Analytical Data
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Gene name
APOBEC3B
- Application
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Alternative Names
APOBEC3BDNA dC->dU-editing enzyme APOBEC-3B; A3B; EC 3.5.4.38; Phorbolin-1-related Protein; Phorbolin-2/3
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Species
Human
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Source
E. coli
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Tag
N-terminal His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UH17
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Expression Region
1-382aa
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AA Sequence
MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGV FRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFL SEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVY NEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYL CYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPA QIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQ MLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAILQ NQGN
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Molecular Weight
49.3kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
APOBEC3B is a member of the APOBEC (Apolipoprotein B mRNA Editing Enzyme Catalytic Polypeptide) family, which is known for its role in regulating RNA and DNA editing. Its primary function involves deaminating cytosine residues in single-stranded DNA, leading to mutations that can hinder viral replication and contribute to genomic diversity. A critical aspect of APOBEC3B research is its implication in cancer biology; overexpression of this enzyme has been linked to the accumulation of mutations in tumor DNA, thereby influencing tumorigenesis and cancer progression. Understanding the structural and functional characteristics of APOBEC3B, including its protein-protein interactions and regulatory mechanisms, is vital for elucidating its role in both antiviral defense and oncogenesis. Additionally, studies have indicated that this enzyme's activity can be modulated by various cellular factors, which positions it as a potential target for therapeutic interventions aimed at controlling viral infections or cancer development. The ongoing exploration of APOBEC3B, including the design and testing of recombinant proteins, aims to enhance our understanding of its diverse functions and pave the way for novel strategies in molecular medicine.
