Recombinant Human Bcl-W / BCL2L2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0371

Recombinant Human Bcl-W / BCL2L2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0371
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Product Overview

Tag His
Host Species Human
Accession Q92843
Synonym BCL-W, BCL2-L-2, BCLW, PPP1R51
Background Beta1,4-Galactosyltransferase-I (B4GALT1), one of seven beta1,4-galactosyltransferases, is an enzyme commonly found in the trans-Golgi complex that adds galactose to oligosaccharides. They have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. B4GALT1 gene directs production of B4GALT1 protein using either of two transcription start sites. The product of the smaller transcript serves the traditional biosynthetic role in the Golgi. This form also complexes with alpha-lactalbumin, a mammary-specific protein, to form lactose synthase. In addition to a biosynthetic role, the protein translated from the longer transcript appears on the plasma membranes of some cells where it serves as a signalling receptor in cell-matrix interactions such as sperm-egg binding.
Description A DNA sequence encoding the human BCL-W (Q92843-1) (Met 1-Thr 172) was fused with a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Thr 172
Molecular Weight The recombinant human BCL-W consisting of 182 a.a. and has a calculated molecular mass of 20 kDa. It migrates as an approximately 18 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 25mM Hepes 0.1MKCl 10% glycerolpH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.
Subcellular Location Mitochondrion membrane; Peripheral membrane protein. Note=Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane.
Protein Families Bcl-2 family
Database References
Tissue Specificity Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or li

