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Recombinant human NAK/TBK1 protein (Active) is a Human Full Length protein, in the 2 to 729 aa range, expressed in Baculovirus infected Sf9, with >=90% purity and suitable for SDS-PAGE, FuncS.

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Images

SDS-PAGE - Recombinant human NAK/TBK1 protein (Active) (AB271752), expandable thumbnail
  • Functional Studies - Recombinant human NAK/TBK1 protein (Active) (AB271752), expandable thumbnail

Key facts

Purity

>=90% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE, FuncS

Biologically active

Yes

Reactivity data

Application

SDS-PAGE

Reactivity

Reacts

Dilution info

-

Notes

-

Application

FuncS

Reactivity

Reacts

Dilution info

-

Notes

-

Target data

Function

Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Phosphorylates and activates AKT1 (PubMed:21464307). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595). Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR (PubMed:29150432, PubMed:31530866). Involved in the regulation of TNF-induced RIPK1-mediated cell death, probably acting via CYLD phosphorylation that in turn controls RIPK1 ubiquitination status (PubMed:34363755). Participates also in the differentiation of T follicular regulatory cells together with the receptor ICOS (PubMed:27135603).

Alternative names

Recommended products

Recombinant human NAK/TBK1 protein (Active) is a Human Full Length protein, in the 2 to 729 aa range, expressed in Baculovirus infected Sf9, with >=90% purity and suitable for SDS-PAGE, FuncS.

Key facts

Purity

>=90% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Applications

SDS-PAGE, FuncS

Biological activity

Specific activity: 80 pmol/min/μg.

Accession
Q9UHD2-1
Animal free

No

Species

Human

Concentration
Loading...
Storage buffer

pH: 7.5
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.27% Glutathione, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride

Sequence info

Amino acid sequence

Accession

Q9UHD2

Protein length

Full Length

Predicted molecular weight

105 kDa

Amino acids

2 to 729

Nature

Recombinant

Tags

GST tag N-Terminus

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Phosphorylates and activates AKT1 (PubMed:21464307). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595). Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR (PubMed:29150432, PubMed:31530866). Involved in the regulation of TNF-induced RIPK1-mediated cell death, probably acting via CYLD phosphorylation that in turn controls RIPK1 ubiquitination status (PubMed:34363755). Participates also in the differentiation of T follicular regulatory cells together with the receptor ICOS (PubMed:27135603).

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.

Post-translational modifications

Autophosphorylation at Ser-172 activates the kinase, and is an essential step for virus-triggered signaling. Phosphorylated by IKBKB/IKKB at Ser-172. Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401. Dephosphorylated at Ser-172 by PPM1B and this negatively regulates its role in mediating antiviral response.

Storage

Shipped at conditions

Dry Ice

Appropriate short-term storage conditions

-80°C

Appropriate long-term storage conditions

-80°C

Storage information

Avoid freeze / thaw cycle

This product is an active protein and may elicit a biological response in vivo, handle with caution.

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The NAK/TBK1 also known as TANK-binding kinase 1 is a fundamental protein kinase in various cellular processes. It weighs approximately 84 kDa and is expressed in many tissues including lymphoid organs and the brain. NAK acts as a serine/threonine-protein kinase which transfers a phosphate group to specific substrates modulating their function and activity. Phosphorylation by TBK1 initiates several signaling events making it an important regulator in immune responses and inflammatory signaling pathways.

Biological function summary

This kinase plays a significant role in antiviral defense and autophagy. NAK/TBK1 is also involved in innate immune signaling and cell survival. TBK1 forms part of a larger signaling complex interacting with adaptors like TRAF3 and TANK which are important for its proper localization and function. Phospho-NAK its phosphorylated form can activate other molecules driving various downstream immune and stress responses.

Pathways

The protein is integral to the type I interferon signaling pathway and NF-kB pathway. NAK/TBK1 interacts closely with IRF3 a transcription factor important for antiviral activity and plays a role alongside other proteins like IKKε. These interactions permit activation of genes necessary for defense mechanisms against viral pathogens and control of inflammation. In the NF-kB pathway TBK1 helps regulate cellular responses to stress and inflammatory signals.

Associated diseases and disorders

NAK/TBK1 has associations with amyotrophic lateral sclerosis (ALS) and various cancers. Research shows connections between TBK1 mutations and ALS indicating its importance in neuronal function and health. Additionally aberrations in TBK1 activity contribute to oncogenesis as it can affect cell proliferation and survival. The protein's relation with signaling proteins such as p62/SQSTM1 highlights its diverse role in disease mechanisms making it a potential therapeutic target.

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2 product images

  • SDS-PAGE - Recombinant human NAK/TBK1 protein (Active) (ab271752), expandable thumbnail

    SDS-PAGE - Recombinant human NAK/TBK1 protein (Active) (ab271752)

    SDS-PAGE analysis of ab271752.

  • Functional Studies - Recombinant human NAK/TBK1 protein (Active) (ab271752), expandable thumbnail

    Functional Studies - Recombinant human NAK/TBK1 protein (Active) (ab271752)

    Specific activity of ab271752.

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