中文名稱：CAPN6抗原（重組蛋白）

英文名稱：CAPN6 Antigen (Recombinant Protein)

儲存：冷凍（-20℃）

相關(guān)類別：抗原

概述

Fusion protein corresponding to a region derived from 26-343 amino acids of human CAPN6

技術(shù)規(guī)格

Full name:

calpain 6

Synonyms:

CANPX, CAPNX, CalpM, DJ914P14.1

Swissprot:

Q9Y6Q1

Gene Accession:

BC000730

Purity:

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

Expression system:

Escherichia coli

Tags:

His tag C-Terminus, GST tag N-Terminus

Background:

Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The protein encoded by this gene is highly expressed in the placenta. Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks critical active site residues and thus is suggested to be proteolytically inactive. The protein may play a role in tumor formation by inhibiting apoptosis and promoting angiogenesis.

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CAPN6抗原（重組蛋白）說明書
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CAPN6抗原（重組蛋白）

Full name:	calpain 6
Synonyms:	CANPX, CAPNX, CalpM, DJ914P14.1
Swissprot:	Q9Y6Q1
Gene Accession:	BC000730
Purity:	>85%, as determined by Coomassie blue stained SDS-PAGE
Expression system:	Escherichia coli
Tags:	His tag C-Terminus, GST tag N-Terminus
Background:	Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The protein encoded by this gene is highly expressed in the placenta. Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks critical active site residues and thus is suggested to be proteolytically inactive. The protein may play a role in tumor formation by inhibiting apoptosis and promoting angiogenesis.