Gene Functions References

  1. the present study demonstrates that miR-422a may serve as a tumor suppressor in osteosarcoma via inhibiting BCL2L2 and KRAS translation both in vitro and in vivo Therefore, miR-422a could be developed as a novel therapeutic target in osteosarcoma. PMID: 29358307
  2. BCL2L2 knockdown was attenuated the effects of SNHG1 overexpression on cell viability, cell apoptosis and protein levels of cleaved caspase-3, cleaved caspase-9 and Bax in H2O2-treated human cardiomyocytes. PMID: 30355909
  3. Our comprehensive analysis indicates B-cell lymphomas commonly select for BCLW overexpression in combination with or instead of other antiapoptotic BCL2 family members. PMID: 28855351
  4. BCL-W contributes to the threshold of anti-apoptotic activity during mitosis PMID: 27231850
  5. we demonstrated that miR-126-5p plays an inhibitory role in human cervical cancer progression, regulating the apoptosis of cancer cells via directly targeting Bcl2l2. PMID: 28438233
  6. High expression of Bcl-w was associated with mesenchymal changes and invading populations in the glioblastoma multiforme; Bcl-w functions as a positive regulator of invasion by enhancing mesenchymal traits of glioblastoma multiforme, consequently contributing to malignancy. PMID: 23826359
  7. BCL2L2 was the virtual target of miR-133b, and we found a negative regulatory relationship between miR-133b and BCL2L2. MiR-133b and BCL2L2 interfered with the viability and apoptosis of cells. PMID: 27802259
  8. we conclude that BER treatment reduces cisplatin resistance of gastric cancer cells by modulating the miR-203/Bcl-w apoptotic axis. BER may be a novel agent to enhance chemotherapeutic responses in cisplatin-resistant gastric cancer patients PMID: 27142767
  9. Data show that BCL2-like 2 protein (BCL2L2) is a direct target of micrRNA miR-29b. PMID: 26155940
  10. these results indicate that miR-335 acts as a novel tumor suppressor to regulate ccRCC cell proliferation and invasion through downregulation of BCL-W expression. PMID: 25846734
  11. miR-15a acts as a tumor suppressor in NSCLC by directly targeting BCL2L2 and may serve as a potential diagnostic biomarker and therapeutic target for NSCLC. PMID: 25874488
  12. over-expression of miR-195 sensitized resistant cells to DOX and enhanced cell apoptosis activity, all of which can be partly rescued by BCL2L2 siRNA and cDNA expression PMID: 23526568
  13. Bcl-w-induced Sp1 activation is a potential marker for aggressiveness of glioblastoma multiforme. PMID: 24552705
  14. HDMF inhibits Bcl-w-induced neurosphere formation and the expression of glioma stem cell markers, such as Musashi, Sox-2 and c-myc. PMID: 24946210
  15. Crystal structure of human BCL-W in complex with different DARPins is virtually identical to the ligand-free conformation of its closest relative BCL-XL. PMID: 24747052
  16. MiR-335 lacks of expression brings about the abnormal accumulation of Bcl-w. PMID: 23708561
  17. Expression of miR-214 reduces cell survival, induces apoptosis and enhances sensitivity to cisplatin through directly inhibiting Bcl2l2 expression. PMID: 23337879
  18. Bcl-w protein plays a significant role in the carcinogenesis of human small intestinal adenocarcinoma. Down-regulation of Bcl-w protein in HuTu-80 cells makes them susceptible to 5-Fu. PMID: 22780970
  19. These findings indicate that miR-29c-mediated BCL2L2 suppression is involved in influenza virus-induced cell death in A549 cells. PMID: 22850539
  20. By using human cancer cells and mouse embryonic fibroblasts, the study shows that BCL-W functions in the mitochondria to increase the levels of reactive oxygen species (ROS), which subsequently stimulates the invasion-promoting signaling pathway. PMID: 22570867
  21. our results provide evidence that miR-335 might function as a metastasis suppressor in gastric cancer by targeting SP1 directly and indirectly through the Bcl-w-induced phosphoinositide 3-kinase-Akt-Sp1 pathway PMID: 21822301
  22. Data show that ABT-737, a small molecule inhibitor of Bcl-2, Bcl-X(L), and Bcl-w, significantly induced apoptosis in HTLV-1 infected T-cell lines as well as in fresh adult T-cell leukemia/lymphoma (ATLL) cells. PMID: 22138435
  23. miR-195 could improve the drug sensitivity at least in part by targeting Bcl-w to increase cell apoptosis in hepatocellular carcinoma cells. PMID: 21947305
  24. The alpha4-alpha5 hinge region is required for dimerization of BCL-W, and functioning of both pro- and antiapoptotic BCL-2 proteins. PMID: 22000515
  25. although the cytosolic domain of BCL-w exhibits an overall structure similar to that of BCL-xL and BCL-2, the unique organization of its C-terminal helix may modulate BCL-w interactions with pro-apoptotic binding partners PMID: 12651847
  26. structure of reveals a role for the C-terminal residues in modulating biological activity PMID: 12660157
  27. Bcl-w may play an important protective role in neurons in the Alzheimer disease brain and this aspect could be therapeutically harnessed to afford neuroprotection PMID: 15147516
  28. Peptide = to BH3 region of proapoptotic protein BID, bound in cleft of antiapoptotic protein BCL-w.Binding induced major conformational rearrangements in both peptide & protein components & led to displacement & unfolding of BCL-w C-terminal alpha-helix. PMID: 16475813
  29. overexpressed BCL2L2, through amplification or other mechanisms, promotes the growth of a non-smalll cell lung caner cell line. PMID: 17459056
  30. Bcl-w is a direct target of miR-122 that functions as an endogenous apoptosis regulator in these human hepatocellular carcinoma -derived cell lines. PMID: 18692484
  31. both uPA and MMP-2 contribute to Bcl-w-induced invasion via the stimulation of the FAK-dependent migratory pathway. PMID: 19097687
  32. Bcl-w is a new member of the Akt pathway PMID: 19114998
  33. BCL-W may function as a downstream effector of inappropriate WNT/beta-catenin signalling. PMID: 19124064
  34. Results show that the folate-induced DNA methylation limits proliferation and increases the sensitivity to temozolomide-induced apoptosis in glioma cells through methylation of PDGF-B, MGMT, survivin, and bcl-w genes. PMID: 19451595
  35. over-expression of miR-133B increased apoptosis in response to gemcitabine and reduced MCL-1 and BCL2L2 expression. PMID: 19654003


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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.

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