Calpain 6 (CAPN6) (NM_014289) Human Tagged ORF Clone Lentiviral Particle

SKU RC200539L3V

Lenti ORF particles, CAPN6 (Myc-DDK tagged) - Human calpain 6 (CAPN6), 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Target Symbol: Calpain 6
• Synonyms: CalpM; CANPX; CAPNX; DJ914P14.1
• Vector: pLenti-C-Myc-DDK-P2A-Puro
• Mammalian Cell Selection: Puromycin
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC200539).
• ACCN: NM_014289
• ORF Size: 1923 bp
• OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
• OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.
• Shipping: Dry Ice

Reference Data

• RefSeq: NM_014289.2
• RefSeq Size: 3604 bp
• RefSeq ORF: 1926 bp
• Locus ID: 827
• UniProt ID: Q9Y6Q1
• Cytogenetics: Xq23
• Domains: C2, Calpain_III
• Protein Families: Druggable Genome, Protease
• MW: 74.6 kDa
• Summary: 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. [provided by RefSeq, Nov 2009]