Analytical Data
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Gene name
CER
- Application
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Alternative Names
CER；DAND4；Cerberus
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95813
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Expression Region
18-267aa
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AA Sequence
TRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ CKVKTEHEDG HILHAGSQDS FIPGVSA
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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
Protein Description
The study of recombinant proteins, particularly those derived from the CER (cysteinyl endopeptidase-related) family, has gained significant attention in recent years due to their potential biotechnological and therapeutic applications. CER proteins play crucial roles in various biological processes, including cell signaling, immune response, and protein catabolism. Their unique biochemical properties make them attractive candidates for various applications ranging from enzyme replacement therapies to biocatalysts in industrial processes. Advances in molecular biology techniques, such as genetic engineering and recombinant DNA technology, have facilitated the production of these proteins in heterologous systems, allowing for higher yields and easier purifications. However, the study of CER proteins is not without its challenges, as issues regarding protein folding, solubility, and post-translational modifications can impact their functional activity. Thus, understanding the structure-function relationships of CER proteins and optimizing their production conditions are vital for harnessing their full potential. As research progresses, the elucidation of their mechanisms of action and interactions with other biomolecules will pave the way for novel therapeutic strategies and innovative applications in biotechnology, ultimately contributing to advancements in medicine and industry.
