|Application ||WB, IHC-P, E|
|Other Accession||NP_068594, 13399304|
|Calculated MW||46408 Da|
|Application Notes||APOBEC3G antibody can be used for detection of APOBEC3G by Western blot at 5 µg/mL. Antibody can also be used for immunohistochemistry starting at 1 µg/mL.|
|Other Names||APOBEC3G Antibody: A3G, ARCD, ARP9, ARP-9, CEM15, CEM-15, MDS019, bK150C2.7, dJ494G10.1APOBEC-related cytidine deaminase, APOBEC-related protein, apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G|
|Target/Specificity||APOBEC3G; APOBEC3G antibody will also detect the APOBEC3F isoform.|
|Reconstitution & Storage||APOBEC3G antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||APOBEC3G Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent 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 simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, P-body. Note=Mainly cytoplasmic. Small amount are found in the nucleus During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF|
|Tissue Location||Expressed in spleen, testes, ovary and peripheral blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive peripheral blood mononuclear cells, and several tumor cell lines; no expression detected in permissive lymphoid and non-lymphoid cell lines. Exists only in the LMM form in peripheral blood-derived resting CD4 T-cells and monocytes, both of which are refractory to HIV-1 infection. LMM is converted to a HMM complex when resting CD4 T-cells are activated or when monocytes are induced to differentiate into macrophages. This change correlates with increased susceptibility of these cells to HIV-1 infection.|
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Provided below are standard protocols that you may find useful for product applications.
APOBEC3G Antibody: The Apoliprotein B mRNA-editing, enzyme-catalytic, polypeptide-like (APOBEC) 3 is a multi-isoform member of the cytidine deaminase family of enzymes that act on monomeric nucleoside and nucleotide substrates. Similar to TRIM5α which targets incoming retroviral capsids, APOBEC3 plays a major role in cellular defense against retroviral infection as at least two isoforms, APOBEC3G and to a lesser extent APOBEC3F, can be incorporated HIV-1 virions and induce hypermutation in the newly synthesized viral DNA and thus destabilize the viral genome. This innate mechanism of retroviral resistance is counteracted by the HIV-1 Vif protein by inducing the ubiquitization and degradation of APOBEC3G; a single amino acid substitution (D128K) blocks APOBEC3G depletion without affecting its inhibitory activity.
Jarmuz A, Chester A, Bayliss J, et al. An anthropoid-specific locus of Orphan C to U RNA-editing enzymes on chromosome 22. Genomics 2002; 79:285-96.
Stremlau M, Owens CM, Perron MJ, et al. The cytoplasmic body component TRIM5a restricts HIV-1 infection in Old World monkeys. Nature 2004; 427:848-53.
Bieniasz PD. Intrinsic immunity: a front-line defense against viral attack. Nat Immunol. 2004; 5:1109-15.
Sheehy AM, Gaddis NC, Choi JD, et al. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002; 418:646-50.
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