Analytical Data
-
Gene name
BNIP3
- Application
-
Alternative Names
BNIP3；NIP3；BCL2/adenovirus E1B 19 kDa Protein-interacting Protein 3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q12983
-
Expression Region
1-194aa
-
AA Sequence
MSQNGAPGMQEESLQGSWVELHFSNNGNGGSVPASVSIYNGDMEKILLDAQHESGRSSSK SSHCDSPPRSQTPQDTNRASETDTHSIGEKNSSQSEEDDIERRKEVESILKKNSDWIWDW SSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSAEFLKVFLPSLLLSHLLAIGLG IYIGRRLTTSTSTF
-
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
BNIP3 (Bcl-2/adenovirus E1B 19 kDa interacting protein 3) is a member of the Bcl-2 family and plays a crucial role in regulating apoptosis and autophagy, contributing to cellular responses under stress conditions such as hypoxia and nutrient deprivation. Its unique ability to promote cell death while also facilitating autophagic processes has drawn significant interest in the fields of cancer research and neurodegenerative diseases. Abnormal expression of BNIP3 has been implicated in tumor progression, where it may help cancer cells survive in low-oxygen environments, leading to chemoresistance. Additionally, BNIP3's involvement in mitochondrial dynamics and its ability to induce mitophagy have implications in neurodegenerative disorders like Parkinson's and Alzheimer's disease, where mitochondrial dysfunction is a hallmark. The development of recombinant BNIP3 proteins has enabled the investigation of its functional mechanisms and interactions with other cellular pathways, providing insights into potential therapeutic targets. By studying BNIP3 in a controlled environment, researchers hope to elucidate its dual roles in cell survival and death, paving the way for novel strategies to manipulate BNIP3 activity in various diseases. This makes the recombinant BNIP3 protein a valuable tool for both basic research and potential clinical applications, as understanding its pathways could lead to innovative treatments for conditions where apoptosis and autophagy are dysregulated.
