APOBEC3D/F Antibody - #DF4334
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*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF4334, RRID:AB_2836702.
Fold/Unfold
A3D; ABC3D_HUMAN; APOBEC3D; APOBEC3DE; APOBEC3E; Apolipoprotein B mRNA editing enzyme catalytic polypeptide like 3D; Apolipoprotein B mRNA editing enzyme catalytic polypeptide like 3E pseudogene; ARP6; bK150C2.9; BK150C2.9 protein; DNA dC >dU editing enzyme APOBEC 3D; DNA dC->dU-editing enzyme APOBEC-3D; hCG_41704; HCG41704, isoform CRA_b; Probable DNA dC->dU-editing enzyme APOBEC-3D; Apolipoprotein B mRNA editing enzyme, catalytic polypeptide like 3F; ARP8; DNA dC->dU-editing enzyme APOBEC-3F; Induced upon T cell activation; KA6;
Immunogens
Expressed in lymphoid organs. Also detected in non-lymphoid tissues including lung.
Q8IUX4 ABC3F_HUMAN:Widely expressed. Highly expressed in ovary.
- Q96AK3 ABC3D_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGPVLPKRQSNHRQEVYFRFENHAEMCFLSWFCGNRLPANRRFQITWFVSWNPCLPCVVKVTKFLAEHPNVTLTISAARLYYYRDRDWRWVLLRLHKAGARVKIMDYEDFAYCWENFVCNEGQPFMPWYKFDDNYASLHRTLKEILRNPMEAMYPHIFYFHFKNLLKACGRNESWLCFTMEVTKHHSAVFRKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLCYFWDTDYQEGLCSLSQEGASVKIMGYKDFVSCWKNFVYSDDEPFKPWKGLQTNFRLLKRRLREILQ
- Q8IUX4 ABC3F_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE
PTMs - Q96AK3/Q8IUX4 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| S46 | Phosphorylation | Uniprot | |
| K62 | Ubiquitination | Uniprot | |
| K347 | Ubiquitination | Uniprot | |
| K365 | Ubiquitination | Uniprot | |
| K368 | Ubiquitination | Uniprot |
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| T32 | Phosphorylation | Uniprot | |
| R136 | Methylation | Uniprot | |
| Y177 | Phosphorylation | Uniprot | |
| S216 | Phosphorylation | Uniprot |
Research Backgrounds
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR and non-LTR retrotransposons.
Cytoplasm. Cytoplasm>P-body.
Expressed in lymphoid organs. Also detected in non-lymphoid tissues including lung.
The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.
Belongs to the cytidine and deoxycytidylate deaminase family.
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Cytoplasm. Cytoplasm>P-body.
Widely expressed. Highly expressed in ovary.
Binds HIV-1 Vif. In the absence of Vif protein, specifically packaged into HIV-1 virions. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with AGO1, AGO2 and AGO3.
The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.
Belongs to the cytidine and deoxycytidylate deaminase family.
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