Mouse Monoclonal RPA32/RPA2 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Rat, Human samples.
IgM
Mouse
Preservative: 0.05% Sodium azide
Constituents: 99.85% PBS, 0.1% BSA
Liquid
Monoclonal
WB | IHC-P | ICC/IF | |
---|---|---|---|
Human | Expected | Tested | Tested |
Rat | Expected | Expected | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info 1/500 | Notes - |
Species Human | Dilution info 1/500 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/10.00000 - 1/100.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
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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. Also plays 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. RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542).
REPA2, RPA32, RPA34, RPA2, Replication protein A 32 kDa subunit, RP-A p32, Replication factor A protein 2, Replication protein A 34 kDa subunit, RF-A protein 2, RP-A p34
Mouse Monoclonal RPA32/RPA2 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Rat, Human samples.
IgM
Mouse
Preservative: 0.05% Sodium azide
Constituents: 99.85% PBS, 0.1% BSA
Liquid
Monoclonal
MA34
Affinity purification Protein G
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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All lanes: Western blot - Anti-RPA32/RPA2 antibody [MA34] (ab111161) at 1/500 dilution
All lanes: Purified RPA32/RPA2 protein
Predicted band size: 29 kDa
Immunofluorescent analysis of RPA32/RPA2 in HeLa cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/200 overnight at 4°C and incubated with a DyLight-488 conjugated secondary antibody. RPA32/RPA2 staining (green) F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Images were taken at 60X magnification.
Immunofluorescent analysis of RPA32/RPA2 in A431 cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/200 overnight at 4°C and incubated with a DyLight-488 conjugated secondary antibody. RPA32/RPA2 staining (green) F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Images were taken at 60X magnification.
Immunofluorescent analysis of RPA32/RPA2 in C6 cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/200 overnight at 4°C and incubated with a DyLight-488 conjugated secondary antibody. RPA32/RPA2 staining (green) F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Images were taken at 60X magnification.
Immunohistochemistry was performed on cancer biopsies of deparaffinized Human breast carcinoma tissue. To expose target proteins heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer and microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature and probed with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/20 or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
Immunohistochemistry was performed on normal biopsies of deparaffinized Human kidney tissue. To expose target proteins heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer and microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature and probed with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/20 or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
Immunohistochemistry was performed on normal biopsies of deparaffinized Human tonsil tissue. To expose target proteins heat induced antigen retrieval was performed using 10mM sodium citrate (pH6.0) buffer and microwaved for 8-15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature and probed with a RPA32/RPA2 monoclonal antibody (ab111161) at a dilution of 1/20 or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.
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