CSTZFND
CompoZr® Custom Zinc Finger Nuclease (ZFN)
ZFN plasmid only
Synonym(s):
CompoZr® Custom Zinc Finger Nuclease (ZFN)
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About This Item
UNSPSC Code:
12352200
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General description
Zinc Finger Nucleases (ZFNs) are a class of engineered DNA-binding proteins that facilitate targeted editing of the genome by creating double-strand breaks in DNA at user-specified locations. Double-strand breaks are important for site-specific mutagenesis in that they stimulate the cell′s natural DNA-repair processes, namely homologous recombination and Non-Homologous End Joining (NHEJ). By implementing established, field-proven methods, these processes can be harnessed to generate precisely targeted genomic edits, resulting in cell lines with precise and heritable gene deletions, integrations or modifications.
Application
Functional Genomics/Target Validation
- Creation of gene knockouts in multiple cell lines
- Complete knockout of genes not amenable to RNAi
- Creation of knock-in cell lines with promoters, fusion tags or reporters integrated into endogenous genes
- Creation of cell lines that produce higher yields of proteins or antibodies
The CompoZr Custom ZFN service can be used to target genes from a variety of organisms. Validation of the custom ZFNs is completed in a proxy cell line for human, mouse, rat and hamster (CHO) projects. In this assay, the candidate ZFNs are delivered to the proxy cell line and activity is identified and measured. Activity is measured by amplifying over the ZFN target site and then using a nuclease mismatch enzyme to cut DNA strands that have been modified. ZFN efficiency can be measured based on the densitometry results of this assay. CompoZr Custom ZFN Projects for human, mouse, rat, and hamster (CHO) will have a production timeline of 10 weeks after the ZFN design is approved.
Components
- Best Performing ZFN Pair
- ZFN Pair in Plasmid Form
- Forward and Reverse Primers that allow for determination of rate of mutation and for screening of individual clones
- Positive Control DNA
- Used to determine a baseline cutting efficiency
Legal Information
All Zinc Finger Nucleases are sold under license from Sangamo Biosciences. For a copy of the Label License provided with purchase of CompoZr ZFNs, please visit the ZFN Label License page.
CompoZr is a registered trademark of Merck KGaA, Darmstadt, Germany
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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Chun Cheng Andy Chen et al.
Physiological genomics, 45(3), 110-118 (2012-12-20)
The present study employed a zinc-finger nuclease strategy to create heterozygous knockout (KO) rats for the transforming growth factor-β1 (Tgfb1) gene on the Dahl SS/Jr genetic background (TGF-β1(+/-) Dahl S). Intercrossing TGF-β1(+/-) rats did not produce any homozygous KO rats
Bettina Schmid et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(13), 4986-4991 (2013-03-05)
Mutations in the Tar DNA binding protein of 43 kDa (TDP-43; TARDBP) are associated with amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43(+) inclusions (FTLD-TDP). To determine the physiological function of TDP-43, we knocked out zebrafish Tardbp and
A Tanaka et al.
Leukemia, 27(8), 1621-1627 (2013-02-16)
Human T-cell leukemia virus type 1 (HTLV-1), which causes adult T-cell leukemia (ATL) in humans, establishes a life-long latent infection. Current therapies are not very effective against HTLV-1-associated disorders. A novel therapeutic approach may help to combat HTLV-1 infection. A
David L Mattson et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 304(6), R407-R414 (2013-02-01)
Hypertension and renal damage in Dahl SS rats are associated with increased infiltrating immune cells in the kidney. To examine the role of infiltrating immune cells in this disease process, a zinc finger nuclease targeting bases 672-706 of recombination-activating gene
Wei-Ta Chen et al.
Molecular and cellular biology, 33(1), 111-126 (2012-10-31)
The histone variant H2AX is a principal component of chromatin involved in the detection, signaling, and repair of DNA double-strand breaks (DSBs). H2AX is thought to operate primarily through its C-terminal S139 phosphorylation, which mediates the recruitment of DNA damage
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