For Research Use Only. Not for use in diagnostic procedures.

Lyophilized powder

Add 100ul of sterile PBS. Final peptide concentration is 1 mg/ml in PBS. For longer periods of storage, store at -20 degree C. Avoid repeat freeze-thaw cycles.

Small volumes of ADD2 blocking peptide vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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 for calmodulin, and is required for association with spectrin and actin. Alternatively spliced transcript variants have been described.

Peptide

Western Blot (WB)

79

adducin 2

beta-adducin

Beta-adducin

ADDB??[Similar Products]

ADDB_HUMAN

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 for calmodulin, and is required for association with spectrin and actin. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jun 2010]

ADD2: a cytoskeletal protein that promotes the assembly of the spectrin-actin network. Adducin is a heterodimeric protein that consists of related subunits. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Beta-adducin is restricted to brain and hematopoietic tissues. Three alternatively-spliced isoforms have been described.

Protein type: Motility/polarity/chemotaxis; Cytoskeletal

Chromosomal Location of Human Ortholog: 2p13.3

Cellular Component: F-actin capping protein complex; cytoplasmic membrane-bound vesicle; plasma membrane

Molecular Function: actin filament binding; calmodulin binding; protein homodimerization activity; spectrin binding; protein heterodimerization activity; actin binding; structural molecule activity

Biological Process: actin filament bundle formation; positive regulation of protein binding; hemopoiesis; protein complex assembly; barbed-end actin filament capping; actin cytoskeleton organization and biogenesis

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