Recombinant Human Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc)

Name: Recombinant Human Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11224P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9GZX7
Target Symbol	AICDA
Synonyms	Activation induced cytidine deaminase; Activation induced deaminase; Activation-induced cytidine deaminase; AICDA; AICDA_HUMAN; AID; ARP 2; ARP2; CDA 2; CDA2; Cytidine aminohydrolase; HIGM2; Integrated into Burkitt's lymphoma cell line Ramos
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL
Expression Range	1-198aa
Protein Length	Full Length
Mol. Weight	28.0 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.
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	Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
Subcellular Location	Nucleus. Cytoplasm.
Protein Families	Cytidine and deoxycytidylate deaminase family
Database References	HGNC: 13203 OMIM: 605257 KEGG: hsa:57379 STRING: 9606.ENSP00000229335 UniGene: PMID: 30081731 induction of AID expression would result in chromosomal translocations in the process of differentiation from B cell derived induced pluripotent stem cells. PMID: 28490810 The distribution of AID and A3s in the epithelial cells as well as germinal centres. PMID: 29343743 patients with AS expressed significantly higher levels of sv2 than HC. TNFi treatment restored the gene expression of the AID variants (FL, sv1, and sv2) in patients with AS. Therefore pre-existing TNFalpha-induced AID expression in B cells may play a role in the pathogenesis of AS. PMID: 28959900 we reported high AID, low miR-181b and high miR-155 expression in de novo adult B-ALL patients. Univariate high AID or low miR-181b expression was an unfavorable prognostic factor. High AID with low miR-181b or with low miR-155 expression is better in predicting unfavorable OS than univariate factor. High AID with low miR-181b and low miR-155 expression confers worst prognosis. PMID: 28140712 AID expression was increased in chronic lymphocytic leukemia patients with del17p or del11q who have poor prognosis. PMID: 28388279 Results indicate activation-induced cytidine deaminase (AICDA) as a driver of epigenetic heterogeneity in B-cell lymphomas with potential significance for other tumors with aberrant expression of cytidine deaminases. PMID: 29335468 The binding and catalytic behavior of purified AID was tested on DNA/RNA hybrid substrates bearing either random sequences or GC-rich sequences simulating Ig S regions. AID exhibited a higher affinity for binding DNA/RNA hybrid substrates made of S region sequences, than any other DNA substrates. In the absence of any other cellular processes or factors, AID itself favors binding and mutating S-region DNA/RNA hybrids. PMID: 29161581 Expression of human AID or increased oxidative stress induces DNA breaks within human chromosomal translocation fragile zones. PMID: 29220655 Data implicate intrinsic preference of AID for structured substrates and uncover the importance of G4 recognition and oligomerization of AID in class switch recombination. PMID: 28757211 the His130Pro mutation allows the enzyme to retain its mutagenic activity and would prevent the interaction of AID with specific cofactors required for class switch recombination but not for somatic hypermutation. Thus, there would be no contradiction between maintaining the catalytic and mutagenic activity of AID and the presence of function defects at the genomic level. PMID: 27716525 The authors found that the viral epsilon RNA and C-terminus of AID are required for AID-mediated hepatitis B virus RNA reduction. PMID: 28779685 silencing of AID in human bone marrow cells skews differentiation toward myelomonocytic lineage. However, in contrast to Tet2 loss, Aid loss does not contribute to enhanced HSC self-renewal or cooperate with Flt3-ITD to induce myeloid transformation. Genome-wide transcription and differential methylation analysis uncover the critical role of Aid as a key epigenetic regulator PMID: 28077417 AID protein is expressed in a large proportion of Philadelphia chromosome-positive B-cell acute lymphoblastic leukemia cases at levels detectable by immunohistochemistry. PMID: 26980048 These data, showing the direct targeting and induction of functional AID by EBNA3C, suggest a novel role for EBV in the etiology of B cell cancers, including endemic Burkitt lymphoma PMID: 27217538 These findings indicated that TNF-alpha-induced AID expression is involved with class switch recombination in cancer. PMID: 25849121 Finnish founder allele causing HIGM2 identified. PMID: 27142677 Structural analysis of AID protein required in immunoglobulin diversification has been reported. PMID: 27258794 this study reports a case of growth hormone deficiency with an autosomal recessive Hyper-immunoglobulin M syndrome by phenotype and genotype, with a novel mutation in AICDA that has not been reported formerly PMID: 27789066 We also report that AID activity results in epigenetic, genetic and genomic damage in fallopian tube epithelial cells PMID: 26936395 AICDA/APOBEC family of cytidine deaminases is significant in innate immunity, as it restricts numerous viruses, including HBV, through hypermutationdependent and independent mechanisms. (Review) PMID: 26398702 DNA methylation dynamics of germinal center B cells are mediated by AID. PMID: 26365193 Mutations in activation-induced cytidine deaminase is associated