MSH3 (NM_002439) Human Tagged ORF Clone Lentiviral Particle

  • LentiORF®
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SKU
RC212391L1V
Lenti ORF particles, MSH3 (Myc-DDK tagged) - Human mutS homolog 3 (E. coli) (MSH3), 200ul, >10^7 TU/mL
  $2,034.00
3 Weeks*
Specifications
Specifications
Product Data
Type Human Tagged ORF Clone Lentiviral Particle
Tag Myc-DDK
Target Symbol MSH3
Synonyms DUP; FAP4; MRP1
Vector pLenti-C-Myc-DDK
Mammalian Cell Selection None
Sequence Data
ORF Nucleotide Sequence
The ORF insert of this clone is exactly the same as(RC212391).
ACCN NM_002439
ORF Size 3411 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_002439.2
RefSeq Size 4645 bp
RefSeq ORF 3414 bp
Locus ID 4437
UniProt ID P20585
Cytogenetics 5q14.1
Domains MutS_I, MutS_II, MutS_III, MutS_V
Protein Families Druggable Genome, Stem cell - Pluripotency
Protein Pathways Colorectal cancer, Mismatch repair, Pathways in cancer
MW 127.2 kDa
Summary The protein encoded by this gene forms a heterodimer with MSH2 to form MutS beta, part of the post-replicative DNA mismatch repair system. MutS beta initiates mismatch repair by binding to a mismatch and then forming a complex with MutL alpha heterodimer. This gene contains a polymorphic 9 bp tandem repeat sequence in the first exon. The repeat is present 6 times in the reference genome sequence and 3-7 repeats have been reported. Defects in this gene are a cause of susceptibility to endometrial cancer. provided by RefSeq, Mar 2011
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Documents
Resources

file-alt Citations

The human DNA mismatch repair protein MSH3 contains nuclear localization and export signals that enable nuclear-cytosolic shuttling in response to inflammation
Tseng-Rogenski, Munakata, Choi et al
Mol. Cell. Biol. (2020)
AI Summary: In this study, OriGene's MSH3 cDNA clone (RC209084) was used to investigate the roles of nuclear localization and export signals in the human MSH3 protein, enabling the authors to analyze how MSH3 shuttles between the nucleus and cytosol in response to inflammation.
Snippet: … CRCs exhibiting elevated microsatellite alterations at selected tetranucleotide repeats (EMAST) show reduced nuclear MutS homolog 3 (MSH3) expression with surrounding inflammation and portends poor patient outcomes. MSH3 reversibly exits from the nucleus to the cytosol in response to the pro-inflammatory cytokine interleukin-6 (IL-6), suggesting that MSH3 may be a shuttling protein. Here, we manipulated three putative nuclear localization (NLS1-3) and two potential nuclear export signals (NES1-2) within MSH3. We found that both NLS1 and NLS2 possess nuclear import function, with NLS1 responsible for nuclear localization within full-length MSH3. We also found that NES1 and NES2 work synergistically to maximize nuclear export, with both being required for IL-6-induced MSH3 export. … With oxidative stress, Δ27bpMSH3 localizes to the cytoplasm, suggesting that NLS1 function in Δ27bpMSH3 is compromised. Overall, MSH3's shuttling in response to inflammation enables accumulation in the cytoplasm;reduced nuclear MSH3 increases EMAST and DNA damage. …CRCs exhibiting elevated microsatellite alterations at selected tetranucleotide repeats (EMAST) show reduced nuclear MutS homolog 3 (MSH3) expression with surrounding inflammation and portends poor patient outcomes. MSH3 reversibly exits from the nucleus to the cytosol in response to the pro-inflammatory cytokine interleukin-6 (IL-6), suggesting that MSH3 may be a shuttling protein. Here, we manipulated three putative nuclear localization (NLS1–3) and two potential nuclear export signals (NES1–2) within MSH3. We found that both NLS1 and NLS2 possess nuclear import function, with NLS1 responsible for nuclear localization within full-length MSH3. We also found that NES1 and NES2 work synergistically to maximize nuclear export, with both being required for IL-6–induced MSH3 export. … With oxidative stress, Δ27bpMSH3 localizes to the cytoplasm, suggesting that NLS1 function in Δ27bpMSH3 is compromised. Overall, MSH3's shuttling in response to inflammation enables accumulation in the cytoplasm;reduced nuclear MSH3 increases EMAST and DNA damage. …
Showing 1-1 of 1 papers.
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