Protein Kinase R (PKR) Recombinant Protein | PKR recombinant protein

Recombinant Protein Kinase R (PKR)

Cat. Num. AAA2011180

• Gene Names: Eif2ak2; Pkr; Prkr
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Protein Kinase R (PKR); Recombinant Protein Kinase R (PKR); PKR recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with two N-terminal Tags, His-tag and T7-tag, its sequence is listed below.; MGSSHHHHHH SSGLVPRGSH MASMTGGQQM GRGS- QA LAELNHANIV QYRVCWEGED YDYDPENSTN GDTSRYKTRC LFIQMEFCDK GTLQQWLEKR NRSQEDKALV LELFEQIVTG VDYIHSKGLI HRDLKPGNIF LVDEKHIKIG DFGLATALEN DGNPRTKYTG TPQYMSPEQK SSLVEYGKEV DIFALGLILA ELLHICKTDS EKIEFFQLLR NGIFSDDIFD NKEKSLLQKL LSSKPRERPN TSEILKTLAE WKNISE
• Sequence Length: 513

• Applicable Applications for PKR recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Rattus norvegicus (Rat)
• Expression System: Prokaryotic expression
• Residues: Gln279~Glu506 (Accession # Q63184) with two N-terminal Tags, His-tag and T7-tag
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-Page

NCBI and Uniprot Product Information

• NCBI GI #: 9506993
• NCBI GeneID: 54287
• NCBI Accession #: NP_062208.1
• NCBI GenBank Nucleotide #: NM_019335.1
• UniProt Accession #: Q63184
• Molecular Weight: 29.9kDa
• NCBI Official Full Name: interferon-induced, double-stranded RNA-activated protein kinase
• NCBI Official Synonym Full Names: eukaryotic translation initiation factor 2-alpha kinase 2
• NCBI Official Symbol: Eif2ak2
• NCBI Official Synonym Symbols: Pkr; Prkr
• NCBI Protein Information: interferon-induced, double-stranded RNA-activated protein kinase; eIF-2A protein kinase 2; protein kinase RNA-activated; tyrosine-protein kinase EIF2AK2; interferon-inducible RNA-dependent protein kinase; Protein kinase, interferon-inducible double stranded RNA dependent
• UniProt Protein Name: Interferon-induced, double-stranded RNA-activated protein kinase
• UniProt Gene Name: Eif2ak2
• UniProt Synonym Gene Names: Prkr; eIF-2A protein kinase 2; PKR
• UniProt Entry Name: E2AK2_RAT

NCBI Description

double-stranded RNA dependent eukaryotic initiation factor 2-kinase [RGD, Feb 2006]

Uniprot Description

Function: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. 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). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also 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. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. Regulates proliferation, differentiation and survival of hematopoietic stem/progenitor cells and induction of cytokines and chemokines

By similarity. Plays a role in cortex-dependent memory consolidation. Ref.3

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation: Initially produced in an inactive form and is activated by binding to viral dsRNA, which causes dimerization and autophosphorylation in the activation loop and stimulation of function. ISGylation can activate it in the absence of viral infection. Can also be activated by heparin, proinflammatory stimuli, growth factors, cytokines, oxidative stress and the cellular protein PRKRA. Activity is markedly stimulated by manganese ions. Activation is blocked by the cellular proteins TARBP2, DUS2L, NPM1, NCK1 and ADAR

By similarity.

Subunit structure: Homodimer

By similarity. Interacts with DNAJC3

By similarity. Interacts with STRBP. Forms a complex with FANCA, FANCC, FANCG and HSP70

By similarity. Interacts with ADAR/ADAR1

By similarity. The inactive form interacts with NCK1 and GSN. Interacts (via the kinase catalytic domain) with STAT3 (via SH2 domain), TRAF2 (C-terminus), TRAF5 (C-terminus) and TRAF6 (C-terminus). Interacts with MAP2K6, IKBKB/IKKB, IRS1, NPM1, TARBP2, NLRP1, NLRP3, NLRC4 and AIM2. Interacts (via DRBM 1 domain) with DUS2L (via DRBM domain). Interacts with DHX9 (via N-terminus) and this interaction is dependent upon activation of the kinase

By similarity. Ref.2

Subcellular location: Cytoplasm

By similarity. Nucleus

By similarity. Cytoplasm › perinuclear region

By similarity.

Induction: By type I interferons

By similarity.

Post-translational modification: Autophosphorylated on several Ser, Thr and Tyr residues. Autophosphorylation of Thr-411 is dependent on Thr-406 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase. Tyrosine autophosphorylation is essential for efficient dsRNA-binding, dimerization, and kinase activation

By similarity.

Sequence similarities: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.Contains 2 DRBM (double-stranded RNA-binding) domains.Contains 1 protein kinase domain.