Recombinant Human Interferon-inducible double stranded RNA-dependent protein kinase activator A (PRKRA)

Code CSB-YP018717HU
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Source Yeast
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Code CSB-EP018717HU
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Source E.coli
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Code CSB-EP018717HU-B
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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.
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Code CSB-BP018717HU
MSDS
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Source Baculovirus
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Code CSB-MP018717HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PRKRA
Uniprot No.
Alternative Names
DYT16; HSD14; Interferon inducible double stranded RNA dependent protein kinase activator A; interferon-inducible double stranded RNA-dependent activator; Interferon-inducible double stranded RNA-dependent protein kinase activator A; PACT; PKR associated protein X; PKR associating protein X; PKR-associated protein X; PKR-associating protein X; PRKRA; PRKRA_HUMAN; Protein activator of the interferon induced protein kinase; Protein activator of the interferon-induced protein kinase; Protein kinase; Protein kinase interferon inducible double stranded RNA dependent activator; RAX
Species
Homo sapiens (Human)
Expression Region
1-313
Target Protein Sequence
MSQSRHRAEA PPLEREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP VYECERSDVQ IHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK ANASICFAVP DPLMPDPSKQ PKNQLNPIGS LQELAIHHGW RLPEYTLSQE GGPAHKREYT TICRLESFME TGKGASKKQA KRNAAEKFLA KFSNISPENH ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSIPNTD YIQLLSEIAK EQGFNITYLD IDELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH NALQYLKIIA ERK
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
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
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.

