Mouse Gamma-adducin (ADD3) ELISA Kit
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Description
Mouse Gamma-adducin (ADD3) ELISA Kit is an ELISA Kit for the in vitro quantitative measurement of Mouse Gamma-adducin concentrations in tissue homogenates, cell lysates and other biological fluids.
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Product specifications
| Category | ELISA Kits |
| Immunogen Target | Gamma-adducin (ADD3) |
| Reactivity | Mouse |
| Detection Method | Colorimetric |
| Assay Data | Quantitative |
| Test Range | 0.156 ng/ml - 10 ng/ml |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Size 1 | 96 tests |
| Form | Lyophilized |
| Tested Applications | ELISA |
| Sample Type | Tissue homogenates, cell lysates and other biological fluids. |
| Availability | Shipped within 5-15 working days. The validity for this kit is 6 months. |
| Storage | Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. |
| Dry Ice | No |
| UniProt ID | Q9QYB5 |
| Gene ID | 27360 |
| Alias | ADDL,CPSQ3,ADDUCIN 3 |
| Background | Elisa kits for ADD3 |
| Status | RUO |
| Note | Validity: The validity for this kit is 6 months. This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. |
Descripción
ADD3 encodes gamma-adducin, a ubiquitously expressed cytoskeletal protein that cooperates with alpha- and beta-adducins to modulate the actin-spectrin network and stabilize cellular membranes. It is most abundantly expressed in the liver, kidneys, and vascular endothelium, where it regulates cell shape, motility, and membrane mechanical properties. Gamma-adducin is also implicated in intracellular signaling and vascular integrity, playing a role in processes such as angiogenesis and endothelial barrier function. Variants in ADD3 have been associated with conditions such as hypertension and vascular diseases due to its role in modulating ion transport and vascular permeability. Dysregulation of gamma-adducin impacts cellular architecture and signaling pathways, contributing to diseases involving structural or functional defects in the actin-spectrin cytoskeleton. Its broad expression and functional versatility highlight its importance in cellular and systemic homeostasis.
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Gamma-Adducin (ADD3) Antibody
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Gamma-Adducin (ADD3) Antibody
Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Alternatively spliced adducin gamma transcripts encoding different isoforms have been described. The functions of the different isoforms are not known.
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