- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
PRO-2826
Synonyms
L2DTL, DCAF2, RAMP, CDT2.
Description
The DTL Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The DTL His-Tagged Fusion Protein, produced in E. coli, is a 31kDa protein containing 126 amino acid residues of the DTL Human, 1-231 amino acids.
Source
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Stability
Store lyophilized DTL at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Purity
Greater than 90% as determined by SDS-PAGE.
Safety Data Sheet
Usage
Background
Denticleless E3 ubiquitin protein ligase (DTL) is part of the E3 ubiquitin ligase family, fundamental to the ubiquitin-proteasome system, which adjusts protein degradation and modification in cells. DTL also participates in numerous critical biological processes, which comprises cell cycle progression, DNA repair, as well as embryonic development. More than a few diseases have been linked with the dysregulation of DTL in particular Cancer, this highlights the importance of DTL as a potential therapeutic goal. DTL takes an important part in regulating the cell cycle, mainly the transition from the G1 phase to the S phase. The degradation of cell cycle regulators, such as cyclins, is also mediated by DTL in that way assuring appropriate cell division in addition to preventing uncontrolled proliferation. DTL is also part of the DNA damage response mechanisms. It ubiquitinates vital proteins which are involved in DNA repair pathways, thus influencing the cellular response to genotoxic stress and preserving genomic integrity.