Analytical Data
-
Gene name
RHOV
- Application
-
Alternative Names
RHOV;ARHV;WRCH2;Rho-related GTP-binding Protein RhoV
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96L33
-
Expression Region
1-236aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPPRELS EAEPPPLRAP TPPPRRRSAP PELGIKCVLV GDGAVGKSSL IVSYTCNGYP ARYRPTALDT FSVQVLVDGA PVRIELWDTA GQEDFDRLRS LCYPDTDVFL ACFSVVQPSS FQNITEKWLP EIRTHNPQAP VLLVGTQADL RDDVNVLIQL DQGGREGPVP QPQAQGLAEK IRACCYLECS ALTQKNLKEV FDSAILSAIE HKARLEKKLN AKGVRTLSRC RWKKFFCFV
-
Molecular Weight
29 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 study of recombinant human ovalbumin (RHOV) proteins is rooted in the growing demand for safe and effective therapeutic proteins in the fields of immunology, vaccine development, and biotechnology. Ovalbumin, a major protein found in egg whites, serves as a model protein for understanding protein structure, expression, and post-translational modifications. The ability to produce RHOV through recombinant DNA technology allows researchers to investigate its immunological properties, making it a valuable tool for studying allergic responses and potential vaccine adjuvants. Additionally, the controlled production of RHOV facilitates the exploration of its structural characteristics and biological functions, opening avenues for various applications, including drug delivery systems and food allergy research. As the field of biosciences progresses, the exploration of RHOV not only enhances our comprehension of protein functionality but also supports advancements in therapeutic interventions and diagnostic tools.
