CNPY2 cDNA ORF Clone in Cloning Vector, Human

Cat: HG13771-G
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CNPY2 cDNA ORF Clone in Cloning Vector, Human General Information
Gene
Species
Human
NCBI Ref Seq
RefSeq ORF Size
549 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence.
Description
Full length Clone DNA of Human canopy 2 homolog (zebrafish).
Plasmid
Vector
pGEM-T Vector
Sequencing Primers
SP6 and T7 or M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.
CNPY2 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

CNPY2 cDNA ORF Clone in Cloning Vector, Human Alternative Names
HP10390 cDNA ORF Clone, Human;MSAP cDNA ORF Clone, Human;TMEM4 cDNA ORF Clone, Human;ZSIG9 cDNA ORF Clone, Human
CNPY2 Background Information

CNPY2 is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain. CNPY2 enhances migration of C6 glioma cells through phosphorylation of the myosin regulatory light chain. It is expressed in different tissues, including brain. Overexpression of CNPY2 enhanced the motility of glioma cells measured in matrigel invasion chambers and using a scratch assay. Downregulation of CNPY2 by RNA interference significantly decreased glioma cell migration and phosphorylation of MRLC. Inhibition of the corresponding MRLC kinase by ML-7 did not affect migration of CNPY2-overexpressing cells.

Full Name
canopy FGF signaling regulator 2
References
  • Trynka G, et al. (2009) Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling. Gut. 58(8):1078-83.
  • Danielsen JM, et al. (2011) Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Mol Cell Proteomics. 10(3):M110.003590.
  • Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 44(2):325-40.
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