Recombinant Mouse ART4/CD297 Protein (Fc Tag) | PKSM040363

Recombinant Mouse ART4/CD297 Protein (Fc Tag) | PKSM040363 | Gentaur US, UK & Europe Disrtribition

Synonyms: 4432404K01Rik;ARTC4;DO;DOK1

Active Protein: N/A

Activity: A DNA sequence encoding the mouse Art4 (NP_080915.1) (Met1-Lys263) was expressed, fused with the Fc region of human IgG1 at the C-terminus.

Protein Construction: A DNA sequence encoding the mouse Art4 (NP_080915.1) (Met1-Lys263) was expressed, fused with the Fc region of human IgG1 at the C-terminus.

Fusion Tag: C-Fc

Species: Mouse

Expressed Host: HEK293 Cells

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

Purity: > 91 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein 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: 53.7 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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

Background: ADP-ribosyltransferase 4 (Dombrock blood group), also known as Mono-ADP-ribosyltransferase 4(ART4), Dombrock blood group carrier molecule and CD297, is a protein that contains a mono-ADP-ribosylation (ART) motif. It is a member of the ADP-ribosyltransferase gene family but enzymatic activity has not been demonstrated experimentally. ADP-ribosyltransferase catalyzes the ADP-ribosylation of arginine residues in proteins. Mono-ADP-ribosylation is a posttranslational modification of proteins that is interfered with by a variety of bacterial toxins including cholera, pertussis, and heat-labile enterotoxins of E. coli. ART4 could be detected on HEL cells and erythrocytes by FACS analysis while it was absent from activated monocytes, despite the presence of ART4 mRNA in these cells. ART is also known as the carrier of the Dombrock blood group alloantigens (Do) which is glycosylphosphatidylinosotol-anchored to the erythrocyte membrane.

Research Area: N/A