with indolent chronic lymphocytic leukaemia. PMID: 26638776 Data suggest novel mechanism in innate immunity allows cytokine TGF-beta to restrict viral circular DNA in hepatocyte nuclei via innate immunity; AID deaminates circular DNA of hepatitis B virus leading to DNA degradation; mechanism depends on UNG. PMID: 26867650 The high levels of memory and activated B cells and follicular helper T cells were positively associated with the progression of immunoglobulin A nephropathy. This may be mediated by the overexpression of AID, which is potentially regulated by IL21. PMID: 26166388 identify AID derivatives that accelerate somatic hypermutation with minimal impact on viability, which will be useful tools for engineering genes and proteins by iterative mutagenesis and selection PMID: 26355458 High expression of activation-induced cytidine deaminase is associated with diffuse large B cell lymphoma. PMID: 26077666 AID mutations leading to AID deficiency are the most frequent underlying molecular basis of hyper IgM syndrome in consanguineous Tunisian patients. PMID: 26545377 Studies indicate that gene conversion mediated by activation-induced cytidine deaminase (AID) has been found to contribute to generation of the primary antibody repertoire. PMID: 26537386 aberrant expression of AID may reflect continuous B cell activation and sustained survival signals in HCV-related CV patients. PMID: 26219420 Surges in ERK activity induced by extracellular cues enhance Arp2/3-mediated actin polymerization to generate protrusion power phases sufficient to promote sustained cell motility. PMID: 25990957 Data show that microRNAs miR-155 and miR-16 downregulate activation-induced cytidine deaminase (AID) and transcription factor E47 in B Cells through binding of the 3'-untranslated regions. PMID: 26223652 Data indicate that both the amount and intensity of the activation-induced cytidine deaminase (AID) protein expression increased with the progression from precancerous to cancerous lesions in pancreatic ductal adenocarcinoma (PDAC) tissues. PMID: 26113087 B cells hijack to supply ssDNA substrates for AID to mutate at immunoglobulin V regions during somatic hypermutation. PMID: 24923561 HSP90 inhibitors indirectly target AID in vivo PMID: 25912253 findings suggest that AID has a role in the development of oral epithelial dysplasia and promotes progression of oral cancer PMID: 24351917 hnRNP K and hnRNP L may serve as A1CF-like cofactors in AID-mediated class switch recombination and somatic hypermutation PMID: 25902538 Activation-induced cytidine deaminase (AID)-induced mutagenic U:G mismatches in DNA may be a fundamental and common cause of mutations in B-cell malignancies. PMID: 25486549 In yeast, AID and the catalytic domain of APOBEC3G preferentially mutate transcriptionally active genes within narrow regions, 110 base pairs in width, fixed at RNA polymerase initiation sites. PMID: 25237741 There was no significant association between the previously reported genetic variant of AICDA gene and the development of Common variable immunodeficiency or selective IgA deficiency PMID: 23731676 demonstrates that intensity of malaria transmission correlates with AID expression levels in the presence of Epstein-Barr virus PMID: 25099163 Study reports that the majority of detectable AID off-target activity in a variety of mouse and human lymphoid or nonlymphoid cell types occurs within focal regions of overlapping sense/antisense transcription within intragenic super enhancers. PMID: 25483776 AID activity and its relationship to chromosome folding and the B cell regulome was studied; find that AID-mediated lesions occur predominantly within B cell super-enhancers and regulatory clusters; further show that the structural and transcriptional features of these domains help explain AID tumorigenic activity in the B cell compartment of mice and humans. PMID: 25483777 data demonstrate that AID is active in CLL in vivo and thus, AID likely contributes to clonal evolution of CLL. PMID: 25179679 analysis of a possible association between AID expression and BRAF mutation in melanoma PMID: 24684646 Results show that both AID mRNA levels and DNA-cytosine deamination activities follow the same general pattern of increase and decline after stimulation in the two genetic backgrounds. PMID: 25154417 DNA repair pathways which are in vitro activated by AID-induced lesions are reminiscent of those found during AID-induced in vivo immunoglobulin diversification. PMID: 24349193 Results show that activation induced cytidine deaminase (AID) expression may be associated with deletions in patients with chronic lymphocytic leukemia (CLL). PMID: 23662991 AID lacking the C terminus is impaired in its ability to recruit nonhomologous end joining repair factors, resulting in accumulation of double-strand breaks that undergo aberrant resection. PMID: 24973444 findings reveal additional functions for AID in innate immune defense against KSHV with implications for a broader involvement in innate immunity to other pathogens. PMID: 24244169

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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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Recombinant Human Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc)

Recombinant Human Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc)

Product Overview

Target Details

FAQs