Recombinant Human Bcl2/Adenovirus E1B 19 Kda Protein-Interacting Protein 3-Like (BNIP3L) Protein (His)

Name: Recombinant Human Bcl2/Adenovirus E1B 19 Kda Protein-Interacting Protein 3-Like (BNIP3L) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10712P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) BNIP3L.

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Product Overview

Description	Recombinant Human Bcl2/Adenovirus E1B 19 Kda Protein-Interacting Protein 3-Like (BNIP3L) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O60238
Target Symbol	BNIP3L
Synonyms	Adenovirus E1B19k binding protein B5; Adenovirus E1B19K-binding protein B5; BCL2/adenovirus E1B 19 kd protein interacting protein 3a; BCL2/adenovirus E1B 19 kDa protein interacting protein 3A; BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like; BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A; BCL2/adenovirus E1B 19kDa interacting protein 3 like; BNI3L_HUMAN; BNIP3a; BNIP3H; BNIP3L; BNIP3L protein; NIP3 like protein X; NIP3-like protein X; NIP3L; NIX
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
Expression Range	1-219aa
Protein Length	Full Length
Mol. Weight	25.9kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.
Subcellular Location	Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane; Single-pass membrane protein. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
Protein Families	NIP3 family
Database References	HGNC: 1085 OMIM: 605368 KEGG: hsa:665 STRING: 9606.ENSP00000370003 UniGene: Hs.131226

Gene Functions References

The results demonstrate that Nix can serve as an alternative mediator of mitophagy to maintain mitochondrial turnover, identifying Nix as a promising target for neuroprotective treatment in PINK1/Parkin-related Parkinson's disease. PMID: 28281653
Here the authors present evidence for phosphorylation-driven regulation of the Nix:LC3B interaction. Isothermal titration calorimetry and NMR indicate a ~100 fold enhanced affinity of the serine 34/35-phosphorylated Nix LC3-interacting region (LIR) to LC3B and formation of a very rigid complex compared to the non-phosphorylated sequence. PMID: 28442745
p75(NTR) and NIX may play critical roles in intracerebral hemorrhage-induced neuronal apoptosis in vitro and in vivo. PMID: 27726026
Data suggest that targeting BNIP3L protein in wild-type p53 tumor suppressor colon cancer cells is an anticancer strategy activating iron depletion signaling and the mitophagy-related cell death pathway. PMID: 26517689
regulates mitophagy during hypoxia, whereas NIX is required for mitophagy during development of the erythroid lineage. PMID: 25753537
Nix protein positively regulates NF-kappaB activation in gliomas PMID: 22984526
mitochondrial ROS and NIX are essential factors for Mieap-induced accumulation of lysosome-like organelles within mitochondria PMID: 21264228
Nix functions as an autophagy receptor, which mediates mitochondrial clearance after mitochondrial damage and during erythrocyte differentiation PMID: 20010802
NIX binds to TSAP6 in tumor cells and has a role in apoptosis PMID: 12606722
The proapoptotic factor Nix is a highly regulated effector of growth during terminal erythroid maturation. PMID: 12663450
Bnip3L, capable of attenuating tumorigenicity, mediates p53-dependent apoptosis under hypoxia. PMID: 15607964
NIX is required for the selective elimination of mitochondria, however, because mitochondrial clearance, in the absence of NIX, is arrested at the stage of mitochondrial incorporation into autophagosomes and autophagosome maturation. PMID: 18048346
Homozygous deletions in a number of biologically important genes were found in prostate cancer cell lines, including PPP2R2A and BNIP3L identified in this study. PMID: 18670647

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.