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RABBIT ANTI NAK (C-TERMINAL)

ArtNr 18-783-313821
Hersteller GENWAY
Menge 0.05 mg
Kategorie
Typ Antibody
Applikationen WB
Specific against other
Host Rabbit
ECLASS 10.1 32160702
ECLASS 11.0 32160702
UNSPSC 12352203
Alias GWB-B74148
Similar products 18-783-313821
Lieferbar
Genway ID:
GWB-B74148
Specificity:
NAK (C-TERMINAL)
Isotype:
Polyclonal IgGSpecies Cross Reactivity: Reacts with: Mouse RatN. B. Antibody reactivity and working conditions may vary between species.
Buffer Solution:
Phosphate buffered saline
Preservative Stabilisers:
0. 02% Sodium Azide (NaN3)Approx. Protein Concentrations: IgG concentration 1. 0mg/ml
Immunogen:
A peptide corresponding to 17 amino acids near the carboxy terminus of human NAK.
Specificity:
Recognises human NF-kB-activating kinase (NAK) otherwise known as TANK-binding kinase 1 (TBK1). It is involved in the signalling cascade of NF-kB activation by directly phosphorylating and activating IKK Beta. It also mediates the production of IFN Beta and CCL5 and plays a key role in the innate immune response. In addition it phosphorylates and activates the interferon regulatory factors -3 and -7 eventually leading to the development of a cellular antiviral state. It may also be involved in the induction of the antiviral interferon response. NAK is expressed ubiquitously with higher expression in testis.
Specificity:
Does not cross-react with IKK Alpha IKK Beta IKK Gamma or IKK Epsilon. Recommended Secondary Antibodies: Sheep Anti Rabbit IgGGoat Anti Rabbit IgG (Fc)Goat Anti Rabbit IgG (H/L)
Function:
Serine/threonine protein involved in the signaling cascade converging to the activation of the transcription factor NF-kappa-B. May function as an IKK kinase playing an essential role in the transcription of a subset of TNF-alpha-induced genes. Also mediates production of RANTES/CCL5 and interferon-beta/IFNB1. Has a pivotal role in the innate immune response. Phosphorylates Borna disease virus (BDV) P protein. Phosphorylates and activates IRF3 and IRF7 and allows their nuclear localization. This leads to production of alpha/beta interferons and the development of a cellular antiviral state. It also seems to be a central factor in the induction of the antiviral interferon response. Inhibition of its interaction with IRF3 due to HCV NS3 binding or BDV P protein seems to be one mechanism of inhibition of the innate immune responses of hepatitis C virus (HCV) infection or Borna disease virus infection respectively. Ref. 1Ref. 2Ref. 6Ref. 8Ref. 9Ref. 12Catalytic activityATP + a protein = ADP + a phosphoprotein. Subunit structureInteracts with TIRAP TANK and TRAF2. Part of a ternary complex consisting of TANK TRAF2 and TBK1. Interacts with AZI2. Interacts with SIKE1. Interacts with TICAM1/TRIF IRF3 and DDX58/RIG-I interactions are disrupted by the interaction between TBK1 and SIKE1. Interacts with CYLD. Interacts with HCV NS3 a hepatitis C virus protein and with BDV P protein a Borna disease virus protein. Ref. 1Ref. 7Ref. 10Ref. 11Ref. 13Ref. 14Ref. 15Ref. 16Subcellular locationCytoplasmRef. 12. Tissue specificityUbiquitous with higher expression in testis. Ref. 2Sequence similaritiesBelongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily. Contains 1 protein kinase domain. Sequence cautionThe sequence BAA92129. 1 differs from that shown. Reason: Erroneous initiation. 1. Southern J. A. et al. (1991) Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics. J. Gen. Virol. 72: 1551-1557. 2. Hanke T. et al. (1992) Construction of solid matrix-antibody-antigen complexes containing simian immunodeficiency virus p27 using tag-specific monoclonal antibody and tag-linked antigen. J. Gen. Virol. 73: 653-660. 3. Randall R. E. et al. (1993) Two-tag purification of recombinant proteins for the construction of solid matrix-antibody antigen (SMAA) complexes as vaccines. Vaccine 11:1247-1252. 