Analytical Data
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Gene name
TRIM28
- Application
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Alternative Names
E3 SUMO-protein ligase TRIM28 (EC:6.3.2.-)KRAB-associated protein 1 ;KAP-1KRAB-interacting protein 1 ;KRIP-1Nuclear corepressor KAP-1RING finger protein 96Tripartite motif-containing protein 28
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13263
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Expression Region
22-291aa
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Molecular Weight
55.8 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
TRIM28, also known as KAP1 (KRAB-associated protein 1), is a member of the tripartite motif (TRIM) protein family, which plays critical roles in various cellular processes including transcriptional regulation, DNA damage response, and chromatin remodeling. It has been identified as a crucial co-repressor in the regulation of gene expression, particularly in embryonic development and stem cell maintenance. The TRIM28 protein interacts with several key transcription factors and epigenetic modifiers, forming complex regulatory networks that govern gene silencing and activation. Recent studies have highlighted its involvement in various pathological conditions, including cancer and viral infections, further emphasizing its potential as a therapeutic target. Understanding the mechanisms by which TRIM28 is regulated and functions at the molecular level is essential for elucidating its role in health and disease. Research on TRIM28 recombinant proteins has gained momentum as scientists aim to develop specific inhibitors or modulators that could interfere with its function, paving the way for novel therapeutic strategies. This growing interest underscores the importance of TRIM28 in biomedical research, as it may provide insights into fundamental biological processes and lead to new approaches for treating diseases linked to aberrant gene regulation.











