Recombinant Human Bcl-2-Like Protein 11 (BCL2L11) Protein (His)

Name: Recombinant Human Bcl-2-Like Protein 11 (BCL2L11) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06602P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Bcl-2-Like Protein 11 (BCL2L11) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O43521
Target Symbol	BCL2L11
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH
Expression Range	1-198aa
Protein Length	Full Length
Mol. Weight	26.2 kDa
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 and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis.
Subcellular Location	Endomembrane system; Peripheral membrane protein.; [Isoform BimEL]: Mitochondrion. Note=Translocates from microtubules to mitochondria on loss of cell adherence.; [Isoform BimL]: Mitochondrion.; [Isoform BimS]: Mitochondrion.; [Isoform Bim-alpha1]: Mitochondrion.
Protein Families	Bcl-2 family
Database References	HGNC: 994 OMIM: 603827 KEGG: hsa:10018 STRING: 9606.ENSP00000376943 UniGene: Hs.469658
Tissue Specificity	Isoform BimEL, isoform BimL and isoform BimS are the predominant isoforms and are widely expressed with tissue-specific variation. Isoform Bim-gamma is most abundantly expressed in small intestine and colon, and in lower levels in spleen, prostate, testis

Gene Functions References

POH1 knockdown induced cell apoptosis through increased expression of p53 and Bim. PMID: 29573636
BIM deletion polymorphism was associated with significantly shorter progression-free survival (PFS) and slightly shorter overall survival (OS), compared to the WT group. Moreover, patients with BIM deletion polymorphism showed significantly inferior response to EGFR TKIs. In conclusion, our analysis confirmed that lung cancer patients harboring the BIM deletion have inferior survival and TKI responses. PMID: 30213299
Our findings suggest that miR-23 plays a crucial role in controlling VSMCs proliferation and apoptosis by targeting BCL2L11 PMID: 30249504
FoxO3a overexpression increased the transcription and protein expression of Bcl2like protein 11 and cyclindependent kinase inhibitor 1B, and inhibited cyclin D1 transcription and expression. PMID: 29257235
Data indicate that miR-34a enhanced the sensitivity to cisplatin by upregulation of c-Myc and Bim pathway. PMID: 29060932
Modulation of MEK/ERK-dependent Bim and Mcl-1 degradation critically mediates sensitivity and resistance of EGFR-mutant non-small cell lung cancer (NSCLC)cells to AZD9291 and hence is an effective strategy to overcome acquired resistance to AZD9291 PMID: 28765329
TMEM16A expression was found to correlate with greater tumor size, less Bim expression, and less apoptotic activity overall in head and neck squamous cell carcinomas (HNSCCs). PMID: 28899969
Hypermethylation of the proapoptotic genes BCL2 L11 and TNFRSF25 is observed in pleomorphic adenoma of the salivary glands. However, this phenomenon did not impact mRNA transcription. PMID: 28941993
Data suggest that regulation of pancreatic beta-cell function and survival/apoptosis involves alternative splicing modulated by key splicing regulator SRP55; SRP55-regulated alternative splicing includes modulation of function of pro-apoptotic proteins (BIM, BAX), JNK signaling, and endoplasmic reticulum stress. (SRP55 = pre-mRNA-splicing factor SRP55; BAX = apoptosis regulator BAX) PMID: 29246973
Bim expression was significantly different in the four molecular subtypes of breast cancer. PMID: 28582840
BIM deletion is a significant predictor of shorter PFS and OS on EGFR-TKIs. Further studies to determine its effect on response to other BIM-dependent therapeutic agents are needed, so that alternative treatment strategies may be devised. PMID: 28467813
These findings indicate the importance of developing HDAC3-selective inhibitors, and their combined use with osimertinib, for treating EGFR-mutated lung cancers carrying the BIM deletion polymorphism PMID: 27986747
Low BIM expression is associated with renal cell carcinoma. PMID: 27582546
The decreased miR-101-3p caused elevated Bim expression by targeting its 3'-untranslated region (3'-UTR). PMID: 28518140
The mitochondrial apoptotic pathway, activated by BH3-only proteins, BIM and PUMA, is essential for endoplasmic reticulum stress-induced cell death; DR5 as well as caspase-8 are not required for this process. PMID: 28409774
sequestration of Bim by Mcl-1 is a mechanism of intrinsic ABT-199 resistance and supports the clinical development of ABT-199 in combination with cytarabine or daunorubicin for the treatment of AML. PMID: 27103402
Knock down of VDR and BIM reduces the enhancement of cell death treated with Cytarabine (AraC) followed by the addition of Doxercalciferol together with Carnosic acid (CA). PMID: 27144333
UMI-77 enhances TRAIL-induced apoptosis by unsequestering Bim and Bak, which provides a novel therapeutic strategy for the treatment of gliomas. PMID: 28337703
Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design. PMID: 29149594
in FOXO3-death-resistant cells no point mutations in the TP53-DBD were found-in these cells FOXO3-TP53 complexes are formed and FOXO3-binding to the BIM-promoter, but not the induction of the detoxifying protein SESN3, were prevented, which in turn increased chemo-protection in this type of high-stage-derived neuroblastoma cells PMID: 28869600
At BCL2L11, the authors identify a haematopoietic enhancer hub that is inactivated by the Epstein-Barr virus repressors EBNA3A and EBNA3C through recruitment of the H3K27 methyltransferase EZH2. PMID: 27490482
observations suggest that an association of a deletion polymorphism of BIM and the response to induction therapy in B-cell precursor acute lymphoblastic leukemia may be clinically minimal PMID: 28641145
