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Goat Anti-PAM / PAL Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P19021 |
| Other Accession | NP_620177, 5066 |
| Reactivity | Human |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 108332 Da |
| Gene ID | 5066 |
|---|---|
| Other Names | Peptidyl-glycine alpha-amidating monooxygenase, PAM, Peptidylglycine alpha-hydroxylating monooxygenase, PHM, 1.14.17.3, Peptidyl-alpha-hydroxyglycine alpha-amidating lyase, 4.3.2.5, Peptidylamidoglycolate lyase, PAL, PAM |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-PAM / PAL Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PAM {ECO:0000303|PubMed:12699694, ECO:0000312|HGNC:HGNC:8596} |
|---|---|
| Function | Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:12699694). 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 (PubMed:12699694). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc- dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:12699694). Similarly, catalyzes the two- step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity). |
| Cellular Location | Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules {ECO:0000250|UniProtKB:P10731} [Isoform 2]: Membrane; Single-pass type I membrane protein [Isoform 4]: Secreted. Note=Secreted from secretory granules |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a multifunctional protein. It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These catalytic domains work sequentially to catalyze neuroendocrine peptides to active alpha-amidated products. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene but some of their full length sequences are not yet known.
References
E3 ligases Arf-bp1 and Pam mediate lithium-stimulated degradation of the circadian heme receptor Rev-erb alpha. Yin L, et al. Proc Natl Acad Sci U S A, 2010 Jun 22. PMID 20534529.
Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score. Rose JE, et al. Mol Med, 2010 Jul-Aug. PMID 20379614.
Poor replication of candidate genes for major depressive disorder using genome-wide association data. Bosker FJ, et al. Mol Psychiatry, 2010 Mar 30. PMID 20351714.
The peptidylglycine alpha-amidating monooxygenase (PAM): a novel prodrug strategy for amidoximes and N-hydroxyguanidines? Schade D, et al. ChemMedChem, 2009 Oct. PMID 19693765.
Common variants conferring risk of schizophrenia. Stefansson H, et al. Nature, 2009 Aug 6. PMID 19571808.
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