin treatment reduces peritoneal dialysis fluid-induced damage
|Vorobiov M,Malki M,Shnaider A,Basok A,Rogachev B,Lewis EC,Chaimovitz C,Zlotnik M,Douvdevani A||Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis (28:648)||2008|
|Human||Not Cited||Prolactin can modulate CD4+ T-cell response through receptor-mediated alterations in the expression of T-bet.||Tomio A,Schust DJ,Kawana K,Yasugi T,Kawana Y,Mahalingaiah S,Fujii T,Taketani Y||Immunology and cell biology (86:616)||2008|
|Human||Not Cited||Molecular mechanisms involved in interleukin-4-induced human neutrophils: expression and regulation of suppressor of cytokine signaling.||Ratthé C,Pelletier M,Chiasson S,Girard D||Journal of leukocyte biology (81:1287)||2007|
|Not Applicable||200 ng/ml||
Dampening of IFN-gamma-inducible gene expression in human choriocarcinoma cells is due to phosphatase-mediated inhibition of the JAK/STAT-1 pathway.
44-426G was used in western blot to investigate phosphatase-mediated suppression of IFN-gamma signaling in trophoblast cells
|Choi JC,Holtz R,Petroff MG,Alfaidy N,Murphy SP||Journal of immunology (Baltimore, Md. : 1950) (178:1598)||2007|
Erythropoietin induces sustained phosphorylation of STAT5 in primitive but not definitive erythrocytes generated from mouse embryonic stem cells.
44-426G was used in western blot to compare erythropoietin signaling between primitive erythroid cells and definitive erythroid cells.
|Tsuji-Takayama K,Otani T,Inoue T,Nakamura S,Motoda R,Kibata M,Orita K||Experimental hematology (34:1323)||2006|
|Non-human primate||Not Cited||G protein coupling and second messenger generation are indispensable for metalloprotease-dependent, heparin-binding epidermal growth factor shedding through angiotensin II type-1 receptor.||Mifune M,Ohtsu H,Suzuki H,Nakashima H,Brailoiu E,Dun NJ,Frank GD,Inagami T,Higashiyama S,Thomas WG,Eckhart AD,Dempsey PJ,Eguchi S||The Journal of biological chemistry (280:26592)||2005|
|Mechanism of protein tyrosine phosphatase 1B-mediated inhibition of leptin signalling.||Lund IK,Hansen JA,Andersen HS,Møller NP,Billestrup N||Journal of molecular endocrinology (34:339)||2005|
|Mouse||Not Cited||Role of tyrosine 441 of interferon-gamma receptor subunit 1 in SOCS-1-mediated attenuation of STAT1 activation.||Qing Y,Costa-Pereira AP,Watling D,Stark GR||The Journal of biological chemistry (280:1849)||2005|
|Rat||Not Cited||Falcarindiol impairs the expression of inducible nitric oxide synthase by abrogating the activation of IKK and JAK in rat primary astrocytes.||Shiao YJ,Lin YL,Sun YH,Chi CW,Chen CF,Wang CN||British journal of pharmacology (144:42)||2005|
|Human||Not Cited||Growth arrest of epithelial cells during measles virus infection is caused by upregulation of interferon regulatory factor 1.||Yokota S,Okabayashi T,Yokosawa N,Fujii N||Journal of virology (78:4591)||2004|
|Human||Not Cited||C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein.||Yokosawa N,Yokota S,Kubota T,Fujii N||Journal of virology (76:12683)||2002|
|Mouse||Not Cited||Protein tyrosine phosphatase 1B negatively regulates leptin signaling in a hypothalamic cell line.||Kaszubska W,Falls HD,Schaefer VG,Haasch D,Frost L,Hessler P,Kroeger PE,White DW,Jirousek MR,Trevillyan JM||Molecular and cellular endocrinology (195:109)||2002|
|Rat||Not Cited||Reactive oxygen species regulate heat-shock protein 70 via the JAK/STAT pathway.||Madamanchi NR,Li S,Patterson C,Runge MS||Arteriosclerosis, thrombosis, and vascular biology (21:321)||2001|
|Rat||Not Cited||Hyperglycemia enhances angiotensin II-induced janus-activated kinase/STAT signaling in vascular smooth muscle cells.||Amiri F,Venema VJ,Wang X,Ju H,Venema RC,Marrero MB||The Journal of biological chemistry (274:32382)||1999|
Distinct and gradient distributions of connexin26 and connexin30 in the cochlear sensory epithelium of guinea pigs.
44-426G was used in immunocytochemistry to study Cx26 and Cx30 in the cochlear sensory epithelium of guinea pigs.
|Zhao HB,Yu N||The Journal of comparative neurology (499:506)||2006|
||Hyperglycemia enhances angiotensin II-induced janus-activated kinase/STAT signaling in vascular smooth muscle cells.||Amiri F,Venema VJ,Wang X,Ju H,Venema RC,Marrero MB||The Journal of biological chemistry (274:32382)||1999|