Recombinant Mouse Interferon-induced, double-stranded RNA-activated protein kinase(Eif2ak2)

Code CSB-YP007511MO
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP007511MO
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP007511MO-B
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP007511MO
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP007511MO
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity >85% (SDS-PAGE)
Target Names Eif2ak2
Uniprot No. Q03963
Alternative Names Eif2ak2; Pkr; Prkr; TikInterferon-induced; double-stranded RNA-activated protein kinase; EC 2.7.11.1; Eukaryotic translation initiation factor 2-alpha kinase 2; eIF-2A protein kinase 2; Interferon-inducible RNA-dependent protein kinase; P1/eIF-2A protein kinase; Protein kinase RNA-activated; PKR; Protein kinase R; Serine/threonine-protein kinase TIK; Tyrosine-protein kinase EIF2AK2; EC 2.7.10.2; p68 kinase
Species Mus musculus (Mouse)
Expression Region 2-515
Target Protein Sequence ASDTPGFYM DKLNKYRQMH GVAITYKELS TSGPPHDRRF TFQVLIDEKE FPEAKGRSKQ EARNAAAKLA VDILDNENKV DCHTSASEQG LFVGNYIGLV NSFAQKKKLS VNYEQCEPNS ELPQRFICKC KIGQTMYGTG SGVTKQEAKQ LAAKEAYQKL LKSPPKTAGT SSSVVTSTFS GFSSSSSMTS NGVSQSAPGS FSSENVFTNG LGENKRKSGV KVSPDDVQRN KYTLDARFNS DFEDIEEIGL GGFGQVFKAK HRIDGKRYAI KRVKYNTEKA EHEVQALAEL NHVNIVQYHS CWEGVDYDPE HSMSDTSRYK TRCLFIQMEF CDKGTLEQWM RNRNQSKVDK ALILDLYEQI VTGVEYIHSK GLIHRDLKPG NIFLVDERHI KIGDFGLATA LENDGKSRTR RTGTLQYMSP EQLFLKHYGK EVDIFALGLI LAELLHTCFT ESEKIKFFES LRKGDFSNDI FDNKEKSLLK KLLSEKPKDR PETSEILKTL AEWRNISEKK KRNTC
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection. Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4. Exerts its antiviral activity on a wide range of DNA and RNA viruses including west nile virus (WNV), sindbis virus (SV), foot-and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic choriomeningitis virus (LCMV). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, and IRS1. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin.
Gene References into Functions
  1. The mutant Rift Valley fever virus-C39S/C40S showed an attenuated phenotype in mice. The results show that two mechanisms are responsible for the attenuation; (1) loss of the interferon antagonistic propriety characteristic of the wild-type NSs and (2) the inability of the attenuated mutant to degrade Proteine Kinase R (PKR). PMID: 29530722
  2. Pharmacological inhibition of the PKM2-EIF2AK2 pathway protects mice from lethal endotoxemia and polymicrobial sepsis. Conditional knockout of PKM2 in myeloid cells protects mice from septic death induced by NLRP3 and AIM2 inflammasome activation. PMID: 27779186
  3. heme-regulated inhibitor (HRI), protein kinase R (PKR), PKR-like endoplasmic reticulum kinase, (PERK) and general control non-depressible 2 (GCN2) are sufficient for the integrated stress response; there are no additional eIF2alpha kinases in vertebrates PMID: 27633668
  4. PKR inhibition ameliorated LPS-induced lung inflammation. PMID: 28511573
  5. PKR activation is an essential part of the molecular switch from adaptation to inflammation in response to hyperosmotic stress. PMID: 27920257
  6. We therefore concluded that in osteoblasts, P. gingivalis activated PKR, which in turn increased NLRP3 expression by activating NF-kappaB. Our results suggest that PKR modulates inflammation by regulating the expression of the NLRP3 inflammasome through the NF-kappaB pathway in periodontal diseases. PMID: 28341446
  7. The data predicts that PKR diminishes inflammasome activity by controlling protein translation to repress the induction of factors that are critical for the activity of the cryopyrin inflammasome. PMID: 26794869
  8. This study provides insight into the molecular pathology of Cornelia de Lange syndrome by establishing a relationship between NIPBL and HDAC8 mutations and PKR activation. PMID: 26725122
