Analytical Data
-
Gene name
codA
- Application
-
Alternative Names
codA；Collagen alpha-1(XIII) chain
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P25524
-
Expression Region
2-427aa
-
AA Sequence
SNNALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHVDVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLESGINVCFGHDDVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKVIASTQPAQTTVYLEQPEAIDYKR
-
Molecular Weight
49.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Protein Description
CodA (cytidine deaminase) is an enzyme that plays a crucial role in the conversion of cytidine and its derivatives into uridine, a process that has significant implications in various biological pathways, including nucleic acid metabolism and regulation. The study of CodA recombinants focuses on its potential applications in biotechnology and synthetic biology, particularly in the development of novel therapeutic strategies and biosensors. Recent advances in molecular biology techniques, such as CRISPR and directed evolution, have enabled researchers to engineer CodA for enhanced activity and specificity. This has opened new avenues for utilizing CodA in chemical synthesis, particularly in the production of modified nucleotides that could serve as valuable tools in gene editing and other molecular applications. Additionally, CodA’s ability to degrade harmful cytidine analogs presents opportunities for targeted cancer therapies. Understanding the structural and functional dynamics of CodA through recombinant protein studies can provide deeper insights into its mechanisms and interactions within cellular systems, ultimately leading to innovative solutions in health and environmental applications. The exploration of CodA's properties, coupled with advances in protein engineering, underscores its potential as a versatile catalyst in both basic research and applied sciences.
