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

CAT#: RC200539L2V

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

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: Calpain 6
• Synonyms: CalpM; CANPX; CAPNX; DJ914P14.1
• Mammalian Cell Selection: None
• Vector: pLenti-C-mGFP
• ACCN: NM_014289
• ORF Size: 1923 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC200539).
• 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.

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
• Gene 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]