Recombinant Human DCUN1D1 Protein (His Tag) | PKSH032344

Recombinant Human DCUN1D1 Protein (His Tag) | PKSH032344 | Gentaur US, UK & Europe Disrtribition

Synonyms: DCN1-Like Protein 1; DCUN1 Domain-Containing Protein 1; Defective in Cullin Neddylation Protein 1-Like Protein 1; Squamous Cell Carcinoma-Related Oncogene; DCUN1D1; DCUN1L1; RP42; SCCRO

Active Protein: N/A

Activity: Recombinant Human DCN1-Like Protein 1 is produced by our E.coli expression system and the target gene encoding Met1-Val259 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Human DCN1-Like Protein 1 is produced by our E.coli expression system and the target gene encoding Met1-Val259 is expressed with a 6His tag at the N-terminus.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 32.3 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.

Reconstitution: Please refer to the printed manual for detailed information.

Background: DCN1-Like Protein 1 is a protein containing 1 DCUN1 domain and 1 UBA-like domain. DCN1-Like Protein 1 contains part of an E3 Ubiquitin Ligase Complex for Neddylation. It is required for Neddylation of Cullin components of E3 Cullin-RING Ubiquitin Ligase complexes. It enhances the rate of Cullins Neddylation. DCN1-Like Protein 1 recruits the NEDD8-charged E2 Enzyme to the Cullin component. DCUN1D1 is involved in the release of inhibitory effects of CAND1 on the Cullin-RING Ligase E3 complex assembly and activity. It acts also as an oncogene facilitating malignant transformation and carcinogenic progression.

Research Area: Cell biology, Cancer