Analytical Data
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Gene name
JUN
- Application
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Alternative Names
JUN；Transcription factor Jun
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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
P05412
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Expression Region
1-131aa
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AA Sequence
MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
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Molecular Weight
41.3 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
Related Products
Protein Description
The research on JUN recombinant proteins is primarily centered around understanding the role of the JUN proto-oncogene, a member of the AP-1 transcription factor family, in various biological processes, including cell proliferation, differentiation, and apoptosis. JUN plays a critical role in the regulation of gene expression in response to extracellular stimuli, such as growth factors and stress signals. Dysregulation of JUN has been implicated in several pathological conditions, including cancer, where its overexpression or aberrant activation contributes to tumorigenesis. Recombinant JUN proteins facilitate the study of its structural and functional properties, enabling researchers to explore the interaction of JUN with other protein partners and its regulatory mechanisms in cellular contexts. Additionally, the use of recombinant technology allows for the production of purified JUN proteins for biochemical assays and structural analysis, aiding in the development of potential therapeutic strategies targeting JUN-related pathways. Understanding the intricacies of JUN function through its recombinant forms can illuminate the underlying mechanisms of carcinogenesis and contribute to the discovery of novel cancer treatment options.
