MME Protein, Human (P.pastoris, His)

MME proteins exhibit thermolysin-like specificity and primarily degrade polypeptides of up to 30 amino acids. Crucially, it plays a key role in cleaving the Gly-Phe bond to degrade opioid peptides, including Met-enkephalin and Leu-enkephalin. MME Protein, Human (P.pastoris, His) is the recombinant human-derived MME protein, expressed by P. pastoris , with N-His labeled tag.

The MME Protein demonstrates a thermolysin-like specificity, predominantly acting on polypeptides of up to 30 amino acids. Biologically crucial, it plays a key role in the degradation of opioid peptides, including Met- and Leu-enkephalins, achieved through the cleavage of a Gly-Phe bond. Additionally, MME catalyzes the cleavage of bradykinin, substance P, and neurotensin peptides and is capable of cleaving angiotensin-1, angiotensin-2, and angiotensin 1-9. The protein is involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)). Furthermore, MME displays UV-inducible elastase activity toward skin preelastic and elastic fibers.

Human

P. pastoris

N-His

P08473 (Y52-W750)

4311  [NCBI]

YDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW

Approximately 81.8 kDa

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

<1 EU/μg, determined by LAL method.