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

Name: Recombinant Mouse Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04805P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Single-Stranded Dna Cytosine Deaminase (AICDA) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9WVE0
Target Symbol	AICDA
Synonyms	Aicda; Aid; Single-stranded DNA cytosine deaminase; EC 3.5.4.38; Activation-induced cytidine deaminase; AID; Cytidine aminohydrolase
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDSLLMKQKKFLYHFKNVRWAKGRHETYLCYVVKRRDSATSCSLDFGHLRNKSGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVAEFLRWNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIGIMTFKDYFYCWNTFVENRERTFKAWEGLHENSVRLTRQLRRILLPLYEVDDLRDAFRMLGF
Expression Range	1-198aa
Protein Length	Full Length
Mol. Weight	31.5 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	KEGG: mmu:11628 STRING: 10090.ENSMUSP00000040524 UniGene: PMID: 29593215 MMSET promotes AICDA-mediated DNA breaks at the donor switch region during immunoglobulin class switch recombination. PMID: 29158395 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 findings suggest that activation of Tnf-Aicda axis and co-inhibitory signals to T cells in coordination with Th1-type immunity has critical roles in the immune response against Hepatitis B virus infection PMID: 28063995 the role of phosphorylation on AID serine38 in AID activity at the Immunoglobulin switch region and off-target Myc gene, is reported. PMID: 29122947 Class switching correlates with replication origin activation in immunoglobulin genes;R loops contribute to the specification of origins of replication; Origin activation is independent of AID and DNA breaks PMID: 27974207 The reduced expression of activation-induced cytidine deaminase (AID). PMID: 28407558 this study shows that enforced expression of Sox2 in splenic B cells severely inhibits AID expression and IgH class switch recombination PMID: 28188246 Aid loss in mice leads to expansion of myeloid cells and reduced erythroid progenitors resulting in anemia, with dysregulated expression of Cebpa and Gata1, myeloid/erythroid lineage-specific transcription factors PMID: 28077417 UNG deficiency reduces B cell clonal expansion in the germinal center in mice and blocks the proliferation of tumor B cells expressing AID. PMID: 27697833 Efficient chemoprotection of CDD and MDR1 transduced hematopoietic 32D as well as primary lin(-) cells was proven in the context of Ara-C and anthracycline application PMID: 26651614 this study indicate that inflammation-induced AID expression promotes skin cancer development independently of UV damage and suggest AID as a potential target for skin cancer therapeutics. PMID: 26974156 Molecular mechanism of Aid interaction with RNA-binding proteins, dimer formation and it's role in DNA-cleavage and recombination PMID: 26929374 DNA methylation dynamics of germinal center B cells are mediated by AID. PMID: 26365193 Demonstrate the importance of AID in generating an appropriate B1a cell response to pathogenic bacteria. PMID: 26456931 AID-induced mutations are prone to generate double-strand breaks PMID: 26263206 Unlike deletion of the AID C terminus, 3 of the substitution mutants reduce DNA double-strand breaks (DSBs) detected within the Sm region in splenic B cells undergoing class switch recombination . PMID: 26267846 Study demonstrates that intronic switch RNA acts in trans to target AID to S region DNA. AID binds directly to switch RNA through G-quadruplexes formed by the RNA molecules. PMID: 25957684 The effect of insertion of transcribed intronic S regions in a locus (Igkappa)strongly recruiting AICDA on class switch recombination is reported. PMID: 26146363 Study finds AID targets somatic hypermutation (SHM) hotspots within V exon and S region passengers at similar frequencies and that the normal SHM process frequently generates deletions, indicating that SHM and class-switch recombination employ the same mechanism. PMID: 26582132 Splice variants of activation induced deaminase (AID) do not affect the efficiency of class switch recombination in murine CH12F3 cells PMID: 25803053 genetic deficiency in spontaneously autoimmune B6.Nba2 mice impairs production of anti-nuclear antibodies, a hallmark of systemic lupus erythematosus PMID: 25634361 AID deficiency inhibits DSA-mediated aortic vasculopathy after aorta transplantation in mice. PMID: 25769064 HSP90 inhibitors indirectly target AID in vivo