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The antibody against RPA1 was raised in rabbit using the Human RPA1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.
The antibody against RPA1 was raised in rabbit using the Human RPA1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.
$600.00
| Cat.No | ADC-47327A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | RPA1 |
| Form | Liquid | Species Reactivity | Human, Mouse, Rat |
| Isotype | IgG | Storage Buffer | 50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.1% Sodium Azide |
| Purification Method | Antigen affinity purified | Conjugate | Non-conjugated |
| Application | ELISA, WB | Storage | Upon receipt |
| Immunogen Description | Human RPA1 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P27694 |
Uniprot Id
P27694
Target Species
Human
Target Name
RPA1
Target Full Name
Replication protein A 70 kDa DNA-binding subunit
Target Function
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.
Target Subcellular Location
Nucleus. Nucleus, PML body.
Target Protein Families
Replication factor A protein 1 family
Target Research Area
Epigenetics and Nuclear Signaling
Target Synonyms
Dmrpa1; Drosophila Replication Protein A; DRPA; HSSB; Human single stranded DNA binding protein ; MST075; MSTP075; p70; REPA1; Replication factor A; Replication factor A protein 1; Replication protein A 70 kDa DNA-binding subunit; Replication protein A 70kDa DNA binding subunit; Replication protein A1 70kDa; Replication protein A1; RF A; RF-A protein 1; RFA; RFA1_HUMAN; RP A; RP-A p70; RPA 70; RPA; rpa1; Single stranded binding protein 70; Single-stranded DNA-binding protein
Target Background
This gene encodes the largest subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The nucleoprotein complex protects the single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. This subunit contains four oligonucleotide/oligosaccharide-binding (OB) domains, though the majority of ssDNA binding occurs in two of these domains. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which ssDNA binding domains are utilized. The different binding modes differ in the length of DNA bound and in the proteins with which it interacts, thereby playing a role in regulating different genomic maintenance pathways.
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