Cat. No.: DAB-0012329
| Product Information | |
|---|---|
| Clonality | Monoclonal |
| Isotype | IgG |
| Host Species | Rabbit |
| Reactivity | Human |
| Applications | WB, IHC, IF |
| Product Description | Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro12 of human Na, K-ATPase α1 protein. |
| Format | Liquid |
| Purity | Affinity purity |
| Target Information | |
|---|---|
| Target Name | ATP1A1 |
| UniProt No. | P05023 |
| Gene ID | 476 |
| Gene Description | The Na, K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit. Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase, Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA. All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na, K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule. Na, K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit. Na, K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors. |
| Shipping & Storage | |
|---|---|
| Shipping | Shipped at 4 °C. |
| Storage Instructions | Store at –20 °C. Do not aliquot the antibody. |
| Storage Buffer | Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. |
