The following CHUK reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

CHUK Antibodies

CHUK Antibodies for Homo sapiens (Human)

CHUK Antibodies for Danio rerio (Zebrafish) (Brachydanio rerio)

CHUK Proteins

CHUK Proteins for Homo sapiens (Human)

CHUK Proteins for Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)

CHUK Proteins for Danio rerio (Zebrafish) (Brachydanio rerio)

CHUK Proteins for Mus musculus (Mouse)

CHUK Proteins for Gallus gallus (Chicken)

CHUK Proteins for Xenopus laevis (African clawed frog)

CHUK Proteins for Bos taurus (Bovine)

CHUK Background

Conserved helix-loop-helix ubiquitous kinase, abbreviated for CHUK, is also called inhibitor of nuclear factor kappa-B kinase subunit alpha (IKK-α/IKKA) or IKK1 [1]. IKK-α, a serine⁄threonine kinase, belongs to the catalytic component of the inhibitor of the NF-kappa B Kinase(IKK) complex that plays a central role in regulating the NF-κB transcription factor [2]. Under homeostatic conditions, NF-κ B is weakly active due to cytoplasmic sequestration via noncovalent binding to IκB (inhibitor of NF-κB) proteins [3]. An NF-κB-inducing kinase (NIK), a central signaling component of the noncanonical NF-κB pathway, is targeted for continuous degradation by a tumor necrosis factor (TNF) receptor-associated factor-3 (TRAF3)-dependent E3 ubiquitin ligase [4]. Stimulated by non-canonical signals, NIK is stabilized from proteolysis to the extent that it becomes capable of recruiting and inducing the kinase activity of IKK-α [5] Subsequently, IKK-α and NIK phosphorylate three serines of NF-κB2/β100 within its C-terminal IκBδ segment, leading to the processing of NF-κB2 precursor protein p100 to p52. Phosphorylation-dependent ubiquitylation and proteasomal degradation of the IκB proteins lead to the release of active NF-κB dimers [6]. In turn, free NF-κB is translocated into the nucleus and activates the transcription of multiple genes involved in immune response, growth control, or protection against apoptosis. Since weak IKK- α activity has been reported in a large percentage of human squamous cell carcinomas, Lahtela J et al. found that normalizing IKK-α in mouse models of skin cancer exhibited an anti-tumorigenic effect [7]. IKK-α mutations in humans have been associated with lethal fetal malformations, which are characterized by shiny, thickened skin and truncated limbs in appearance [8].

[1] Mock BA, Connelly MA, et al. CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human chromosome 10 and mouse chromosome 19 [J]. Genomics. 1995, 27 (2): 348-51.
[2] Häcker H, Karin M. Regulation and function of IKK and IKK-related kinases [J]. Sci. STKE. 2006 (357): re13.
[3] Hinz M, Scheidereit C The IκB kinase complex in NF-κB regulation and beyond [J]. EMBO Rep. 2014 Jan; 15(1):46-61.
[4] Qing G, Qu Z, Xiao G Stabilization of basally translated NF-kappaB-inducing kinase (NIK) protein functions as a molecular switch of processing of NF-kappaB2 p100 [J]. J Biol Chem. 2005 Dec 9; 280 (49):40578-82.
[5] Vallabhapurapu S, Matsuzawa A, et al. Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling [J]. Nat Immunol. 2008 Dec; 9(12):1364-70.
[6] Hayden MS, Ghosh S Shared principles in NF-kappaB signaling [J]. Cell. 2008 Feb 8; 132(3):344-62.
[7] Liu B, Park E, et al. A critical role for IκB kinase α in the development of human and mouse squamous cell carcinomas [J]. Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (46): 17202-7.
[8] Lahtela J, Nousiainen HO, et al.Mutant CHUK and severe fetal encasement malformation [J]. New England Journal of Medicine. 2010, 363 (17): 1631-1637.

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