Analytical Data
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Gene name
RFPL1
- Application
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Alternative Names
RFPL1; RFPL1L; RNF78; Ret finger protein-like 1; RING finger protein 78
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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
O75677
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Expression Region
1-317 aa
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AA Sequence
MKRLSLVTTN RLSPHGNFLP LCTFPLAVDM AALFQEASSC PVCSDYLEKP MSLECGCAVC FKCINSLQKE PHGEDLLCCC CSMVSQKNKI RPSWQLERLA SHIKELEPKL KKILQMNPRM RKFQVDMTLD ADTANNFLLI SDDLRSVRSG CITQNRQDLA ERFDVSICIL GSPRFTCGRH YWEVDVGTST EWDLGVCRES VHRKGRIHLT TERGFWTVSL RDGSRLSAST VPLTFLFVDR KLQRVGIFLD MGMQNVSFFD AEGGSHVYTF RSVSAEEPLH LFFAPPSPPN GDKSVLSICP VINPGTTDAP VHPGEAK
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Molecular Weight
35.4 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
RFPL1, or "RNA binding protein with specific E3 ligase activity 1," has emerged as a significant subject of study in the realms of molecular biology and cancer research. This protein, part of the RFPL family, is known for its unique role in regulating RNA metabolism and gene expression, which is crucial for maintaining cellular homeostasis. Research indicates that RFPL1 is implicated in various cellular processes, including cell proliferation, apoptosis, and differentiation. Its dysregulation has been linked to several types of cancer, suggesting that RFPL1 may function as an oncogene or tumor suppressor, depending on the context. Investigating RFPL1's structure, function, and interactions with other cellular molecules is essential for understanding its contributions to cancer development and progression. Moreover, the identification of RFPL1 as a potential biomarker or therapeutic target could lead to innovative strategies for cancer diagnosis and treatment. Continued research into RFPL1 and its role in the regulatory networks of RNA and protein interactions holds promise for uncovering novel insights into cancer biology and the development of new therapeutic approaches. Overall, the study of RFPL1 represents a vital avenue of exploration that bridges molecular mechanisms with clinical implications.
