Analytical Data
-
Gene name
HSPB11
- Application
-
Alternative Names
IFT25;C1orf41;HSPB11;Intraflagellar transport Protein 25 homolog
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y547
-
Expression Region
1-144aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMRKIDLCLSSEGSEVILATSSDEKHPPENI IDGNPETFWTTTGMFPQEFIICFHKHVRIERLVIQSYFVQTLKIEKSTSK EPVDFEQWIEKDLVHTEGQLQNEEIVAHDGSATYLRFIIVSAFDHFASVH SVSAEGTVVSNLSS
-
Molecular Weight
19 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
HSPB11, a member of the small heat shock protein (sHSP) family, has garnered significant attention in recent years due to its potential roles in cellular stress responses and neuroprotection. Research indicates that HSPB11 is involved in various critical biological processes, including protein folding, aggregation prevention, and apoptosis regulation. Its expression is often upregulated in response to thermal stress, oxidative stress, and other cellular insults, suggesting a protective function in maintaining cellular homeostasis. Furthermore, studies have linked HSPB11 to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and Alzheimer's disease, where it may contribute to the mitigation of toxic protein aggregation. The recombinant production of HSPB11 allows for detailed biochemical studies and offers insights into its structural properties and functional mechanisms. By exploring HSPB11 through recombinant protein techniques, researchers aim to elucidate its role in cellular stress response pathways and its potential as a therapeutic target. Understanding HSPB11's molecular interactions and cellular roles could pave the way for novel approaches in treating diseases characterized by protein misfolding and aggregation. Overall, further investigation into HSPB11 not only enhances our comprehension of protein homeostasis but also holds promise for developing therapeutic strategies for associated neurodegenerative conditions.
