Recombinant Human Replication factor C subunit 1 (RFC1), partial
| Product Name | Recombinant Human Replication factor C subunit 1 (RFC1), partial |
|---|---|
| Description | The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA. Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair. |
| Synonyms | Activator 1 140 kda subunit |
| Host | E.coli |
| Molecular Weight | 14.8 kDa |
| Amino Acid Sequence | GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIRTMPGKKSKYEIA |
| Protein Length | Partial, 402-492aa |
| Tag | N-terminal 10xHis-tagged and C-terminal Myc-tagged |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| References |
"The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3' processing of mRNA." Lu Y., Riegel A.T. Gene 145:261-265(1994) |
| Background |
The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA. Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair. |
| Supplier | Cusabio |
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