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| Cat.No | ACP09415 | Target Name | CAPN6 |
|---|---|---|---|
| Target Synonyms | CALP M; Calpain-6; Calpain-like protease X-linked; Calpamodulin; CalpM; CAN6_HUMAN; CANP X; CANPX; CAPN 6; Capn6 | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Expression Range | 1-641 |
| Protein Length | Full length protein | Purity | >85% (SDS-PAGE) |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9Y6Q1 |
|---|
Uniprot Id
Q9Y6Q1
Target Species
Human
Target Name
CAPN6
Target Full Name
Calpain-6
Target Function
Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues.
Target Subcellular Location
Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle.
Target Protein Families
Peptidase C2 family
Target Tissue Specificity
Expressed only in placenta.
Target Synonyms
CALP M; Calpain-6; Calpain-like protease X-linked; Calpamodulin; CalpM; CAN6_HUMAN; CANP X; CANPX; CAPN 6; Capn6
Target 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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