

| Catalog No. | HB756014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human, Mouse, Rat | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human PAM (Phe21-Cys288). | ||||||||
| Target | PAL, PHM, PAM, Peptidylamidoglycolate lyase, Peptidyl-glycine alpha-amidating monooxygenase | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P19021 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Peptidyl-glycine alpha-amidating monooxygenase (PAM) is a ~108 kDa protein. Bifunctional enzyme that catalyzes amidation of the C-terminus of proteins. Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity. C-terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome. Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the 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. 1. Satani, M. et al. (2003) Protein expression and purification 28, 293-302. PMID: 12699694 2. Glauder, J. et al. (1990) Biochemical and biophysical research communications 169, 551-8. PMID: 2357221 3. Eipper, BA. et al. (1992) Annual review of neuroscience 15, 57-85. PMID: 1575450 4. Stadtman, ER. (1990) Biochemistry 29, 6323-31. PMID: 2207077 | ||||||||
| Note | For research use only. |
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