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Target Background

Function
Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner.
Gene References into Functions
  1. Low PACT expression is associated with Arenaviral infections. PMID: 29669840
  2. phenotype of our patients overlaps that of previouslyreported DYT16 patients PMID: 26990861
  3. this study shows that PACT is an essential coactivator of the MDA5-dependent type I IFN response to viral RNA PMID: 28760879
  4. High PRKRA mRNA expression is associated with colorectal cancer. PMID: 27859935
  5. It was established in this report that interactions between PACT, ADAR1 and HIV-1-encoded Tat protein diminish the activation of PKR in response to HIV-1 infection. PMID: 28167698
  6. 5 genomic variants in GSC, HOXA2 and PRKRA were identified through mutational analysis in Chinese patients with microtia. PMID: 28109504
  7. MicroRNA-122 Inhibits the Production of Inflammatory Cytokines by Targeting the PKR Activator PACT in Human Hepatic Stellate Cells. PMID: 26636761
  8. The interferon-induced protein kinase(PACT) partially rescued defects of interferon-beta1 and chemokine (C-C motif) ligand 5/RANTES (regulated on activation normal T cell expressed and secreted) induction in DDX3-knockdown HEK293 cells. PMID: 26454002
  9. These findings support a model in which a measles virus defective interfering RNA is sensed by PACT and RIG-I to initiate an innate antiviral response via activation of interferon-beta production. PMID: 26608320
  10. this study demonstrates for the first time that OV20.0 of Orf virus is also able to interact with the dsRNA binding domain of PACT and that the presence of dsRNA strengthened the interaction of these two molecules. PMID: 26355092
  11. the affinity of PACT-PACT and PACT-PKR interactions is enhanced in dystonia patient lymphoblasts, thereby leading to intensified PKR activation and enhanced cellular death. PMID: 26231208
  12. Altered PRKRA signalling and C / EBPbeta expression is associated with HLA-B27 expression in monocytic cells. PMID: 21988375
  13. This stuidy provides the first independent replication of the DYT16 locus at 2q31.2 and strongly confirms the causal contribution of the PRKRA gene to DYT16. Our data suggest worldwide involvement of PRKRA in dystonia. PMID: 25142429
  14. NS1 prevents PACT from interacting with an essential component of the virus. PMID: 24899174
  15. PKR is activated in uninfected cells, specifically during mitosis, by binding to dsRNAs formed by inverted Alu repeats (IRAlus). PMID: 24939934
  16. In contrast to its previously described activity, PACT contributes to PKR dephosphorylation during HIV-1 replication. PMID: 24020926
  17. MERS-CoV 4a protein interacted with PACT in an RNA-dependent manner but not with RIG-I or MDA5. PMID: 24522921
  18. Ebola virus VP35 inhibits PACT-induced RIG-I ATPase activity in a dose-dependent manner. PMID: 23870315
  19. Herpes simplex virus 1 Us11 suppresses host interferon beta1 production through the inhibition of the PACT. PMID: 24067967
  20. Protein kinase R modulates c-Fos and c-Jun signaling to promote proliferation of hepatocellular carcinoma with hepatitis C virus infection. PMID: 23844083
  21. in vitro binding patterns of human TRBP and PACT to siRNA PMID: 23658827
  22. The results show that PACT and TRBP have distinct effects on Dicer-mediated dsRNA processing. PMID: 23661684
  23. RISC proteins PACT, TRBP, and Dicer, together with PKR, are steroid receptor RNA activator-binding nuclear receptor coregulators that are recruited to the promoters of hormone-regulated genes and regulate the expression of downstream target genes. PMID: 23550157
  24. PACT may be associated with the plasma cell function and eosinophilic inflammation in CRSwNP. PMID: 22961479
  25. DGCR8, AGO1, AGO2, PACT, and TARBP1 expression levels were significantly higher in the epithelial skin cancer groups than the healthy controls (P > 0.05). PMID: 22025453
  26. The PACT-protein kinase PKR pathway represents a potential link between Abeta accumulation, PKR activation and tau phosphorylation. PMID: 21790829
  27. Data demonstrate that PACT-PACT interaction is essential for efficient PKR activation. PMID: 22473766
  28. NF-kappa-B is involved in the protein activator of PKR-RNA-dependent protein kinase interaction and the production of pro-inflammatory cytokines in periodontitis. PMID: 21882225
  29. show that PACT physically binds to the C-terminal repression domain of RIG-I and potently stimulates RIG-I-induced type I interferon production PMID: 21501829
  30. though mutation analysis demonstrated no mutation of PACT in the patients of microtia in the present study, suggest that PACT may play an essential role in mammalian ear development PMID: 21595004
  31. results demonstrate for the first time that stress-induced PACT phosphorylation functions to free PACT from the inhibitory interaction with TRBP and also to enhance its interaction with PKR PMID: 21526770
  32. The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase PMID: 11985496
  33. Us11 protein of herpes simplex virus type 1 can block PKR activation by PACT both in vitro and in vivo PMID: 12368348
  34. RAX, the cellular activator of PKR, has a novel role in synergistically stimulating SV40 large T antigen-dependent gene expression PMID: 12874289
  35. The interaction with Dicer involves the third dsRNA-binding domain (dsRBD) of PACT and the N-terminal region of Dicer containing the helicase motif. Like TRBP, PACT is not required for the pre-microRNA (miRNA) cleavage reaction step. PMID: 16424907
  36. RAX (PRKRA) may function as a negative regulator of growth that is required to activate PKR in response to a broad range of apoptosis-inducing stress. PMID: 16861340
  37. The underlying biochemical mechanism of the activation of PKR via PACT phosphorylation at specific activation domain residues is reported as the major mode of transmission of cellular stress response to PKR. PMID: 16982605
  38. Results show that PACT is expressed ubiquitously in different cell types at varying abundance, and Sp1 is the major transcription factor responsible for PACT promoter activity. PMID: 17125937
  39. Results indicate that human TRBP and PACT directly interact with each other and associate with Dicer to stimulate the cleavage of double-stranded or short hairpin RNA to siRNA. PMID: 17452327
  40. DYT16, a novel young-onset dystonia-parkinsonism disorder, identification of a segregating mutation in the stress-response protein PRKRA. PMID: 18243799
  41. A heterozygous frameshift mutation in PRKRA (DYT16) associated with generalised dystonia in a German patient. PMID: 18420150
  42. TRBP controls PACT activation of PKR, an activity that is reversed by stress. PMID: 18936160
  43. writer's cramp as presenting symptom is not associated with mutations in DYT11, DYT16, but it can be the sole manifestation of DYT1 GAG deletion mutation carriers. PMID: 19441135
  44. Strong protein kinase R (PKR) binding is needed for PACT-mediated PKR activation and phosphorylation in vivo. PMID: 19580324
  45. RAX phosphorylation is required for PKR activation, full protein synthesis inhibition, and rapid apoptosis following stress. PMID: 15299031

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Involvement in disease
Dystonia 16 (DYT16)
Subcellular Location
Cytoplasm, perinuclear region. Cytoplasm.
Protein Families
PRKRA family
Database Links

HGNC: 9438

OMIM: 603424

KEGG: hsa:8575

STRING: 9606.ENSP00000318176

UniGene: Hs.570274

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