MEG1 (PTPN4) (NM_002830) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC202072L4V

Lenti ORF particles, PTPN4 (mGFP-tagged) - Human protein tyrosine phosphatase, non-receptor type 4 (megakaryocyte) (PTPN4), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: PTPN4
• Synonyms: MEG; PTPMEG; PTPMEG1
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_002830
• ORF Size: 2778 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC202072).
• 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_002830.2, NP_002821.1
• RefSeq Size: 3963 bp
• RefSeq ORF: 2781 bp
• Locus ID: 5775
• Cytogenetics: 2q14.2
• Domains: Y_phosphatase, B41, PDZ, PTPc_motif
• Protein Families: Druggable Genome, Phosphatase
• MW: 105.7 kDa
• Gene Summary: 'The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. This PTP has been shown to interact with glutamate receptor delta 2 and epsilon subunits, and is thought to play a role in signalling downstream of the glutamate receptors through tyrosine dephosphorylation. [provided by RefSeq, Jul 2008]'