  9. Deletion of PKR does not affect HFD-induced obesity, hepatic steatosis or glucose metabolism, and only modestly affects adipose tissue inflammation. PMID: 26838266
  10. results show that ceramide acts at two distinct levels of the insulin signaling pathway (IRS1 and Akt). PKR, which is induced by both inflammation signals and ceramide, could play a major role in the development of insulin resistance in muscle cells. PMID: 26698173
  11. Data (including data from studies in transgenic/knockout mice) suggest that PACT/RAX (protein activator of protein kinase R) functions as negative regulator of PKR/Eif2ak2 (protein kinase R) in development of postnatal anterior pituitary tissue. PMID: 26414443
  12. Data indicate increasing expression of PKR during TNF-a-induced osteoclast formation. Its inhibition prevents TNF-a-induced bone destruction in vivo and can be then considered as new therapeutic target for bone disease. PMID: 25739386
  13. The authors show that Murine cytomegalovirus m142 and m143 knockout mutants attain organ titers equivalent to those attained by wild-type virus in Pkr knockout mice. PMID: 26512090
  14. these data indicate a pivotal role for PKR's protein-binding function on the proliferation of pancreatic beta cells through TRAF2/RIP1/NF-kappaB/c-Myc pathways. PMID: 25715336
  15. Activated PKR inhibits pancreatic beta-cell proliferation through sumoylation-dependent stabilization of P53. PMID: 26446704
  16. These data indicate that the association between PKR and TRBP integrates metabolism with translational control and inflammatory signaling and plays important roles in metabolic homeostasis and disease. PMID: 25843719
  17. The age-associated accumulation of somatic mutations that occurs in the Nup98-HOXD13 (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR transgene. PMID: 26202421
  18. these findings demonstrate that PKR plays a major role in brain changes induced by LPS and could be a valid target to modulate neuroinflammation and Abeta production. PMID: 25687824
  19. Thiamine deficiency activates the PKR-eIF2alpha pathway, increases the BACE1 expression levels of amyloid beta in specific thalamus nuclei and induces motor deficits and neurodegeneration. PMID: 25590804
  20. These results suggest an unprecedented and unexpected model whereby snoRNAs play a role in the activation of PKR under metabolic stress. PMID: 25848059
  21. PKR mediates angiogenesis through a VEGF pathway, which may form the basis for future intervention of Peripheral artery disease. PMID: 25587101
  22. PKR is a maladaptive factor upregulated in hemodynamic overload that contributes to myocardial inflammation, cardiomyocyte apoptosis, and the development of congestive heart failure. PMID: 24463368
  23. The results demonstrate the ability of PKR to balance neuroinflammation by selectively modulating key cytokines and chemokines in CNS resident and CD4 T cells. PMID: 24642385
  24. miR-29b mediated ethanol neurotoxicity through the SP1/RAX/PKR cascade. PMID: 24554719
  25. PKR-induced translational inhibition appears to be specific to Dcp1a because the expression of other P-body components, Pan2, Pan3, Ccr4, or Caf1, did not result in the inhibition of poliovirus gene expression or induce eIF2alpha phosphorylation. PMID: 24382890
  26. findings identified PKR as a mediator of anti-microbial activity and promoter of protection against disease caused by a non-viral pathogen, revealed that PKR is activated by CD40 via TRAF6 and TRAF2 PMID: 23990781
  27. Local control of protein synthesis at synapses is crucial for synaptic plasticity, memory formation and learning processes. PMID: 23418065
  28. PKR has important functions in the differentiation of chondrocytes. PMID: 23180319
  29. Activation of double-stranded RNA-activated protein kinase (PKR) by interferon-stimulated gene 15 (ISG15) modification down-regulates protein translation PMID: 23229543
  30. Data show that protein kinase R as the principal kinase that mediates eukaryotic initiation factor 2alpha (eIF2alpha) phosphorylation by large RasGAP SH3-binding protein (G3BP)-induced granules. PMID: 22833567
