Analytical Data
-
Gene name
BNIP3L
- Application
-
Alternative Names
Adenovirus E1B19K-binding protein B5 BCL2/adenovirus E1B 19KDA protein-interacting protein 3A NIP3-like protein X Short name: NIP3L
-
Species
Human
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O60238
-
Expression Region
1-219aa
-
Molecular Weight
25.9 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
BNIP3L, also known as BCL2/adenovirus E1B 19-kDa interacting protein 3-like, is a member of the BNIP family of proteins, which are known to play crucial roles in regulating cellular responses to stress, particularly in the context of apoptosis and autophagy. Research on BNIP3L has gained momentum due to its significant involvement in various physiological and pathological processes, including cancer progression, neurodegenerative diseases, and ischemic injury. The protein exerts its functions primarily through modulating mitochondrial dynamics and cellular metabolism. Notably, BNIP3L has been implicated in promoting autophagy under hypoxic conditions, making it particularly relevant in cancer biology where hypoxia is a common feature of solid tumors. Moreover, its interaction with key proteins involved in apoptosis and autophagy pathways highlights its potential as a therapeutic target. Recent studies have focused on characterizing the structural and functional aspects of recombinant BNIP3L, providing insights into its mechanism of action and interactions with other cellular components. As the understanding of BNIP3L's roles in cellular homeostasis and dysregulation grows, it offers promising avenues for developing innovative strategies in treating diseases associated with dysfunctional autophagy and apoptosis. Overall, BNIP3L's exploration not only enhances our knowledge of cell survival mechanisms but also paves the way for novel therapeutic interventions in cancer and other related disorders.
