Analytical Data
-
Gene name
KBTBD11
- Application
-
Alternative Names
KBTBD11; Kelch repeat and BTB domain-containing protein 11; Chronic myelogenous leukemia-associated protein; Kelch domain-containing protein 7B
-
Species
Human
-
Source
Baculovirus
-
Tag
N-StrepⅡ;N-8*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O94819
-
Expression Region
E2-P623
-
Protein Length
Full Length
-
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
KBTBD11, a member of the kelch repeat and BTB (BR-C, tTA, Bric a brac) domain containing proteins, has garnered attention due to its potential role in cellular processes such as protein degradation and intracellular signaling. Research indicates that KBTBD11 may function as an E3 ubiquitin ligase, implicating it in the regulation of ubiquitylation pathways, which are critical for maintaining cellular homeostasis and regulating various biological functions. Dysregulation of these pathways has been associated with several diseases, including cancer and neurodegenerative disorders. Thus, the study of KBTBD11 and its recombinant protein forms is crucial for understanding its functional mechanisms and pathological implications. Furthermore, exploring the structural properties and interactions of KBTBD11 can provide insights into its role in the ubiquitin-proteasome system and facilitate the development of targeted therapeutic strategies for diseases linked to its dysfunction. Ongoing investigations aim to elucidate KBTBD11’s structure-function relationships and its contribution to cellular signaling networks, highlighting its importance as a potential biomarker or therapeutic target in disease contexts.
