Human PAM (Peptidylglycine Alpha Amidating Monooxygenase) Sandwich ELISA Kit Ready-To-Use Kit (STJE0017653)
SPECIFICATIONS
General Information
| Short Description | This PAM Sandwich ELISA Kit, Ready-To-Use is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in human serum, plasma, tissue homogenates or other biological fluids.. |
| Applications | ELISA |
| Reactivity | Human |
| Sensitivity | 13.5pg/mL |
| Detection Limit | 31.2-2000pg/mL |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Storage Instruction | The whole kit may be stored at-20°C for up to 12 months from receipt. An unopened kit may be stored in the fridge at 2-8°C for up to 6 months. Once opened store individual kit contents according to components table provided with the kit. |
| Assay Time | 3 hrs |
Target Information
| Gene Symbol | PAM |
| Gene ID | 5066 |
| Uniprot ID | AMD_HUMAN |
| Immunogen Region | Ready-To-Use |
| Sample Type | serum, plasma, tissue homogenates or other biological fluids. |
Additional Info
| Tissue Specificity | |
| Post Translational Modifications | |
| Function | 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. 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. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate. |
| Protein Name | Peptidyl-Glycine Alpha-Amidating MonooxygenasePam Includes - Peptidylglycine Alpha-Hydroxylating MonooxygenasePhm - Peptidyl-Alpha-Hydroxyglycine Alpha-Amidating LyasePeptidylamidoglycolate LyasePal |
| Database Links | |
| Cellular Localisation | Cytoplasmic VesicleSecretory Vesicle MembraneSingle-Pass Membrane ProteinSecretory GranulesIsoform 1: MembraneSingle-Pass Type I Membrane ProteinIsoform 2: MembraneIsoform 3: SecretedSecreted From Secretory GranulesIsoform 4: Secreted |
| Alternative ELISA Names | Peptidyl-Glycine Alpha-Amidating Monooxygenase ELISA kitPam Includes - Peptidylglycine Alpha-Hydroxylating Monooxygenase ELISA kitPhm - Peptidyl-Alpha-Hydroxyglycine Alpha-Amidating Lyase ELISA kitPeptidylamidoglycolate Lyase ELISA kitPal ELISA kitPAM ELISA kit |
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Information sourced from Uniprot.org