  31. Report mechanism of autophagy control that involves STAT3 and PKR as interacting partners. PMID: 23084476
  32. PKR may have a role in insulin sensitivity under normal physiological conditions and may represent a central mechanism for the integration of pathogen response and innate immunity with insulin action and metabolic pathways that are critical in obesity. PMID: 22948222
  33. PKR positively regulates the differentiation of osteoblasts by mediating GSK-3beta activity through a beta-catenin-independent pathway. PMID: 22484461
  34. Japanese encephalitis virus nonstructural protein 2A blocks double-stranded RNA-activated protein kinase PKR PMID: 22787234
  35. results show a crucial role for PKR in inflammasome activation, and indicate that it should be possible to pharmacologically target this molecule to treat inflammation PMID: 22801494
  36. Heme-regulated eIF2alpha kinase activated Atf4 signaling pathway in oxidative stress and erythropoiesis. PMID: 22498744
  37. The authors demonstrate for the first time that upon CD40 ligation, PKR is rapidly phosphorylated and activated, indicating that PKR is an early and novel downstream mediator of CD40 signaling pathways. PMID: 21994357
  38. Loss of PKR increases the late phase of long-lasting synaptic potentiation (L-LTP) in hippocampal slices. These effects are caused by an IFN-gamma-mediated selective reduction in GABAergic synaptic action. PMID: 22153080
  39. PKR is not activated by the West Nile virus dsRNA in infected cells. PMID: 21982595
  40. Data show that PKR inhibition prevented Abeta42-induced activation of IkappaB and NF-kappaB, strongly decreased production and release of tumor necrosis factor (TNFalpha) and interleukin (IL)-1beta, and limited apoptosis. PMID: 21699726
  41. sunitinib treatments prevent antiviral innate immune responses mediated by RNase L and PKR. PMID: 21636578
  42. A critical role of PKR in regulating virus-host interaction. PMID: 21311764
  43. In endotoxin tolerance, the kinetics of the differential ubiquitination of PKR is altered, resulting in a predominance of K48-linked chains, concomitant with a loss of PKR activation. PMID: 20978539
  44. These findings reveal that activation of the antiviral response by rotavirus is dependent on MAVS/IPS-1 and IRF3 and involves both RIG-I and MDA-5 and that IFN-beta secretion during rotavirus infection is regulated by PKR. PMID: 21307186
  45. Hyperoxia increases CHOP expression via an endoplasmic reticulum stress-independent, PKR-dependent pathway and that increased CHOP expression protects against hyperoxia-induced lung injury. PMID: 21186267
  46. The eIF2alpha kinases PKR and GCN2 promote apoptosis. PMID: 21076179
  47. Activation of the dsRNA-activated protein kinase PKR by viral RNA enabled phosphorylation of NFAR1 and NFAR2 on Thr 188 and Thr 315 PMID: 21123651
  48. PKR plays important roles in the differentiation of osteoclasts. PMID: 20728438
  49. These data suggest that PKR is a signaling molecule for immune responses during Respiratory syncytial virus infections. PMID: 20038207
  50. Taken together, PKR and Hck were critical for DON-induced ribosomal recruitment of p38, its subsequent phosphorylation, and, ultimately, p38-driven proinflammatory cytokine expression. PMID: 20181660

Show More

Hide All

Subcellular Location Cytoplasm. Nucleus. Cytoplasm, perinuclear region.
Protein Families Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily
Tissue Specificity Expressed in heart, lung, brain, kidney, testes, thymus and bone marrow.
Database Links

KEGG: mmu:19106

STRING: 10090.ENSMUSP00000024884

UniGene: Mm.378990

Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
Address
7505 Fannin St. Ste 610-312, Houston, TX 77054, USA
Join Us with

Subscribe newsletter

Leave a message

© 2007-2022 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1