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MSH2 Antibody

Purified Mouse Monoclonal Antibody (Mab)

     
  • 1 - MSH2 Antibody AP52824
    Western blot detection of MSH2 in K562,CEM,Jurkat,293T and A431 cell lysates using MSH2 mouse mAb (1:1000 diluted).Predicted band size:100KDa.Observed band size:100KDa.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P43246
Reactivity Human
Host Mouse
Clonality Monoclonal
Isotype IgG2b
Calculated MW 100 KDa
Additional Information
Gene ID 4436
Other Names BAT26;COCA 1;COCA1;DNA mismatch repair protein Msh2;FCC 1;FCC1;hMSH2;HNPCC 1;HNPCC;HNPCC1;LCFS2;MSH 2;Msh2;MSH2_HUMAN;MutS homolog 2;MutS homolog 2 colon cancer nonpolyposis type 1;MutS protein homolog 2.
Dilution WB~~1:1000
Format Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.02% sodium azide and 50% glycerol.
Storage Store at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name MSH2
Function Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containg DNA strand (PubMed:26300262). ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B- induced cell cycle regulation and apoptosis.
Cellular Location Nucleus. Chromosome
Tissue Location Ubiquitously expressed.
Research Areas

BACKGROUND

Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.

REFERENCES

Fishel R.,et al.Cell 75:1027-1038(1993).
Fishel R.,et al.Cell 77:167-167(1994).
Leach F.S.,et al.Cell 75:1215-1225(1993).
Kolodner R.D.,et al.Genomics 24:516-526(1994).
Wijnen J.,et al.Am. J. Hum. Genet. 56:1060-1066(1995).

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