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Recombinant human DTL protein

Cat:P04096

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 1-350aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: DTL
【Full Name】: denticleless homolog (Drosophila)
【Uniprot】: Q9NZJ0
【Gene ID】: 51514
【Species Reactivity】: Human Mouse (Chicken)
【Mol Mass】: 39kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: N0
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis.The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2.CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication.CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing.KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration.Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation.In undamaged proliferating cells, the DCX(DTL) complex also

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