M6PR Protein, Human (Cell-Free, His)

M6PR, vital in cellular transport, guides phosphorylated lysosomal enzymes from Golgi and cell surface to lysosomes. Recognizing phosphomannosyl residues, it forms receptor-ligand complexes, transported to acidic prelyosomal compartments. Low pH triggers complex dissociation. M6PR, functioning as a homodimer, interacts with adaptors GGA1, GGA2, and GGA3, ensuring the precision of this transport mechanism. M6PR Protein, Human (Cell-Free, His) is the recombinant human-derived M6PR protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of M6PR Protein, Human (Cell-Free, His) is 251 a.a., with molecular weight of 30.7 kDa.

M6PR, a crucial player in cellular transport processes, facilitates the movement of phosphorylated lysosomal enzymes from both the Golgi complex and the cell surface to lysosomes. This intricate system relies on lysosomal enzymes carrying phosphomannosyl residues, which selectively bind to mannose-6-phosphate receptors within the Golgi apparatus. The ensuing formation of receptor-ligand complexes is then transported to an acidic prelyosomal compartment, where the low pH environment triggers the dissociation of these complexes. Notably, M6PR functions as a homodimer and interacts with adaptor proteins GGA1, GGA2, and GGA3 to contribute to the precision of this intricate transport mechanism.

Human

E. coli Cell-free

N-10*His

P20645 (T27-M277)

4074

TEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM

30.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.