Reactive species
Human;Rat;Mouse;
Applications
IHC;IF;ELISA
Antibody type
Polyclonal Antibody
Protein name
RAD52 motif-containing protein 1
Immunogen
The antiserum was produced against synthesized peptide derived from human RDM1. AA range:118-167
Specificity
RDM1 Polyclonal Antibody detects endogenous levels of RDM1 protein.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
IHC: 1/100 - 1/300. ELISA: 1/5000.. IF 1:50-200
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
RDM1; RAD52B; RAD52 motif-containing protein 1; RAD52 homolog B
Background
This gene encodes a protein involved in the cellular response to cisplatin, a drug commonly used in chemotherapy. The protein encoded by this gene contains two motifs: a motif found in RAD52, a protein that functions in DNA double-strand breaks and homologous recombination, and an RNA recognition motif (RRM) that is not found in RAD52. The RAD52 motif region in RAD52 is important for protein function and may be involved in DNA binding or oligomerization. Alternatively spliced transcript variants encoding different isoforms have been reported. [provided by RefSeq, Jul 2008],
Function
caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,domain:C-terminal half (amino acids 134-284) contains cytoplasmic retention domains as well as determinants involved in its stress-induced nucleolar accumulation.,function:May confer resistance to the antitumor agent cisplatin. Binds to DNA and RNA.,induction:Heat-shock stress up-regulated mRNA expression of isoform 10 and isoform 11. Heat-shock stress down-regulated short N-terminal mRNA expression of isoform 2, isoform 4, isoform 6 and isoform 9.,similarity:Contains 1 RRM (RNA recognition motif) domain.,subcellular location:Isoform 1 is predominantly cytoplasmic. Isoform 3 and isoform 10 are predominantly nuclear and nucleolar. After treatment with proteasomal inhibitors and mild heat-shock stress, isoform 1, isoform 3, isoform 5, isoform 7, isoform 8 and
