Analytical Data
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Gene name
ZNF9
- Application
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Alternative Names
CCHC-type zinc finger nucleic acid binding protein. Cellular nucleic acid-binding protein. CNBP. Zinc finger protein 9
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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
P62633
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Expression Region
1-170 aa
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AA Sequence
MSSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA
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Molecular Weight
44.44 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
ZNF9 (Zinc Finger Protein 9) is a crucial protein implicated in various cellular processes, including transcriptional regulation, cell differentiation, and response to stress. Research on ZNF9 has gained momentum due to its association with several human diseases, particularly its role in myotonic dystrophy type 2 (DM2), a genetic disorder characterized by muscle wasting and insulin resistance. The protein features an array of zinc finger domains, which facilitate its interaction with DNA and other proteins, thereby influencing gene expression. Given its potential therapeutic implications, the recombination and characterization of ZNF9 protein have become a significant focus of molecular biology studies. Researchers aim to elucidate its structural properties, functional mechanisms, and interaction networks to provide insights into its role in cellular pathophysiology. The recombinant ZNF9 protein serves as a valuable tool for studying these aspects in vitro and in vivo, offering opportunities for developing novel therapeutic strategies for diseases associated with ZNF9 dysregulation. Through these investigations, a deeper understanding of the molecular underpinnings of ZNF9-related disorders may lead to innovative treatments and interventions.
