Overview
| 别名 | Peptidyl-glycine alpha-amidating monooxygenase; PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase; PHM); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidylamidoglycolate lyase; PAL] |
| 基因名 | PAM |
| UniProt ID | P19021 |
| 反应种属 | Human |
| 应用 | WB,IHC-P |
| 宿主 | Mouse |
| 偶联物 | Unconjugated |
| 修饰 | Unmodified |
| 亚型 | IgG1 |
| 克隆号 | 9T7-Z2-N7 |
| 克隆性 | Monoclonal Antibody |
| 分子量 | Calculated MW: 108 kDa |
| 纯化方式 | Affinity Purified |
| 产品形式 | Liquid |
| 推荐稀释比 | WB-1:1000; IHC-1:50 |
| 存储缓冲液 | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% sodium azide |
| 保存温度 | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| 背景信息 | Peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional enzyme crucial for the biosynthesis of many signaling peptides and fatty acid amides. It catalyzes the conversion of peptides with a C-terminal glycine into peptides with a terminal amide group, a process essential for the bioactivity of these peptides. PAM has two enzymatically active domains: peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). The PHM domain hydroxylates the C-terminal glycine residue using a copper ion cofactor and oxygen, while the PAL domain completes the conversion by eliminating glyoxylate from the hydroxylated glycine, producing the alpha-amidated peptide. This enzyme is encoded by the PAM gene in humans and is expressed in various endocrine and exocrine glands. The transformation makes peptides more hydrophobic and neutrally charged, enhancing their ability to bind to receptors. |
检测原理