Analytical Data
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Gene name
BNIP3L
- Application
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Alternative Names
BNIP3L；BNIP3A；BNIP3H；NIX；BCL2/adenovirus E1B 19 kDa Protein-interacting Protein 3-like
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60238
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Expression Region
43-130aa
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AA Sequence
SSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSH CDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKE
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Molecular Weight
35 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 BCL2 family of proteins and plays a crucial role in regulating programmed cell death and autophagy. Research on BNIP3L has gained significant attention due to its involvement in various cellular processes, particularly under stress conditions such as hypoxia and nutrient deprivation. Studies indicate that BNIP3L interacts with mitochondria and modulates mitochondrial dynamics, contributing to cellular survival and death decisions. The protein's dual function in promoting autophagy while inhibiting apoptosis highlights its potential as a therapeutic target in cancer, neurodegenerative diseases, and ischemic injuries. Furthermore, the expression levels of BNIP3L can influence tumorigenesis, with alterations linked to cancer progression and resistance to therapies. Understanding the precise mechanisms by which BNIP3L operates at the molecular level may unveil novel strategies for disease intervention and therapeutic development. As research continues to elucidate the multifaceted roles of BNIP3L, the generation of recombinant BNIP3L proteins will support biochemical studies aimed at characterizing its interactions and functions, potentially leading to insights into how modulation of BNIP3L activity can combat various diseases. Thus, the study of BNIP3L and its recombinant forms is pivotal for advancing our knowledge of cellular homeostasis and disease pathogenesis.
