Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide-Like 3B Proteins (APOBEC3B)

APOBEC3B is a member of the cytidine deaminase gene family. Additionally we are shipping APOBEC3B Antibodies (42) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
APOBEC3B 9582 Q9UH17
APOBEC3B 315137  
APOBEC3B    
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Top APOBEC3B Proteins at antibodies-online.com

Showing 5 out of 5 products:

Catalog No. Origin Source Conjugate Images Quantity Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 50 Days
$6,749.58
Details
Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 60 Days
$9,626.73
Details
Wheat germ Human GST tag 10 μg 11 to 12 Days
$414.29
Details
Yeast Cricetulus longicaudatus His tag   1 mg 60 to 71 Days
$3,094.67
Details
Yeast Rat His tag   1 mg 60 to 71 Days
$3,197.33
Details

APOBEC3B Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,
,
Rat (Rattus)

Cricetulus longicaudatus

More Proteins for Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide-Like 3B (APOBEC3B) Interaction Partners

Human Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide-Like 3B (APOBEC3B) interaction partners

  1. Study reports structures of the A3B catalytic domain in a new crystal form that show alternative, yet still closed, conformations of active site loops. All-atom molecular dynamics simulations support the dynamic behavior of active site loops and recapitulate the distinct modes of interactions that maintain a closed active site.

  2. APOBEC3B in high-grade serous ovarian carcinoma is related to an active immune infiltrate. However, there is no evidence for APOBEC3B as a clinically relevant prognostic biomarker

  3. High APOBEC3B expression is associated with hepatocarcinogenesis and metastasis through novel deaminase-independent activity.

  4. The APOBEC3B protein can deaminate the cytosine bases at two sites whose mutant states are subject to high net realized selection intensities-PIK3CA E545K and E542K.

  5. results indicated a specific interaction of A3B with hnRNP A3 (heterogeneous nuclear ribonucleoprotein). This interaction was verified by co-immunoprecipitation and was found to be RNA-dependent. Furthermore, A3B and hnRNP A3 colocalized as evident from immunofluorescence analysis.

  6. results reveal the structural basis for DNA binding and relatively lower catalytic activity of A3B and provide opportunities for rational design of specific inhibitors to benefit cancer therapeutics

  7. It is the major target for C-to-T substitutions in the HPV genomes.

  8. These experiments combine to implicate the RB/E2F axis in promoting APOBEC3B transcription, yet they also suggest that the polyomavirus large T antigen RB-binding motif has at least one additional function in addition to RB inactivation for triggering APOBEC3B upregulation in virus-infected cells.

  9. This study reports preferred nucleotide sequences for A3B substrates, including optimized 4-mer oligonucleotides, and reveals a breadth of substrate recognition that includes DNA sequences known to be mutated in drug-resistant cancer clones.

  10. APOBEC3B upregulation and APOBEC mutation count can be used as novel predictive markers in guiding NSCLC checkpoint blockade immunotherapy.

  11. We identified genes harboring CNVs that are highly differentiated between PM and global populations, indicating that these genes are predominantly enriched in immune responses and defense functions, including APOBEC3A_B, beta-defensin genes, and CCL3L1, followed by other biological functions, such as drug and toxin metabolism and responses to radiation

  12. 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.

  13. results suggest that B-Myb-A3B contributes to DNA damage and could be targeted by inhibiting EGF receptor.

  14. 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

  15. 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.

  16. 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.

  17. review of current understanding of APOBEC3A and APOBEC3B biology in human papillomavirus Infection restriction, evolution, and associated cancer mutagenesis

  18. 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.

  19. Data show that the larger oligomeric state of APOBEC3B (A3B) inhibited its activity.

  20. APOBEC3B*c.783delG showed evidence of modest association with breast cancer and seemed to contribute to earlier onset of the disease.

Pig (Porcine) Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide-Like 3B (APOBEC3B) interaction partners

  1. Porcine endogenous retrovirus type C infectivity was strongly inhibited by poA3Z2-Z3, but it did not markedly reduce porcine endogenous retrovirus type B infectivity.

  2. These results strongly imply that human and porcine APOBEC3 could inhibit porcine endogenous retroviruses replication in vivo, thereby reducing the risk of infection of human cells in the context of pig-to-human xenotransplantation.

APOBEC3B Protein Profile

Protein Summary

This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. A hybrid gene results from the deletion of approximately 29.5 kb of sequence between this gene, APOBEC3B, and the adjacent gene APOBEC3A. The breakpoints of the deletion are within the two genes, so the deletion allele is predicted to have the promoter and coding region of APOBEC3A, but the 3' UTR of APOBEC3B. Two transcript variants encoding different isoforms have been found for this gene.

Gene names and symbols associated with APOBEC3B

  • apolipoprotein B mRNA editing enzyme catalytic subunit 3B (APOBEC3B)
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3B (Apobec3b)
  • A3B protein
  • APOBEC1L protein
  • Apobec3 protein
  • APOBEC3B protein
  • APOBEC3F protein
  • APOBEC3Z2 protein
  • APOBEC3Z3 protein
  • ARCD3 protein
  • ARP4 protein
  • bK150C2.2 protein
  • DJ742C19.2 protein
  • PHRBNL protein

Protein level used designations for APOBEC3B

DNA dC->dU-editing enzyme APOBEC-3B , cytidine deaminase , phorbolin 2 , phorbolin 3 , phorbolin-1-related protein , phorbolin-2/3 , probable DNA dC->dU-editing enzyme APOBEC-3B , apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B , apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D , DNA dC->dU-editing enzyme APOBEC3 , apolipoprotein B editing complex 3 , apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F , probable DNA dC->dU-editing enzyme APOBEC3 , apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3B

GENE ID SPECIES
9582 Homo sapiens
743891 Pan troglodytes
315137 Rattus norvegicus
100037939 Sus scrofa
100628312 Macaca mulatta
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