PAM Protein, Human (HEK293, His)

The PAM protein is a bifunctional enzyme that coordinates the α-amidation process, which is critical for the biosynthesis of neuropeptides and endocrine peptides. The peptidyl α-hydroxylating monooxygenase (PHM) domain hydroxylates the C-terminal glycine, and the peptidylglycine amide glycolate lyase (PAL) domain cleaves the NC-α bond, producing α-amidated peptides. PAM Protein, Human (HEK293, His) is the recombinant human-derived PAM protein, expressed by HEK293 , with C-His labeled tag. The total length of PAM Protein, Human (HEK293, His) is 866 a.a., with molecular weight of ~94.4 kDa.

The PAM protein operates as a bifunctional enzyme, overseeing the post-translational modification of inactive peptidylglycine precursors to their bioactive alpha-amidated peptide forms—a crucial terminal modification in the biosynthesis of numerous neural and endocrine peptides. The alpha-amidation process involves two sequential reactions, each governed by distinct catalytic domains within the enzyme. In the first step, the peptidyl alpha-hydroxylating monooxygenase (PHM) domain catalyzes a copper-, ascorbate-, and O2-dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The subsequent step, orchestrated by the peptidylglycine amidoglycolate lyase (PAL) domain, entails a zinc-dependent cleavage of the N-C-alpha bond, resulting in the production of the alpha-amidated peptide and glyoxylate. Additionally, PAM exhibits a similar capacity to catalyze the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate in a manner reminiscent of its peptidylglycine modification function.

Measured by its ability to convert Hippurate to Benzamide and Glyoxylate. The specific activity is 731.87 pmol/min/μg, as measured under the described conditions.

Human

HEK293

C-His

P19021-2 (M1-S866)

5066  [NCBI]

Approximately 94.4 kDa

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

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.