[Isoform 1]: E3 ubiquitin-protein ligase (PubMed:22529100). May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1 (PubMed:19100260, PubMed:22529100). Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251).; [Isoform 2]: Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251). Negatively regulates the canonical NF-kappa-B signaling pathway via stabilization of CACTIN in an ubiquitination-independent manner (PubMed:26363554).

E3 ubiquitin-protein ligase TRIM39 (EC 2.3.2.27) (RING finger protein 23) (RING-type E3 ubiquitin transferase TRIM39) (Testis-abundant finger protein) (Tripartite motif-containing protein 39)
TRIM39 RNF23 TFP RNF23; TFP; TRIM39B

Q9HCM9

Human, Mouse, Rat

WB

WB 1:2000

56.2 kDa

Mouse

Human recombinant protein fragment corresponding to amino acids 144-378 of human TRIM39 (NP_742013) produced in E.coli.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.