|Detection of Human CD-M6PR Lumenal Domain by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human CD-M6PR Lumenal Domain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5320) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for CD-M6PR Lumenal Domain at approximately 45 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
The CD-M6PR (cation-dependent mannose 6-phosphate receptor; also CD-MPR) is a 44‑46 kDa member of the P-type lectin family of proteins. It is ubiquitously expressed, found internally, and transports newly formed mannose 6-phosphate bearing acid hydrolases from the secretory pathway to acidified lysosomes. Mature human CD-M6PR is a type I transmembrane glycoprotein that is 251 amino acids (aa) in length. It functions as a homodimer, and contains a 159 aa luminal region (aa 27‑185) plus a 67 aa cytoplasmic domain. The aa residues Gln66, Arg111, Glu133 and Tyr143 recognize carbohydrate; Asp103 interacts with divalent cation (Mn2+), increasing ligand affinity and receptor oligomerization. Over aa 27‑184, human CD-M6PR shares 90% aa identity with mouse CD-M6PR.
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