Human DNA Mismatch Repair Protein Mlh1 (MLH1) Protein
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Description
Human DNA Mismatch Repair Protein Mlh1 (MLH1) Protein is a Recombinant Human protein expressed in E. coli.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | DNA Mismatch Repair Protein Mlh1 (MLH1) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 26.7 kDa Observed MW: 27 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Ser2-Val213 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 90% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P40692 |
| Gene ID | 4292 |
| NCBI Accession | NP_000240.1, NM_000249.3 |
| OMIM | 114500 |
| Background | Protein MLH1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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MLH1 antibody
Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system(MMR). DNA repair is initiated by MutS alpha(MSH2-MSH6) or MutS beta(MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha(MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis.
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MLH1 Antibody is a Rabbit Polyclonal antibody against MLH1. Mismatch repair (MMR), a conserved process that involves correcting errors made during DNA synthesis, is crucial to the maintenance of genomic integrity. MLH1 is the human homologue of the E. coli MMR gene mutL. MMR requires recognition of a base mismatch or insertion/deletion loop by a MutS homolog followed by recruitment of a MutL heterodimeric complex consisting of MLH1 and PMS1 (MutL-α), PMS2 (MutL-β) or MLH3 (MutL-γ). Other factors required for MMR in eukaryotes are EXO1, PCNA, RFC, RPA, DNA polymerases and DNA ligase (reviewed in 1). Inactivation of the MLH1 gene causes genome instability and predisposition to cancer (2-5). The MLH1 gene is frequently mutated in hereditary nonpolyposis colon cancer (HNPCC) (6). MLH1 also plays a role in meiotic recombination (7). 1.Modrich, P. (2006) J Biol Chem 281, 30305-9. 2.Seng, T.J. et al. (2008) Br J Cancer 99, 375-82. 3.Harley, I. et al. (2008) Gynecol Oncol 109, 384-7. 4.Mao, G. et al. (2008) J Biol Chem 283, 3211-6. 5.Hubner, R.A. and Houlston, R.S. (2007) J Natl Cancer Inst 99, 1490; author reply 1490-1. 6.Vasen, H.F. (2005) Fam Cancer 4, 219-25. 7.Argueso, J.L. et al. (2003) Mol Cell Biol 23, 873-86.
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