Recombinant Human Probable DNA dC->dU-editing enzyme APOBEC-3B (APOBEC3B)

Code CSB-YP887025HU
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Source Yeast
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Code CSB-EP887025HU
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Source E.coli
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Code CSB-EP887025HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP887025HU
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Source Baculovirus
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Code CSB-MP887025HU
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Source Mammalian cell
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Product Details

Purity
≥85% (SDS-PAGE)
Target Names
APOBEC3B
Uniprot No.
Alternative Names
APOBEC3BDNA dC->dU-editing enzyme APOBEC-3B; A3B; EC 3.5.4.38; Phorbolin-1-related protein; Phorbolin-2/3
Species
Homo sapiens (Human)
Expression Region
1-251
Target Protein Sequence
MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVY FKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISA ARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAF LHRTLKEILRLRIFSVAFTAAMRSCASWTWFLLCSWTRPRSTGSLGSSPGAPASPGAVPG KCVRSFRRTHT
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. 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 against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.
Gene References into Functions
  1. the knockdown of APOBEC3B by clustered regularly interspaced short palindromic repeats/CRISPR associated protein 9 resulted in reduced proliferation and enhanced chemosensitivity of glioma cells. Thus, APOBEC3B contributes to glioma progression and may be a future target for therapeutic intervention. PMID: 30226610
  2. results suggest that B-Myb-A3B contributes to DNA damage and could be targeted by inhibiting EGF receptor. PMID: 28276478
  3. APOBEC3A/B deletion was associated with young age at diagnosis among the cancer cases for both cancer forms (lung cancer: P = 0.02; dominant model and prostate cancer PMID: 29140415
  4. These studies combine to indicate that APOBEC3B promotes drug resistance in breast cancer and that inhibiting APOBEC3B-dependent tumor evolvability may be an effective strategy to improve efficacies of targeted cancer therapies. PMID: 27730215
  5. Our results provide evidence that APOBEC3B can interact with HBV core protein and edit HBV DNAs during reverse transcription. These data suggest that APOBEC3B exerts multifaceted antiviral effects against HBV. PMID: 29129707
  6. review of current understanding of APOBEC3A and APOBEC3B biology in human papillomavirus Infection restriction, evolution, and associated cancer mutagenesis PMID: 28825669
  7. This study found that A3B C-terminal domain shows higher activity toward its target sequence in short ssDNA and efficiently deaminates a target sequence located near the center of ssDNA. PMID: 28952713
  8. Data show that the larger oligomeric state of APOBEC3B (A3B) inhibited its activity. PMID: 28981865
  9. APOBEC3B*c.783delG showed evidence of modest association with breast cancer and seemed to contribute to earlier onset of the disease. PMID: 28062980
  10. Data show that APOBEC3B (A3B) expression is inversely related to p53 status in different cancer types and demonstrate that this is due to a direct and pivotal role for p53 in repressing A3B expression. PMID: 28977491
  11. Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation have been reported. PMID: 28575276
  12. A lysine-free derivative of human APOBEC3B was constructed and shown to be indistinguishable from the wild-type enzyme in DNA cytosine deamination, HIV-1 restriction, and nuclear localization activities. PMID: 28841445
  13. exposures to relevant environmental factors might induce APOBEC3A or APOBEC3B expression above genotoxic levels and initiate tumorigenesis in a tissue-specific manner in the right cellular environment where ssDNA is available PMID: 27643540
  14. APOBEC3B expression increased the incorporation of genomic uracil, invoked DNA damage response (DDR) biomarkers and caused cell cycle arrest. PMID: 28535155
  15. The findings demonstrate that covalently-closed circular DNA levels are significantly lower in hepatocellular carcinoma tissues, and that the lower levels are likely to stem in part from up-regulation of APOBEC3B. PMID: 27310677
  16. 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
  17. APOBEC3B mRNA levels are significantly higher in breast cancer metastases as compared to the corresponding estrogen receptor-positive primary tumors. PMID: 28141868
  18. tumour-infiltrating immune cells may be an important feature of breast cancers arising in women with APOBEC3B germline deletion, and that this may be of particular interest in Asian women where the germline deletion is more common. PMID: 27233495
  19. the APOBEC3B deletion polymorphism has neither a prognostic nor a predictive value for breast cancer patients. PMID: 27552096
  20. Single-strand DNA-specific cytidine deaminase APOBEC3B (A3B) damages tRNA genes at 1000-fold higher efficiency than other non-tRNA genomic regions in Saccharomyces cerevisiae. A3B-induced lesions in tRNA genes were predominantly located on non-transcribed strand, while no transcriptional strand bias was observed in protein coding genes. It suggests transcription-dependent mechanism for A3B-induced tRNA gene hypermutation PMID: 28351647
