PIK3C2B (NM_002646) Human Tagged ORF Clone Lentiviral Particle

SKU RC218354L2V

Lenti ORF particles, PIK3C2B (mGFP-tagged)-Human phosphoinositide-3-kinase, class 2, beta polypeptide (PIK3C2B), 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Target Symbol: PIK3C2B
• Synonyms: C2-PI3K
• Vector: pLenti-C-mGFP
• Mammalian Cell Selection: None
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC218354).
• ACCN: NM_002646
• ORF Size: 4902 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_002646.2
• RefSeq Size: 7618 bp
• RefSeq ORF: 4905 bp
• Locus ID: 5287
• UniProt ID: O00750
• Cytogenetics: 1q32.1
• Protein Families: Druggable Genome
• Protein Pathways: Inositol phosphate metabolism, Metabolic pathways, Phosphatidylinositol signaling system
• MW: 184.6 kDa
• Summary: The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is sensitive to low nanomolar levels of the inhibitor wortmanin. The C2 domain of this protein was shown to bind phospholipids but not Ca2+, which suggests that this enzyme may function in a calcium-independent manner. [provided by RefSeq, Jul 2008]