Analytical Data
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Gene name
RHOF
- Application
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Alternative Names
ARHF; FLJ20247; Ras homolog gene family member F (in filopodia); Ras homolog gene family member F; Rho F; Rho family GTPase Rif; Rho in filopodia; Rho related GTP binding protein RhoF; Rho-related GTP-binding protein RhoF; Rhof; RHOF_HUMAN; RIF
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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
Q9HBH0
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Expression Region
1-208 aa
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AA Sequence
MDAPGALAQT AAPGPGRKEL KIVIVGDGGC GKTSLLMVYS QGSFPEHYAP SVFEKYTASV TVGSKEVTLN LYDTAGQEDY DRLRPLSYQN THLVLICYDV MNPTSYDNVL IKWFPEVTHF CRGIPMVLIG CKTDLRKDKE QLRKLRAAQL EPITYMQGLS ACEQIRAALY LECSAKFREN VEDVFREAAK VALSALKKAQ RQKKRRLC
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Molecular Weight
23.6 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
Recombinant proteins, such as those produced by the Recombination of Homologous DNA Fragments (RHOF) method, have garnered significant interest in the fields of biotechnology and pharmaceutical research. These proteins are created using advanced genetic engineering techniques, enabling the production of high-purity proteins with specific biological functions. The study of RHOF recombinant proteins is particularly relevant because they can be leveraged for various applications, including therapeutic agents, vaccines, and diagnostic tools. The ability to manipulate and express exquisite protein structures has paved the way for innovations in treating diseases and understanding complex biological processes. Moreover, RHOF technology facilitates the rapid development of proteins by allowing scientists to combine genetic materials from different sources, which can lead to the creation of novel synthetic proteins that mimic or enhance natural processes. This method capitalizes on the advances in molecular biology and has the potential to overcome some limitations faced by traditional protein production methods, such as low yield and purity. As researchers continue to explore the vast capabilities of RHOF recombinant proteins, they are opening doors to new treatments for diseases ranging from cancer to infectious diseases, highlighting the profound impact that this technology can have on health and medicine. The ongoing research in this area emphasizes the significance of recombinant proteins in modern science, reflecting a growing recognition of their role in developing next-generation biopharmaceuticals and improving public health outcomes globally.
