Rabbit Recombinant Monoclonal FXYD3 antibody - conjugated to Alexa Fluor® 555.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
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Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell (PubMed:17077088). Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (PubMed:21454534). Induces a hyperpolarization-activated chloride current when expressed in Xenopus oocytes (PubMed:7836447). Isoform 1. Decreases the apparent K+ and Na+ affinity of the sodium/potassium-transporting ATPase over a large range of membrane potentials. Isoform 2. Decreases the apparent K+ affinity of the sodium/potassium-transporting ATPase only at slightly negative and positive membrane potentials and increases the apparent Na+ affinity over a large range of membrane potentials.
MAT8, PLML, FXYD3, FXYD domain-containing ion transport regulator 3, Chloride conductance inducer protein Mat-8, Mammary tumor 8 kDa protein, Phospholemman-like, Sodium/potassium-transporting ATPase subunit FXYD3
Rabbit Recombinant Monoclonal FXYD3 antibody - conjugated to Alexa Fluor® 555.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
FXYD3 also known as Mat-8 plays a role as a regulatory subunit associated with the Na+/K+-ATPase pump modulating its ion transport activity. The protein has a molecular weight of approximately 10 kDa. FXYD3 is expressed in various tissues but it shows higher levels in epithelial tissues particularly in gastrointestinal and mammary tissues. The protein consists of a single transmembrane domain which suggests its function in modulating ion exchange across membranes.
FXYD3 modulates ion transport processes important for maintaining cellular homeostasis. It forms part of the larger Na+/K+-ATPase complex interacting with other subunits to influence the pump's activity. This association affects the electrochemical gradients across the cell membrane impacting various cellular processes including volume regulation pH balance and nutrient uptake. Therefore FXYD3 is involved in key physiological roles in tissues where electrolyte balance is essential.
FXYD3 integrates into ion transport and signaling pathways including the sodium ion transmembrane transport pathway. It interacts closely with proteins like the α and β subunits of the Na+/K+-ATPase in this context regulating their pump activity. This integration with the sodium ion transmembrane transport and signal transduction pathways exemplifies FXYD3’s role in cellular ion homeostasis and how it may influence specific physiological responses.
FXYD3 shows links to cancer particularly breast cancer. Altered expression of FXYD3 has been observed in malignant tissues suggesting a contribution to tumor development and progression. The relationship between FXYD3 and proteins like E-cadherin in this context may indicate its role in cellular adhesion and migration alterations seen in cancer. Another disorder linked to FXYD3 is cystic fibrosis where its modulation of ion channels could affect disease severity or progression especially regarding electrolyte transport abnormalities.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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