Analytical Data
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Gene name
RFPL4B
- Application
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Alternative Names
RFPL4B; RNF211; Ret finger protein-like 4B; RING finger protein 211
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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
Q6ZWI9
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Expression Region
1-263 aa
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AA Sequence
MAKRLQAELS CPVCLDFFSC SISLSCTHVF CFDCIQRYIL ENHDFRAMCP LCRDVVKVPA LEEWQVSVLT LMTKQHNSRL EQSLHVREEL RHFREDVTLD AATASSLLVF SNDLRSAQCK KIHHDLTKDP RLACVLGTPC FSSGQHYWEV EVGEVKSWSL GVCKEPADRK SNDLFPEHGF WISMKAGAIH ANTHLERIPA SPRLRRVGIF LDADLEEIQF FDVDNNVLIY THDGFFSLEL LCPFFCLELL GEGESGNVLT ICP
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Molecular Weight
29.9 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
RFPL4B (RNA-binding motif protein, family member 4B) is a member of the RFPL protein family, which has garnered attention in recent years due to its potential roles in various biological processes, including regulation of RNA metabolism, cell proliferation, and differentiation. Alterations in RFPL4B expression have been implicated in several types of cancers and developmental disorders, highlighting its importance in both normal physiology and disease states. The protein is characterized by an RNA recognition motif (RRM), which is essential for its function in RNA binding and subsequent regulatory activities. Research has demonstrated that RFPL4B can interact with specific RNA targets, influencing gene expression and cellular responses. Despite these insights, the precise mechanisms by which RFPL4B exerts its effects at the molecular level remain poorly understood. Investigating the recombinant form of RFPL4B allows researchers to study its biochemical properties and functional roles in detail, providing a foundation for developing therapeutics that target RFPL4B-related pathways in diseases. Understanding the structure-function relationship of RFPL4B through recombinant protein studies may also reveal novel insights into its role in gene regulation and the cellular processes it governs, paving the way for advancements in molecular biology and medicine. Overall, the study of RFPL4B recombinant protein represents a crucial step toward deciphering the complex regulatory networks involving this protein and its implications in health and disease.
