ARG54117

anti-RAD9A antibody

anti-RAD9A antibody for Western blot,Immunoprecipitation and Human,Mouse,Rat,Monkey

Gene Regulation antibody

Overview

Product Description Mouse Monoclonal antibody recognizes RAD9A
Tested Reactivity Hu, Ms, Rat, Mk
Tested Application IP, WB
Host Mouse
Clonality Monoclonal
Isotype IgG2b
Target Name RAD9A
Antigen Species Human
Immunogen Purified recombinant human RAD9A protein fragments expressed in E.coli
Conjugation Un-conjugated
Alternate Names DNA repair exonuclease rad9 homolog A; Cell cycle checkpoint control protein RAD9A; EC 3.1.11.2; RAD9; hRAD9

Application Instructions

Application Suggestion
Tested Application Dilution
IPAssay-dependent
WB1:500
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
Observed Size 55 kDa

Properties

Form Liquid
Purification Affinity purified
Buffer PBS (pH 7.4), 0.2% Sodium azide and 50% Glycerol
Preservative 0.2% Sodium azide
Stabilizer 50% Glycerol
Concentration 4.5 mg/ml
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 19367 Mouse RAD9A

GeneID: 5883 Human RAD9A

Swiss-port # Q99638 Human Cell cycle checkpoint control protein RAD9A

Swiss-port # Q9Z0F6 Mouse Cell cycle checkpoint control protein RAD9A

Gene Symbol RAD9A
Gene Full Name RAD9 homolog A (S. pombe)
Background Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair.The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C(RFC)clamp loader complex.Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair(LP-BER).The 9-1-1 complex stimulates DNA polymerase beta(POLB)activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds;endonuclease FEN1 cleavage activity on substrates with double,nick,or gap flaps of distinct sequences and lengths;and DNA ligase I(LIG1)on long-patch base excision repair substrates.The 9-1-1 complex is necessary for the recruitment of C12orf32/RHINO to sites of double-stranded breaks(DSB)occurring during the S phase.RAD9A possesses 3'->5' double stranded DNA exonuclease activity.Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.
Function Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex. [UniProt]
Cellular Localization Nucleus
Research Area Gene Regulation antibody
Calculated MW 43 kDa
PTM Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.