Analytical Data
-
Gene name
hlb
- Application
-
Alternative Names
hlb；Protein HLB1
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P09978
-
Expression Region
35-330aa
-
AA Sequence
ESKKDDTDLKLVSHNVYMLSTVLYPNWGQYKRADLIGQSSYIKNNDVVIFNEAFDNGASDKLLSNVKKEYPYQTPVLGRSQSGWDKTEGSYSSTVAEDGGVAIVSKYPIKEKIQHVFKSGCGFDNDSNKGFVYTKIEKNGKNVHVIGTHTQSEDSRCGAGHDRKIRAEQMKEISDFVKKKNIPKDETVYIGGDLNVNKGTPEFKDMLKNLNVNDVLYAGHNSTWDPQSNSIAKYNYPNGKPEHLDYIFTDKDHKQPKQLVNEVVTEKPKPWDVYAFPYYYVYNDFSDHYPIKAYSK
-
Molecular Weight
35.7 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
HLB (hydrophilic-lipophilic balance) recombinant proteins have gained significant attention in the field of biochemistry and biotechnology due to their potential applications in drug delivery, biomaterials, and therapeutic agents. These proteins are engineered to possess specific properties that balance water-loving (hydrophilic) and fat-loving (lipophilic) characteristics, making them versatile for various applications, especially in nanotechnology and medical fields. Researchers are exploring the mechanisms by which HLB influences protein behavior, as it affects solubility, stability, and interactions with cell membranes. Furthermore, the ability to tailor the hydrophilic and lipophilic properties through genetic modification opens up possibilities for designing proteins that can improve drug solubility and bioavailability, enhance targeted delivery systems, and develop new therapeutic strategies for complex diseases. The study of HLB recombinant proteins is crucial for creating more efficient and effective biopharmaceuticals, thereby addressing the challenges associated with traditional drug delivery systems. As research continues, the integration of HLB characteristics into protein design will likely pave the way for innovative solutions in medical treatments and other scientific advances.
