Anti-Human CTNNA1 DyLight® 550 conjugated Antibody

Primary Antibodies, Rabbit Polyclonal Antibodies

Boster Bio Anti-Human CTNNA1 DyLight® 550 conjugated Antibody catalog # A01617-Dyl550. Tested in Flow Cytometry applications. This antibody reacts with Human.

CTNNA1, also known as Catenin alpha-1 or Catenin (cadherin-associated protein), alpha 1, is a protein that in humans is encoded by the CTNNA1 gene. It is mapped to 5q31.2. When surface epithelium CTNNA1 was ablated, hair follicle development was blocked and epidermal morphogenesis was dramatically affected, with defects in adherens junction formation, intercellular adhesion, and epithelial polarity. In vitro, CTNNA1 null keratinocytes were poorly contact inhibited and grew rapidly. These differences were not dependent upon intercellular adhesion and were in marked contrast to keratinocytes conditionally null for another essential intercellular adhesion protein, desmoplakin Knockout keratinocytes exhibited sustained activation of the Ras-MAPK cascade due to aberrations in growth factor responses. It is concluded that features of precancerous lesions often attributed to defects in cell cycle regulatory genes can be generated by compromising the function of CTNNA1.

Flow Cytometry, 1-3μg/1x10⁶ cells

0.5-1mg/ml, actual concentration vary by lot. Use suggested dilution ratio to decide dilution procedure.

E.coli-derived human CTNNA1 recombinant protein (Position: D143-D292). Human CTNNA1 shares 98% amino acid (aa) sequence identity with mouse CTNNA1.

At -20°C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.

Expressed ubiquitously in normal tissues.