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| Cat.No | ACP12342 | Target Name | EDEM2 |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Expression Range | 22-578 | Protein Length | Full Length of Mature Protein |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9BV94 |
|---|
Uniprot Id
Q9BV94
Target Species
Human
Target Name
EDEM2
Target Full Name
ER degradation-enhancing alpha-mannosidase-like protein 2
Target Function
Involved in the endoplasmic reticulum-associated degradation (ERAD) pathway that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. May initiate ERAD by promoting the first mannose trimming step of ERAD substrates, from Man9GlcNAc2 to Man8GlcNAc2. Seems to recognize and bind to exposed hydrophobic regions in target proteins.
Target Subcellular Location
Endoplasmic reticulum lumen.
Target Protein Families
Glycosyl hydrolase 47 family
Target Tissue Specificity
Expressed ubiquitously in all tissues tested with slightly higher levels detected in small intestine and peripheral blood leukocytes and weakest levels in brain and skeletal muscle.
Target Synonyms
bA4204.1; C20orf31; C20orf49; EDEM 2; EDEM2; EDEM2_HUMAN; ER degradation enhancer mannosidase alpha like 2; ER degradation enhancing alpha mannosidase like 2; ER degradation enhancing alpha mannosidase like protein 2; ER degradation enhancing mannosidase like protein 2; ER degradation-enhancing alpha-mannosidase-like 2; FLJ10783; UNQ573/PRO1135
Target Background
In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). EDEM2 belongs to a family of proteins involved in ERAD of glycoproteins (Mast et al., 2005 [PubMed 15537790]).
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