Recombinant Full Length Human APOBEC3C Protein, C-Flag-tagged
Cat.No. : | APOBEC3C-2141HFL |
Product Overview : | Recombinant Full Length Human APOBEC3C Protein, fused to Flag-tag at C-terminus, was expressed in Mammalian cells. |
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Description : | 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. |
Source : | Mammalian cells |
Species : | Human |
Tag : | Flag |
Form : | 25 mM Tris HCl, pH 7.3, 100 mM glycine, 10% glycerol. |
Molecular Mass : | 22.6 kDa |
AA Sequence : | MNPQIRNPMKAMYPGTFYFQFKNLW EANDRDETWLCFTVEGIKRRSVVSW KTGVFRNQVDSETHCHAERC FLSWFCDDILSPNTKYQVTWYTSWS PCPDCAGEVAEFLARHSNVNLTIFT ARLYYFQYPCYQEGLRSLSQ EGVAVEIMDYEDFKYCWENFVYNDN EPFKPWKGLKTNFRLLKRRLRESLQ TRTRPLEQKLISEEDLAANDILDYK DDDDKV |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining. |
Stability : | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : | Store at -80 centigrade. |
Concentration : | >50 ug/mL as determined by microplate BCA method. |
Preparation : | Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. |
Gene Name : | APOBEC3C apolipoprotein B mRNA editing enzyme catalytic subunit 3C [ Homo sapiens (human) ] |
Official Symbol : | APOBEC3C |
Synonyms : | A3C; PBI; ARP5; ARDC2; ARDC4; APOBEC1L; bK150C2.3 |
Gene ID : | 27350 |
mRNA Refseq : | NM_014508.3 |
Protein Refseq : | NP_055323.2 |
MIM : | 607750 |
UniProt ID : | Q9NRW3 |
Products Types
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APOBEC3C-359H | Recombinant Human APOBEC3C Protein, His (Fc)-Avi-tagged | +Inquiry |
APOBEC3C-1574H | Recombinant Human APOBEC3C protein | +Inquiry |
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APOBEC3C-362R | Recombinant Rhesus monkey APOBEC3C Protein, His-tagged | +Inquiry |
◆ Lysates | ||
APOBEC3C-95HCL | Recombinant Human APOBEC3C cell lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (16)
Ask a questionResearch on APOBEC3C involves techniques such as gene expression analysis, protein assays, next-generation sequencing, immunohistochemistry, and cell-based assays. These techniques help understand its expression, protein-protein interactions, and functional consequences.
There is limited evidence suggesting that APOBEC3C can induce DNA mutations in human cells. However, its mutational activity may be weaker compared to other APOBEC3 proteins.
APOBEC3C shares structural similarities with other APOBEC3 proteins but has distinct functional characteristics. It has been found to have weaker antiviral activity than some other members, such as APOBEC3A and APOBEC3G.
APOBEC3C has been shown to have activity against retroviruses like HIV-1 and other related viruses. However, its antiviral activity against other viruses is not well-characterized.
Currently, there is no direct evidence linking APOBEC3C to any specific human diseases. However, it is possible that dysregulation or mutations in APOBEC3C could play a role in virus-related diseases or cancer development.
The regulation of APOBEC3C expression is not well-studied. However, similar to other APOBEC3 family members, it is likely regulated at the transcriptional level by various factors and signaling pathways.
APOBEC3C has been reported to interact with certain proteins involved in antiviral defense and DNA repair pathways, such as APOBEC3G, A3G mRNA-binding protein, and RAD52. These interactions suggest possible functional crosstalk between different proteins in these pathways.
APOBEC3C, like other APOBEC3 proteins, acts as a host innate immune defense against viral infections. By deaminating viral DNA or RNA, it disrupts viral replication or leads to the degradation of viral genetic material.
There is limited information available regarding APOBEC3C's role in drug resistance. Further research is needed to understand its potential involvement in this process.
As of now, there are no specific inhibitors or activators known for APOBEC3C. Further research is needed to identify molecules that can modulate its activity.
Currently, there are no specific ongoing research studies or clinical trials focused solely on APOBEC3C. However, as more is understood about its functions and relevance in human diseases, it may become a subject of future investigations.
Although not extensively studied, APOBEC3C mutations or dysregulation could potentially contribute to cancer development or progression. Some studies have shown an association between elevated APOBEC3C expression and certain types of cancer.
Targeting APOBEC3C for therapeutic interventions is still an area of active research. Modulation of its activity or expression could potentially be explored as a strategy against specific viral infections or virus-associated diseases.
APOBEC3C is expressed at low levels in various normal tissues, such as testis, lung, and liver. However, its expression pattern and physiological functions in normal tissues are not well-characterized.
Currently, there is limited evidence suggesting APOBEC3C as a potential biomarker for certain cancers. However, further research is needed to validate its diagnostic or prognostic value.
Studies have identified genetic variations or single-nucleotide polymorphisms (SNPs) in the APOBEC3C gene. However, their functional implications and potential association with diseases are still not well-understood.
Customer Reviews (4)
Write a reviewI highly recommend the APOBEC3C protein for a wide range of research applications.
The APOBEC3C protein's robustness and stability have contributed significantly to the success of my experiments, enabling precise and reproducible measurements.
Its ability to preserve structural integrity and facilitate high-resolution imaging has greatly enhanced my understanding of protein complexes and their interactions.
Furthermore, the APOBEC3C protein has demonstrated great utility in protein electron microscopy structure analysis.
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