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You are here:Home » Antibodies » Antibodies-Actin Related Proteins » Anti -Actinin, alpha

Anti -Actinin, alpha


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Clone Host Grade Applications
Monoclonal Mouse Affinity Purified B IH
Alpha-actinin was initially isolated from rabbit skeletal muscle as a factor that induces the gelation of F-actin and promotes the superprecipitation of actomyosin. Alpha actinins are actin-binding proteins that carry out different purposes in different different cell types. In myofibrillar cells, alpha-actinin constitutes a major component of Z-discs in striated muscle and of the functionally analogous dense bodies and dense plaques in smooth muscle. alpha-actinin (alpha A) shares structural homology with spectrin and dystrophin.
Catalog #A0762-01
ApplicationsSuitable for use in Western Blot and Immunohistochemistry. Other applications not tested.
Recommended DilutionsWestern Blot: 3.5ug/ml
Immunohistochemistry (Paraffin, frozen): 3.5-7ug/ml in formalin fixed, paraffin embedded sections and formalin or acetone fixed tissues. Boiling paraffin sections is required.
Optimal dilutions to be determined by the researcher.
Storage and StabilityLyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Clone TypeMonoclonal
Clone No10K98
FormSupplied as a lyophilized powder from 1.2% sodium acetate, 2% BSA, 0.01% sodium azide. Reconstitute with 1ml sterile PBS.
PurityPurified by affinity chromatography.
ImmunogenRabbit skeletal alpha-actinin
SpecificityRecognizes alpha-Actinin. Species Crossreactivity: human, mouse and rat.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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