Analytical Data
-
Gene name
env
- Application
-
Alternative Names
env；Envelope glycoProtein gp130
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P04578
-
Expression Region
33-511aa
-
AA Sequence
KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR
-
Molecular Weight
69.7 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 Env (envelope) proteins has gained significant attention due to their crucial role in the viral life cycle, particularly in the context of retroviruses such as HIV. Env proteins are responsible for mediating the entry of viruses into host cells by facilitating the fusion of viral and cellular membranes. This process is governed by the structural dynamics and conformational changes of Env, which can be influenced by various factors, including receptor interactions and the presence of neutralizing antibodies. Research has focused on understanding the molecular mechanisms of Env protein folding, trimerization, and the conformational states that enable viral entry. Furthermore, the variability of Env proteins among different strains poses challenges for vaccine development, as it necessitates a comprehensive understanding of the protein's antigenic properties. Recent advancements in structural biology, including cryo-electron microscopy and X-ray crystallography, have provided detailed insights into the architecture of Env proteins, facilitating the design of novel antiviral strategies. These studies aim to uncover potential targets for therapeutics and vaccines that can elicit broadly neutralizing responses against diverse viral strains, highlighting the importance of Env in both virology research and the broader field of infectious disease prevention.