4. Randall R. E. et al. (1994) Purification of antibody-antigen complexes containing recombinant SIV proteins; comparison of antigen and antibody-antigen complexes for immune priming. Vaccine 12: 351-358. 5. Hanke T. et al. (1995) Attachment of an oligopeptide epitope to the C-terminus of recombinant SIV gp160 facilitates the construction of SMAA complexes while preserving CD4 binding J. Virol. Methods 149-156. 6. Jaffray E. et al. (1995) Domain organization of I kappa B alpha and sites of interaction with NF-kappa B p65 Mol. Cell. Biol. 15: 2166-2172. 7. Rodriguez M. S. et al. (1995) Inducible degradation of I kappa B alpha in vitro and in vivo requires the acidic C-terminal domain of the protein. Mol. Cell. Biol. 15: 2413-2419. 8. Arenzana-Seisdedos F. et al. (1995) Inducible nuclear expression of newly synthesised IkBa negatively regulates DNA binding and transcriptional activities of NF-kB. Mol. Cell. Biol. 15: 2689-2696. 9. Hirst K. et al. (1994) The transcription factor the Cdk its cyclin and their regulator: directing the transcriptional response to a nutritional signal EMBO J. 13: 5410-5420. 10. Dunn C. et al. (1999) Fine mapping of the binding sites of monoclonal antibodies raised against the Pk tag. J. Immunol. Methods. 224: 141-150. 11. Young D. F. et al. (2001) Single amino acid substitution in the V protein of simian virus 5 differentiates its ability to block interferon signaling in human and murine cells J. Virol. 75 (7): 3363 - 3370. 12. Stuart A. MacNeill (2004) The C-terminal zinc finger of the catalytic subunit of DNA polymerase {delta} is responsible for direct interaction with the B-subunit Nucleic Acids Research 32: 3005-3016 [1] \" Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the paramyxovirus SV5. \" Thomas S. M. Lamb R. A. Paterson R. G. Cell 54:891-902(1988) [PubMed: 3044614] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] RNA EDITING. [2] \" NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined using a novel protein:protein capture assay. \" Randall R. E. Bermingham A. Virology 224:121-129(1996) [PubMed: 8862406] [Abstract]Cited for: INTERACTION WITH PROTEIN NP. [3] \" The RNA binding region of the paramyxovirus SV5 V and P proteins. \" Lin G. Y. Paterson R. G. Lamb R. A. Virology 238:460-469(1997) [PubMed: 9400618] [Abstract]Cited for: RNA-BINDING. [4] \" The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase mda-5 and inhibit its activation of the IFN-beta promoter. \" Andrejeva J. Childs K. S. Young D. F. Carlos T. S. Stock N. Goodbourn S. Randall R. E. Proc. Natl. Acad. Sci. U. S. A. 101:17264-17269(2004) [PubMed: 15563593] [Abstract]Cited for: INTERACTION WITH HUMAN IFIH1/MDA5 INTERFERON EVASION. [5] \" In vitro and in vivo specificity of ubiquitination and degradation of STAT1 and STAT2 by the V proteins of the paramyxoviruses simian virus 5 and human parainfluenza virus type 2. \" Precious B. Young D. F. Andrejeva L. Goodbourn S. Randall R. E. J. Gen. Virol. 86:151-158(2005) [PubMed: 15604442] [Abstract]Cited for: UBIQUITINATION OF HUMAN STAT1 AND HUMAN STAT2. [6] \" The role of simian virus 5 V protein on viral RNA synthesis. \" Lin Y. Horvath F. Aligo J. A. Wilson R. He B. Virology 338:270-280(2005) [PubMed: 15950997] [Abstract]Cited for: FUNCTION. [7] \" Simian virus 5 V protein acts as an adaptor linking DDB1 to STAT2 to facilitate the ubiquitination of STAT1. \" Precious B. Childs K. Fitzpatrick-Swallow V. Goodbourn S. Randall R. E. J. Virol. 79:13434-13441(2005) [PubMed: 16227264] [Abstract]Cited for: INTERACTION WITH HUMAN DDB1 AND HUMAN STAT2. [8] \" Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase. \" Li T. Chen X. Garbutt K. C. Zhou P. Zheng N. Cell 124:105-117(2006) [PubMed: 16413485] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2. 85 ANGSTROMS) OF 1-222.

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