中文名稱：CTNNA1抗原（重組蛋白）

英文名稱：CTNNA1 Antigen (Recombinant Protein)

儲(chǔ) 存：冷凍（-20℃）

相關(guān)類別：抗原

概述

Fusion protein corresponding to C terminal 300 amino acids of human CTNNA1

技術(shù)規(guī)格

Full name:

Catenin (cadherin-associated protein), alpha 1, 102kDa

Synonyms:

CAP102

Swissprot:

P35221

Gene Accession:

BC031262

Purity:

>85%, as determined by Coomassie blue stained SDS-PAGE

Expression system:

Escherichia coli

Tags:

His tag C-Terminus, GST tag N-Terminus

Background:

Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. 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.

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CTNNA1抗原（重組蛋白）說明書
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021-54845833/15800441009

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CTNNA1抗原（重組蛋白）

Full name:	Catenin (cadherin-associated protein), alpha 1, 102kDa
Synonyms:	CAP102
Swissprot:	P35221
Gene Accession:	BC031262
Purity:	>85%, as determined by Coomassie blue stained SDS-PAGE
Expression system:	Escherichia coli
Tags:	His tag C-Terminus, GST tag N-Terminus
Background:	Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. 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.