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Mouse Anti-Canine Actinin-Alpha 2 Monoclonal Antibody

Cat. No.VD8N39

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for canine actinin-alpha 2. It can be applied to WB, IF and ICC assays of canine actinin-alpha 2.

Specifications

Application WB; IF; ICC
Clonality Monoclonal
Classification Primary Antibody
Clone G3N3
Host Mouse
Target Species Canine
Species Reactivity Canine
Specificity Canine Actinin-Alpha2
Isotype IgG
Immunogen Purified recombinant canine actinin-α2 (C-terminus) protein fragments
Concentration 1 mg/mL
Conjugation Unconjugated
Physical State Liquid

Target Information

Actinin-alpha2 (ACTN2) is an essential component of the muscle cytoskeleton, particularly abundant in fast-twitch muscle fibers. It is a member of the actinin family of proteins, which are characterized by their antiparallel dimer formation and their role as cross-linkers of actin filaments. ACTN2 contributes to the stability of muscle cells by connecting the actin cytoskeleton to integrins and other structural proteins within the muscle fiber. This protein is crucial for muscle contraction and maintaining the structural integrity of muscle tissue. ACTN2's function in muscle is so significant that mutations in the ACTN2 gene have been associated with various muscular disorders, including certain types of congenital myopathies.

Target Canine Actinin-Alpha2
Target Synonym ACTN2; Alpha-actinin-2
UniProt ID A0A8C0RGI1

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C (up to 12 months) on receipt. Avoid repeated freezing and thawing as this may denature the antibody.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Casella, James F., et al. "Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin." Journal of Biological Chemistry 269.9 (1994): 6992-6998.
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