Analytical Data
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Gene name
ANKRD53
- Application
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Alternative Names
ANKRD53Ankyrin repeat domain-containing Protein 53
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N9V6
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Expression Region
1-343aa
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AA Sequence
MASAGSTARRAGSGSWHSERGEGRGARPQPTPSGSMQQANKVSLKATWTDAESKQPSQPLPDLADHLSAQATALARPRRPASLTPPRADPSPSKESDQTAIDQTAIGSYYQLFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQGQGCSVHFPFAFSPITPETLLWQDISLLSDCGFLWRRRELSF
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Molecular Weight
64.6 KDa
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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
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Protein Description
ANKRD53 is a protein associated with various cellular processes, including cell proliferation, differentiation, and DNA repair mechanisms. Research has indicated that ANKRD53 plays a crucial role in maintaining genomic stability, and its dysfunction has been linked to several cancers and neurodegenerative diseases. Given its significance in cellular pathways, the study of recombinant ANKRD53 proteins has gained traction in both basic and applied research. Scientists are particularly interested in elucidating the structure-function relationships of ANKRD53 to understand its molecular interactions and regulatory roles in signaling pathways. The production of recombinant ANKRD53 allows for in-depth investigations into its biochemical properties, post-translational modifications, and interaction partners. This research not only aims to clarify the mechanistic pathways involving ANKRD53 but also holds potential for therapeutic applications, such as targeted drug development and biomarker discovery. Furthermore, understanding how ANKRD53 contributes to disease mechanisms may pave the way for innovative strategies in cancer therapy and regenerative medicine, making it a pivotal focus in contemporary biomedical research.











