Recombinant Human EDEM2/C20orf31 Protein (His Tag) | PKSH030522

Recombinant Human EDEM2/C20orf31 Protein (His Tag) | PKSH030522 | Gentaur US, UK & Europe Disrtribition

Synonyms: bA4204.1;C20orf31;C20orf49;UNQ573/PRO1135

Active Protein: N/A

Activity: A DNA sequence encoding the human EDEM2 (AAH01371.1) (Met1-Lys492) was expressed with a polyhistidine tag at the C-terminus.

Protein Construction: A DNA sequence encoding the human EDEM2 (AAH01371.1) (Met1-Lys492) was expressed with a polyhistidine tag at the C-terminus.

Fusion Tag: C-His

Species: Human

Expressed Host: HEK293 Cells

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

Purity: > 95 % 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: 54 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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

Background: EDEM2, also known as C20orf31, belongs to a family of proteins involved in ER-associated degradation (ERAD) of glycoproteins. In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome. Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). EDEM2 is one of the EDEM homologs. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD.

Research Area: N/A