Analytical Data
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Gene name
ZNF330
- Application
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Alternative Names
anti-NOA36; HSA6591; NOA36; NOA36; Nucleolar autoantigen 36; Nucleolar cysteine rich Protein; Nucleolar cysteine-rich Protein; Zinc finger autoantigen 330; Zinc finger Protein 330; ZN330_HUMAN; ZNF 330; ZNF330
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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
Q9Y3S2
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Expression Region
1-320 aa
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AA Sequence
MPKKKTGARK KAENRREREK QLRASRSTID LAKHPCNASM ECDKCQRRQK NRAFCYFCNS VQKLPICAQC GKTKCMMKSS DCVIKHAGVY STGLAMVGAI CDFCEAWVCH GRKCLSTHAC ACPLTDAECV ECERGVWDHG GRIFSCSFCH NFLCEDDQFE HQASCQVLEA ETFKCVSCNR LGQHSCLRCK ACFCDDHTRS KVFKQEKGKQ PPCPKCGHET QETKDLSMST RSLKFGRQTG GEEGDGASGY DAYWKNLSSD KYGDTSYHDE EEDEYEAEDD EEEEDEGRKD SDTESSDLFT NLNLGRTYAS GYAHYEEQEN
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Molecular Weight
36.2 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
ZNF330, a member of the Zinc Finger Protein family, is implicated in various biological processes, including gene regulation, cell differentiation, and development. Its unique structure, characterized by multiple zinc finger motifs, allows it to bind DNA and interact with other proteins, thus influencing transcriptional activities. Recent studies have suggested that ZNF330 may play a role in certain diseases, including cancers, due to its regulatory functions in vital cellular pathways. The recombinant expression of ZNF330 protein has become an important area of research, enabling scientists to investigate its functional properties and potential therapeutic applications. By producing ZNF330 in a controlled laboratory environment, researchers can explore its interaction with DNA and other nuclear factors, providing insights into its role in gene expression modulation. Furthermore, understanding the mechanisms by which ZNF330 exerts its effects can aid in uncovering novel targets for drug development, particularly in oncology. As such, the study of ZNF330 and its recombinant protein form is crucial for elucidating the intricate networks of gene regulation and for advancing potential clinical applications.
