Recombinant Human Dna Dc->Du-Editing Enzyme Apobec-3G (APOBEC3G) Protein (His-SUMO)

Name: Recombinant Human Dna Dc->Du-Editing Enzyme Apobec-3G (APOBEC3G) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07492P
Price: 1464.8 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Dna Dc->Du-Editing Enzyme Apobec-3G (APOBEC3G) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9HC16
Target Symbol	APOBEC3G
Species	Homo sapiens (Human)
Expression System	in vitro E.coli expression system
Tag	N-6His-SUMO
Target Protein Sequence	MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN
Expression Range	1-384aa
Protein Length	Full Length
Mol. Weight	62.4 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular 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.
Protein Families	Cytidine and deoxycytidylate deaminase family
Database References	HGNC: 17357 OMIM: 607113 KEGG: hsa:60489 STRING: 9606.ENSP00000385057 UniGene: Hs.660143
Tissue Specificity	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

Gene Functions References

It has been shown that HCMV has evolved mutational robustness against IFN-beta by limiting the presence of APOBEC3G hot spots in essential open reading frames of its genome. PMID: 30045985
We found that A3G regulates the expression of several cellular proteins, which influences the capacity of the host cell to replicate measles virus. PMID: 29925665
Low APOBEC3G expression is associated with HIV-1 replication. PMID: 29677220
study concludes that hA3G may restrict porcine endogenous retrovirus (PERV) by both deamination-dependent mechanisms and inhibition of DNA strand transfer during PERV reverse transcription. PMID: 29610985
two stem-loop structures within the 5'-untranslated region of A3G mRNA are crucial for translation inhibition by Vif in HIV-infected cells, and most Vif alleles neutralize A3G translation efficiently PMID: 27996044
DNA substrate selection by APOBEC3G PMID: 29596531
these findings indicate that A3G is associated with cervical intraepithelial neoplasia , suggesting its important roles in human papillomavirus-induced pathophysiological processes such as cervical intraepithelial neoplasia progression and viral elimination PMID: 28590025
These findings report genetic variants possibly associated with susceptibility to HIV-1 infection (CUL5 rs11212495, rs7103534, rs7117111) and partial viral load control (APOBEC3G rs2294367). PMID: 28302043
analysis indicated that IL-6 also increased the expression of A3B through JAK1/STAT3 signaling pathway, which formed a positive feedback to maintain the continuous expression of A3B and IL-6, and thereby promoted the prolonged non-resolving inflammation PMID: 28646470
The goal of this methods review is through example of our research on APOBEC3G, describe the application of cross-linking methods to characterize and quantify macromolecular interactions and their functional implications PMID: 26988126
Our results identify APOBEC3G as a new candidate biomarker for tumor-infiltrating T lymphocytes and favorable prognoses for HGSOC. PMID: 27016308
propose that APOBEC3G has the ability to induce T cell plasticity and modulate immune response. PMID: 27282578
The results show for the first time the nuclear translocation of A3G in activated-proliferating CD4(+) T cells. PMID: 26987686
Mouse mammary tumour virus only moderately susceptible to inhibition by the human APOBEC3G. PMID: 28809145
Data suggest that heat shock proteins, in particular Hsp90, stimulate APOBEC3-mediated DNA deamination activity toward hepatitis B viral DNA, suggesting a potential physiological role in mutagenesis/carcinogenesis and viral innate immunity; Hsp90 stimulates deamination activity of APOBEC3G, APOBEC3B, and APOBEC3C during co-expression in human liver HepG2 cells. PMID: 28637869
Study indicates that the A3G rs8177832 polymorphism is associated with a decreased risk of chronic hepatitis B virus infection and hepatocellular carcinoma (HCC), while the rs2011861 polymorphism is associated with an increased risk of HCC. PMID: 28127197
APOBEC3G through its variants rs6001417, rs8177832, and rs35228531, in this study interferes with HIV-1/HBV co-infection could be due the HIV-1 mono-infection in a population from Burkina Faso. PMID: 27449138
APOBEC3DE binds to itself, APOBEC3F, and APOBEC3G and antagonizes APOBEC3F and, to a lesser extent, APOBEC3G restriction of hepatitis B virus replication. PMID: 27289067
cyclin F functions as an intrinsic cellular regulator of HIV-1 Vif and has a negative regulatory effect on the maintenance of viral infectivity by restoring APOBEC3G expression. Gene Indexing Project Expand All Collapse All PMID: 28184007
These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication. PMID: 27439715
Here, the authors show that APOBEC3G polyubiquitination is essential for its HIV-1 vif-induced degradation. PMID: 27297094
DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315 PMID: 28381554
