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>   首页   >   产品   >   一抗   >   其他   >   REV1 Antibody - C-terminal region   

REV1 Antibody - C-terminal region

Rabbit Polyclonal Antibody

     
  • 1 - REV1 Antibody - C-terminal region AI16092

    Host: Rabbit
    Target Name: REV1
    Sample Tissue: Fetal Lung lysates
    Antibody Dilution: 1.0μg/ml
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession Q9UBZ9
Other Accession XP_005264024
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 138248 Da
Additional Information
Gene ID 51455
Alias Symbol REV1, REV1L,
Other Names DNA repair protein REV1, 2.7.7.-, Alpha integrin-binding protein 80, AIBP80, Rev1-like terminal deoxycytidyl transferase, REV1, REV1L
Format Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Reconstitution & Storage Add 50 &mu, l of distilled water. Final Anti-REV1 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
PrecautionsREV1 Antibody - C-terminal region is for research use only and not for use in diagnostic or therapeutic procedures.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name REV1 (HGNC:14060)
Synonyms REV1L
Function Bifunctional protein involved in the maintenance of genome stability through translesion DNA synthesis (TLS) and antibody diversification via somatic hypermutation (PubMed:16263170, PubMed:23143872). Functions as a molecular adapter protein at stalled DNA replication, coordinating polymerases recruitment, selection, and switching, in a manner independent of its deoxycytidyl transferase activity (PubMed:23143872). At the site of DNA lesion, recruits and mediates the switch between low-fidelity inserter DNA polymerases, such as POLK, that incorporate nucleotides opposite lesions and the extender DNA polymerase zeta complex which continues DNA synthesis from distorted primer termini (PubMed:23143872). In vitro, acts as a template-dependent deoxycytidyl transferase that preferentially incorporates deoxycytidine residues from dCTP to the 3'-end of a DNA primer opposite apurinic/apyrimidinic (AP) site, uracil, undamaged DNA templates (G > A > C > T) and a variety of damaged DNA templates (PubMed:10536157, PubMed:11278384, PubMed:38612916). Opposite template guanine, efficiently incorporates not only dCMP but also non- complementary dGMP and dTMP, with lower efficiency for dAMP, demonstrating low fidelity on undamaged DNA (PubMed:10536157, PubMed:11711549, PubMed:38612916). This catalytic activity has been implicated in somatic hypermutation, likely achieved by incorporation of deoxycytidine opposite abasic sites, generated at cytidines via activation-induced deoxycytidine deaminase (AID)-mediated deamination and uracil DNA glycosylase (UNG) activity, respectively (PubMed:16263170). In addition, exhibits a 5'-deoxyribose-5-phosphate lyase activity in vitro, though its necessity in vivo is not confirmed (By similarity).
Cellular Location Nucleus. Note=In response to replication stress, is recruited to stalled DNA replication through recognition of monoubiquitinated PCNA, and accumulates in nuclear foci in a process facilitated by FAAP20 binding (PubMed:22266823). Nuclear foci localization likely reflects the recruitment of REV1 to DNA lesions in response to replication stress, and depends on its ubiquitin-binding motif (UBM) domains (PubMed:22266823).
Tissue Location Ubiquitous.
Research Areas

BACKGROUND

Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.

REFERENCES

Lin W.,et al.Nucleic Acids Res. 27:4468-4475(1999).
Gibbs P.E.M.,et al.Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000).
Masuda Y.,et al.J. Biol. Chem. 276:15051-15058(2001).
Murakumo Y.,et al.J. Biol. Chem. 276:35644-35651(2001).
Ota T.,et al.Nat. Genet. 36:40-45(2004).

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