|Tested species reactivity||Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant fragment corresponding to a region within amino acids 354 and 598 of Human beta Adducin|
|Purification||Antigen affinity chromatography|
|Storage buffer||0.1M tris glycine, pH 7, with 10% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:500-1:3000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA5-29499 targets beta Adducin in WB applications and shows reactivity with mouse samples.
The PA5-29499 immunogen is recombinant fragment corresponding to a region within amino acids 354 and 598 of Human beta Adducin.
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. Various adducin beta mRNAs, alternatively spliced at 3'end and/or internally spliced and encoding different isoforms, have been described. The functions of all the different isoforms are not known.
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