PMID: 25912253 class switch recombination is programmed to occur in a productive deletional orientation and does so via an unprecedented mechanism that involves in cis Igh organizational features in combination with frequent S-region DSBs initiated by AID PMID: 26308889 Observed an activity-dependent induction of BDNF exon IV mRNA expression, which correlated with reduced DNA methylation within the BDNF P4 promoter. Knockdown of AID disrupted these effects and inhibited BDNF exon IV mRNA expression. PMID: 25041363 These data suggest that Aid does not have crucial functions in DNA demethylation during induced pluripotent stem cell generation. PMID: 24718089 B cell Rab7 mediates induction of activation-induced cytidine deaminase expression and class-switching in T-dependent and T-independent antibody responses. PMID: 25740947 results elucidate the molecular basis of AID cytoplasmic retention, define its functional relevance and distinguish it from other mechanisms regulating AID. PMID: 25824822 miR-155 controls the outcome of the the germinal center reaction by modulating its initiation (Aicda) and termination (Socs1/p53 response). PMID: 25645925 AID target genes are enriched in chromatin modifications associated with active enhancers (such as H3K27Ac) and marks of active transcription (such as H3K36me3) in both fibroblasts and B cells PMID: 25512519 Chronic lung injury by constitutive expression of activation-induced cytidine deaminase leads to focal mucous cell metaplasia and cancer. PMID: 25659078 our results suggest a stringent and sophisticated control of Aicda by a novel IL-10/miR-155 PMID: 25381386 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 AICDA does not appear to be required for tumor development in the two virus-induced tumor mouse models. PMID: 24569264 IkappaB-zeta regulates TLR-mediated CSR by inducing AID PMID: 25124037 RNA exosome regulation of ncRNA recruits AID to single-strand DNA-forming sites of antisense and divergent transcription in the B-cell genome, thereby creating a link between ncRNA transcription and overall maintenance of B-cell genomic integrity PMID: 25119026 Results indicate a role for apurinic/apyrimidinic endonuclease (APE) 2 (Apex2) in the protection of germinal center (GC) cells from activation-induced cytidine deaminase (AID)-independent damage. PMID: 24935922 To have dominant negative (DN) function, AID lacking the C terminus (DeltaAID) must have deaminase activity, suggesting that its ability to induce double-strand breaks is important for the DN function. PMID: 24973444 Activation-induced deaminase-coupled DNA demethylation is not crucial for the generation of induced pluripotent stem cells. PMID: 24083501 GANP regulates the choice of DNA repair pathway by DNA-PKcs interaction in AID-dependent IgV region diversification. PMID: 24808370 findings suggest that S regions are preferred targets for AID and, aided by polypyrimidine tract binding protein-2, act as "sinks" to sequester AID activity from other genomic regions. PMID: 24879790 A domain of AID is required to link the DNA damage step with the subsequent repair during CSR as well as for chromosomal translocations, a collateral effect of class switch recombination. PMID: 24591601 Hypoxia within spheres together with loss of Zeb1 repression synergize to cause superinduction of Hif1a, which in turn leads to induction of the DNA demethylase Aid/Aicda, demethylation of the Oct4 promoter/enhancer and multipotency. PMID: 23554223 Murine Aicda(-/-) GC B cells accumulate as centrocytes and inefficiently generate plasma cells. PMID: 24244021 Fate mapping and AID reporter mice were used to determine if AID expression in the mouse extends beyond lymphocytes. PMID: 23861962 GANP-mediated chromatin modification promotes transcription complex recruitment and positioning at immunoglobulin variable loci to favour AID targeting. PMID: 23652018 Precise regulation of the Aicda promoter appears to depend on a coordinated balance of activities between enhancer and silencer elements. PMID: 23613851 studies identified a late step of reprogramming associated with methylation status, and implicated a secondary set of pluripotency network components; AID regulates this late step, removing epigenetic memory to stabilize the pluripotent state PMID: 23803762

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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.

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