Analytical Data
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Gene name
ZNF414
- Application
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Alternative Names
ZNF414Zinc finger Protein 414
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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
Q96IQ9
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Expression Region
1-312 aa
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AA Sequence
MEEKPSGPIP DMLATAEPSS SETDKEVLSP AVPAAAPSSS MSEEPGPEQA ATPPVWERGG AGGMQQGSSP APDSCQPGPG PSPGLTSIVS GTSEDLRPPR RRPPPGKQIP CSSPGCCLSF PSVRDLAQHL RTHCPPTQSL EGKLFRCSAL SCTETFPSMQ ELVAHSKLHY KPNRYFKCEN CLLRFRTHRS LFKHLHVCAE HAQSPAPPPP PALDREPPAP ERPPEVDPAS APGLPFPLLE PFTTPAPAPT GPFLPYLNPA PFGLSPPRLR PFLAAAPGPP ASSAAVWKKS QGAGSSPRRP QGGSDAPSGA CR
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Molecular Weight
32.7 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
ZNF414, a member of the zinc finger protein family, has garnered significant interest in recent years due to its potential roles in transcriptional regulation and cellular processes. Research indicates that ZNF414 is involved in various biological functions, including cell differentiation, proliferation, and response to stress. Given its structural features, particularly the presence of multiple zinc finger motifs, ZNF414 is thought to interact with specific DNA sequences, influencing gene expression patterns that may contribute to developmental processes and disease mechanisms. The exploration of ZNF414 as a recombinant protein has become increasingly relevant as scientists seek to elucidate its biological functions and regulatory pathways. By expressing ZNF414 in a recombinant system, researchers can produce large quantities of the protein for in-depth studies, including functional assays, protein-protein interactions, and potential therapeutic applications. Understanding the precise role of ZNF414 in cellular dynamics could shed light on its involvement in pathologies such as cancer or genetic disorders, thereby providing insights that could lead to novel diagnostic and therapeutic strategies. As such, the study of ZNF414 recombinant protein not only enriches our understanding of zinc finger proteins but also opens avenues for innovative research in molecular biology and medicine.