  21. These data link oncogene, loss of tumour suppressor gene and drug-induced replication stress with APOBEC3B activity, providing new insights into how cytidine deaminase-induced mutagenesis might be activated in tumourigenesis and limited therapeutically. PMID: 27634334
  22. High APOBEC3B mRNA expression was related to the aggressive phenotypes of breast cancer, high frequency of TP53 mutation and poor prognosis, especially in ER-positive tumors. PMID: 27977754
  23. crystal structures of human APOBEC3A and a chimera of human APOBEC3B and APOBEC3A bound to ssDNA at 3.1-A and 1.7-A resolution, respectively. PMID: 27991903
  24. the classical NF-kappaB pathway is responsible for activation of A3B mRNA expression. PMID: 27577680
  25. Collectively, these results indicate that human papillomavirus 16 E6 induces upregulation of APOBEC3B through increased levels of TEADs, highlighting the importance of the TEAD-APOBEC3B axis in carcinogenesis. PMID: 28077648
  26. APOBEC3B mRNA expression was higher in OSCCs than in controls. APOBEC3B protein expression was high in both OSCCs and normal samples. PMID: 27818121
  27. The expression of APOBEC3B in breast cancer was higher than in non-cancerous tissues and was related to the lymph node metastasis and nuclear grade. PMID: 26476745
  28. results suggest that the APOBEC3A/3B deletion polymorphism is not significantly associated with cancer risk in our study population PMID: 27155849
  29. This suggests that APOBEC3B deletion may attenuate innate cellular immunity against HIV-1 and thus confer the host persistence for HIV infection. PMID: 27522954
  30. APOBEC3B expression was increased in some population of tumor cells of drug resistant cell lines. PMID: 27044816
  31. APOBEC3A and APOBEC3B preferentially deaminate the lagging strand template during DNA replication. PMID: 26832400
  32. Data indicate that SIVmac239 Vif protein efficiently degrades human DNA cytosine deaminase APOBEC3B protein (huA3B). PMID: 26544511
  33. 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
  34. APOBEC3B is required for regulation of gene expression by ERalpha and acts by causing C-to-U deamination at ERalpha binding regions. PMID: 26411678
  35. These results suggest that functional potential of APOBEC3B and APOBEC3C involved in cancer mutagenesis is associated with estrogen receptor status. PMID: 26682542
  36. The APOBEC3B deletion polymorphism was found to be associated with HBV, HCV, TTV, and T. gondii co-infection in Indonesian HIV-infected individuals. PMID: 26305823
  37. Germline variant and deletion polymorphism in APOBEC3B gene are not associated with breast cancer risk. PMID: 26320772
  38. APOBEC3B expression was correlated with unfavorable prognosis in patients with gastric cancer. PMID: 26191203
  39. APOBEC3B expression is an independent predictor of recurrence in patients with ccRCC, and the prognostic value is most prominent in those with low-risk disease. PMID: 26051357
  40. report the first structures of the APOBEC3B catalytic domain in multiple crystal forms. These structures reveal a tightly closed active site conformation and suggest that substrate accessibility is regulated by adjacent flexible loops PMID: 26416889
  41. APOBEC3B overexpression and Fhit-loss induced DNA damage are independent events that, when occurring together, result in a significantly increased frequency of APOBEC-induced mutations that drive cancer progression. PMID: 25401976
  42. The N-terminal domain of A3B and at least three residues involved in DNA binding by the A3Bc catalytic domain contribute to the A3B attenuation of the double stranded DNA break phenotype. PMID: 26384561
  43. Multiple experimental approaches combined demonstrate direct transcriptional upregulation of APOBEC3B by a signal transduction pathway involving the classical protein kinase C isoform protein kinase Ca and the noncanonical NF-kB transcription factor RELB. PMID: 26420215
  44. APOBEC3A-mediated mutagenesis is much more frequent than APOBEC3B because APOBEC3A itself is highly proficient at generating DNA breaks. PMID: 26258849
  45. This study defines and characterizes the catalytic domain of human APOBEC3B (A3B) enzyme. PMID: 26281709
  46. DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B. PMID: 26195824
  47. Study provides evidence that APOBEC3B is overexpressed in chondrosarcoma tissues and cell lines and interferes with RUNX3 transcription. PMID: 25176183
  48. High APOBEC3B is associated with the pathogenesis of primary effusion lymphoma. PMID: 25650088
  49. results indicate that E6 activates the A3B promoter through the distal and proximal regions, and that ZNF384 is required for the proximal-region-mediated activation of A3B PMID: 25800874
  50. These studies suggest a model in which high-risk human papillomavirus E6 causes derepression of APOBEC3B gene transcription, leading to a mutator phenotype that explains the observed cytosine mutation biases in papillomavirus positive cancers. PMID: 25538195

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Subcellular Location
Nucleus.
Protein Families
Cytidine and deoxycytidylate deaminase family
Tissue Specificity
Expressed at high and moderate levels in peripheral blood leukocytes, spleen, testes, heart, thymus, prostate and ovary. Also expressed at low levels in several other tissues.
Database Links

HGNC: 17352

OMIM: 607110

KEGG: hsa:9582

STRING: 9606.ENSP00000327459

UniGene: Hs.226307

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