The findings suggest that APOBEC3G polymorphisms alone may not have significant predictive power for inferring genetic susceptibility to vertical transmission of HIV in children perinatally exposed to HIV PMID: 27245545
APOBEC3G binds viral RNA and DNA in vitro; this binding may constitute the basis of APOBEC3G antiviral activity. PMID: 28029777
an APOBEC3F/APOBEC3G hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif. PMID: 27881650
using novel human A3G transgenic mouse models that express varying levels of A3G as is seen in humans, this study clearly demonstrates that polymorphic vif alleles can have differential anti-A3G activity in vivo PMID: 27363431
thousands of mutation clusters introduced along primate evolution which exhibit features that strongly fit the known patterns of APOBEC3G mutagenesis. These results suggest that APOBEC3G-induced mutations have contributed to the evolution of all genomes PMID: 27056836
the effect of APOBEC3G over-expression upon AATF gene expression, was examined. PMID: 27611213
The results disclosed no association between the single nucleotide polymorphisms of APOBEC3G and susceptibility to HIV-1, or effects of these polymorphisms on the CD4(+) T cell count or clinical phase of disease. PMID: 27730383
APOBEC-3G serves as a suppressor of cervical cancer cell proliferation and invasion. PMID: 26722417
Findings support a role for APOBEC3G/F proteins in the generation of plasma drug-resistant minority human immunodeficiency virus type 1 variants (DRMVs). However, this role seems to be limited to a small subset of mutations and does not explain most of the DRMVs evaluated. PMID: 26482266
STAT3 plays an important role in IFN-induced A3G production, and HBsAg may correlated with poor response to IFN treatment PMID: 27003258
Atomic Force spectroscopy revealed two distinct binding modes by which A3G interacts with ssDNA. One mode requires sequence specificity, as demonstrated by stronger and more stable complexes with deaminase specific ssDNA than with nonspecific ssDNA. PMID: 26503602
results demonstrate that the up-regulation of A3G in pancreatic cancer cells induces anoikis resistance, and they provide novel insight into the mechanism by which A3G affects the malignant behavior of pancreatic cancer cells PMID: 26178819
Data show that restriction factor APOBEC3G (A3G) is susceptible to degradation by the HIV-1 Vif protein, whereas restriction factor APOBEC3B (A3B) is resistant to Vif. PMID: 26668372
This study demonstrates an association of rs6001417, rs8177832, and rs35228531 of APOBEC3G with HIV-1 infection in a population from Burkina Faso. PMID: 26741797
Results were consistent with Pokeweed antiviral protein activity inhibiting translation of Vif, which in turn reduces the effect of Vif to inactivate the host restriction factor APOBEC3G. PMID: 26275799
USF1 gene can take part in basal transcription regulation of the human A3G gene in hepatocyte, and the identified E-box represented a binding site for the USF1. PMID: 26772882
Incomplete APOBEC3G/F neutralization by a single Vif amino acid substitution. PMID: 26055363
This study identifies a new cellular complex, HDAC6/A3G, involved in the autophagic degradation of Vif, and suggests that HDAC6 represents a new antiviral factor capable of controlling HIV-1 infectiveness by counteracting Vif and its functions. PMID: 26105074
Human APOBEC3G C-terminal directly binds hepatitis C virus non-structural protein NS3 at its C-terminus. PMID: 25811715
The data predicts a mechanistic model of RNA inhibition of ssDNA binding to APOBEC3G in which competitive and allosteric interactions determine RNA-bound versus ssDNA-bound conformational states. PMID: 26424853
This study showed a high level of APOBEC3F/3G editing in HIV-2 sequences from antiretroviral-naive patients. PMID: 25985400
upregulated in the skin of Lichen planus patients PMID: 25384438
APOBEC3G is more efficient at mutating retroviral DNA than APOBEC3F. PMID: 26048885
A3G and A3F inhibit porcine endogenous retrovirus replication. PMID: 26016442
These results highlight that the N-terminal domain of the full length A3G protein has an important influence on its DNA sequence specificity and mutator activity. PMID: 25974865
Vif continues to protect HIV-1 from the deleterious effects of APOBEC3G, even after packaging of APOBEC3G has occurred. PMID: 25304135
The rather indiscriminate RNA binding characteristics of A3G and A3F promote functionality by enabling recruitment into a wide range of retroviral particles whose packaged RNA genomes comprise divergent sequences. PMID: 25590131
It may be concluded hepatitis B virus up-regulates HBD-3 and A3G expression in vivo and in vitro in placental trophoblast and lack of this up-regulation is possibly associated with intrauterine transmission of hepatitis B. PMID: 25196417

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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