expression of Bim is mediated by FoxO1 and indirectly downregulated by thyroid hormone/thyroid hormone receptor, leading to chemotherapy resistance and doxorubicin-promoted metastasis of hepatoma cells. PMID: 27490929
BIM is associated with favorable prognostic markers for prediction of disease-free survival and overall survival in cervical cancer. PMID: 28870908
this study shows that BIM deletion polymorphisms are associated with a poor clinical response to erlotinib and represents an independent prognostic factor for patients with EGFR positive non-small-cell lung cancer PMID: 27926478
The Bim deletion polymorphism was found to be associated with primary resistance to crizotinib in patients with ALK fusion-positive NSCLC. PMID: 28346673
increased apoptosis resistance was associated with significantly reduced up-regulation of proapoptotic Bim in T cells from patients with primary sclerosing cholangitis. PMID: 27630216
Results suggest that valproic acid (VPA) reduces paraoxonase 2 (PON2) expression in glioblastoma multiforme (GBM) cells, which in turn increases reactive oxygen species (ROS) production and induces Bim protein production that inhibits cancer progression via the PON2-Bim cascade. PMID: 28108734
Little difference in Bim expression among CD20+ cells was seen between tonsil primary follicles, tonsil germinal centers, and lupus nephritis renal tissue. The frequency of Bim-positive cells among CD4+ lymphocytes was significantly lower in lupus nephritis kidneys compared to tonsil controls. PMID: 27159593
Inhibition of mTORC1-mediated 4EBP1 phosphorylation leads to decreased expression of c-MYC and subsequent upregulation of the proapoptotic BCL2 family member PUMA, whereas inhibition of mTORC2 results in nuclear factor-kappaB-mediated expression of the Early Growth Response 1 (EGR1) gene, which encodes a transcription factor that binds and transactivates the proapoptotic BCL2L11 locus encoding BIM. PMID: 26917778
miR-423-3p activates oncogenic and Beclin-1-dependent autophagy and promotes GC progression by reducing the expression of Bim. The newly identified miR-423-3p-Bim axis might be a potential therapeutic target in GC. PMID: 28254439
activation of the PI3K pathway does not suppress activation of the ARF or BIM gene by over-expressed E2F1 PMID: 27888102
have shown that Bim protein expression in CM is an independent predictor for advanced disease confirming that this pro-apoptotic BH3-only protein might be a potent biomarker and promising therapeutic target PMID: 27356803
BIM deletion polymorphism does not account for intrinsic resistance to EGFR-TKI in Patients With Lung Adenocarcinoma PMID: 27077907
Mechanistically, G-Rg1 promoted the phosphorylation of Akt and FoxO3a and led to the cytoplasmic translocation of FoxO3a, which in turn suppressed FoxO3a-modulated expression of proapoptotic Bim and elevated the ratio of Bcl-2 to Bax. PMID: 27522666
Dnd1 facilitates apoptosis by increasing the expression of Bim via its competitive combining with miR-221 in Bim-3'UTR. PMID: 28191469
patients with BIM-g had significantly shorter progression-free survival than those without BIM-gamma (median: 304 vs. 732 days; p=0.023). CONCLUSION: Expression of BIM-gamma mRNA and BIM deletion polymorphism were strongly associated. BIM-gamma overexpression may have a role in apoptosis related to EGFR-tyrosine kinase inhibitor PMID: 27807070
MicroRNA-301b directly targets the expression of Bim, a well-known pro-apoptotic protein. PMID: 27352910
FOXO4 has an inhibitory effect in clearcell renal carcinoma cells, at least in part through inducing apoptosis via upregulation of Bim in the mitochondria-dependent pathway. PMID: 26780985
Results indicate that upregulation of miR-124 could regulate apoptosis and impaired autophagy process in the MPTP model of Parkinson's disease, thus reducing the loss of dopaminergic neurons PMID: 25976060
the Bim activated by doxorubicin-induced DNA damage might directly interrupt the interaction of Bcl-xl with pro-apoptotic proteins, Bak/Bax, to activate mitochondriadriven apoptosis. PMID: 26694174
the BIM deletion polymorphism enhanced the emergence of populations with complete imatinib resistance, mimicking the situation in patients. PMID: 26517680
BimEL-Bax pro-apoptotic cascade is activated by cAMP signalling of Bordetella adenylate cyclase toxin through SHP-1 phosphatase in phagocytes. PMID: 26334669
miR-24 was found to be up-regulated while the expression of BCL2L11 was inhibited in tumor tissues of gastric cancer PMID: 26758252
The potent antitumor activity of RHL may be mediated through downregulation of Bcl-2 and cyclin D expression and upregulation of BAX and Bim expression. PMID: 26707131
mRNA expression of BIM and MTOR in 57 patients with EGFR-mutant non-small-cell lung cancer. PMID: 26639561
miR-24 promotes tumor growth and angiogenesis by suppressing Bim expression in a model of pancreatic carcinoma PMID: 26517093
miR-181b/Bim pathway may be a novel target used to overcome the chemoresistance in breast cancer PMID: 26572075
Bcl-2 dependent NB cell lines are exquisitely sensitive to ABT-199 . Treatment with ABT-199 displaces Bim from Bcl-2 in NB to activate caspase 3, confirming the restoration of mitochondrial apoptosis PMID: 26874859
Fluorizoline bind to prohibitin, inducing mitochondrial apoptotic pathway through NOXA and BIM upregulation. PMID: 26497683

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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.

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