Cow Transmembrane emp24 domain-containing protein 9 (TMED9) ELISA Kit

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AE14721BO
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Product Name Cow Transmembrane emp24 domain-containing protein 9 (TMED9) ELISA Kit
Description TMED9 Belongs to the EMP24/GP25L family.Contains 1 GOLD domain. Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have been shown to be critical components of the coated vesicles that are involved in the transportation of cargo molecules from the endoplasmic reticulum to the Golgi complex. The p24 proteins form hetero-oligomeric complexes and are believed to function as receptors for specific secretory cargo. The identification of the GOLD domain could aid in directed investigation of the role of the p24 proteins in the secretion process. The newly detected group of GOLD-domain proteins, which might simultaneously bind membranes and other proteins, point to the existence of a novel class of adaptors that could have a role in the assembly of membrane-associated complexes or in regulating assembly of cargo into membranous vesicles. This assay has high sensitivity and excellent specificity for detection of Bovine TMED9. No significant cross-reactivity or interference between Bovine TMED9 and analogues was observed.
Synonyms HSGP25L2G, gp25L2 protein
Method Sandwich ELISA
Detection Range Request Information
Sensitivity Request Information
Reactivity Bovine
Sample Types Serum, Plasma, Other biological fluids.
Background TMED9 Belongs to the EMP24/GP25L family.Contains 1 GOLD domain. Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have been shown to be critical components of the coated vesicles that are involved in the transportation of cargo molecules from the endoplasmic reticulum to the Golgi complex. The p24 proteins form hetero-oligomeric complexes and are believed to function as receptors for specific secretory cargo. The identification of the GOLD domain could aid in directed investigation of the role of the p24 proteins in the secretion process. The newly detected group of GOLD-domain proteins, which might simultaneously bind membranes and other proteins, point to the existence of a novel class of adaptors that could have a role in the assembly of membrane-associated complexes or in regulating assembly of cargo into membranous vesicles.
Supplier Abebio

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