Recombinant Human Bcl2A1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0368

Recombinant Human Bcl2A1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0368
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Product Overview

Tag His
Host Species Human
Accession NP_004040
Synonym ACC-1, ACC-2, ACC1, ACC2, BCL2L5, BFL1, GRS, HBPA1
Background B-cell lymphoma 2-related protein A1 (BCL2A1) is a member of the BCL-2 family of anti-apoptotic proteins that confers resistance to treatment with anti-cancer drugs. Immunohistochemical expression of Wnt11 and BCL2A1 in complete moles and normal villi. Bcl2 family proteins control mitochondrial apoptosis and its members exert critical cell type and differentiation stage-specific functions, acting as barriers against autoimmunity or transformation. Anti-apoptotic Bcl2a1/Bfl1/A1 is frequently deregulated in different types of blood cancers in humans but its physiological role is poorly understood as quadruplication of the Bcl2a1 gene locus in mice hampers conventional gene targeting strategies. In a physiological context, BCL2A1 is mainly expressed in the hematopoietic system, where it facilitates survival of selected leukocytes subsets and inflammation. However, BCL2A1 is overexpressed in a variety of cancer cells, including hematological malignancies and solid tumors, and may contribute to tumor progression. The development of small molecule inhibitors of BCL2A1 may be a promising approach mainly to sensitize tumor cells for apoptosis and thus improve the efficiency of anti-cancer therapy.
Description A DNA sequence encoding the human BCL2A1 (NP_004040 ) (Met1-Ser152) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met 1
AA Sequence Met1-Ser152
Molecular Weight The recombinant human BCL2A1 consists of 170 a.a. and predicts a molecular mass of 19.7 kDa.
Purity >85% as determined by SDS-PAGE.
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS pH 7.4..
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 Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11.
Subcellular Location Cytoplasm.
Protein Families Bcl-2 family
Database References
Tissue Specificity Seems to be restricted to the hematopoietic compartment. Expressed in peripheral blood, spleen, and bone marrow, at moderate levels in lung, small intestine and testis, at a minimal levels in other tissues. Also found in vascular smooth muscle cells and h

Gene Functions References

  1. Crystal structures of anti-apoptotic BFL-1 and its complex with a covalent stapled BH3 peptide inhibitor have been presented. PMID: 29276033
  2. Demonstrate immunohistochemical expression of Wnt11 and BCL2A1 in complete moles and normal villi. PMID: 27386628
  3. Bfl-1 was mitochondrially resident in both resting and apoptotic cells and experienced regulation by the proteasome and NFkappaB pathways. PMID: 25486183
  4. Bcl2a1 overexpressing granulocytic MDSCs demonstrated prolonged survival. PMID: 24810636
  5. Results indicate that mismatches in minor H antigens HA-8 (KIAA0020) and ACC-1 (BCL2A1) predisposed to chronic graft-versus-host disease (GvHD). PMID: 23480177
  6. BCL2A1 is a novel marker associated with seizure prognosis following surgery for low-grade brain neoplasms. PMID: 23841872
  7. MITF-BCL2A1 as a lineage-specific oncogenic pathway in melanoma and underscore its role for improved response to BRAF-directed therapy. PMID: 23447565
  8. Bcl2a1 should be considered as a proto-oncogene with a potential role in both lymphoid and myeloid leukemogenesis PMID: 23118966
  9. Mitochondrial antiapoptotic factor Bfl-1 is significantly reduced by suppressor of cytokine signaling (SOCS)1. PMID: 23152563
  10. results highlight Bfl-1 as a major effector in activation-induced human mast cell survival PMID: 22720045
  11. Data indicate that BCL2a1 expression enhances tumor cell survival in nervous system (CNS) leading to intracranial tumor growth. PMID: 22865454
  12. Data demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active alpha-helices that are responsible for its conversion into a pro-apoptotic factor. PMID: 22745672
  13. neutrophils from patients with sepsis express reduced levels of antiapoptotic Mcl1 and A1 PMID: 22231730
  14. results directly implicate Bfl-1 and Bcl-x(L) in HTLV-1-infected T-cell survival and suggest that both Bfl-1 and Bcl-x(L) represent potential therapeutic targets for ATLL treatment. PMID: 22553204
  15. The transcription factor Spi-B regulates human plasmacytoid dendritic cell survival through direct induction of the antiapoptotic gene BCL2-A1. PMID: 22510878
  16. Inhibition of Mcl-1 and A1 strongly induced cell death in some melanoma cell lines. PMID: 22292048
  17. These findings are the first indication that Bfl-1 plays a crucial role in setting the elevated threshold of resistance of this malignant cell type to apoptosis PMID: 21491422
  18. Bfl-1 importantly regulates lung cancer cell sensitivity to gemcitabine. PMID: 21843371
  19. Bfl-1/A1 negatively regulates autophagy and expression of Bfl-1/A1 in H37Rv infected macrophages PMID: 21167304
  20. Defective ubiquitin-mediated degradation of antiapoptotic Bfl-1 predisposes to lymphoma. PMID: 20185581
  21. role for NF-kappa B in bfl-1 transcription PMID: 12665576
  22. the level of Bfl-1 gene expression was higher in more advanced breast cancers than in early cancers; it seems that the increased expression of the Bfl-1 gene serves as a contributory factor in breast cancer in the same way that another group of genes PMID: 12692420
  23. identification of two novel minor histocompatibility antigens, encoded by two separate single nucleotide polymorphisms on a single gene, BCL2A1, and restricted by HLA-A*2402 and B*4403 PMID: 12771180
  24. Epstein Barr virus LMP1 drives bfl-1 promoter activity through interactions with components of the tumor necrosis factor receptor (TNFR)/CD40 signaling pathway; evidence presented that this process is NF-kappa B dependent PMID: 14747545
  25. confers protection from hydrogen peroxide- and peroxynitrite- induced apoptosis in neutrophils and HL-60 cells PMID: 14966372
  26. The expression of BCL2A1 was compared in two inbred strains of mice. PMID: 14981542
  27. High expression of bfl-1 contributes to the apoptosis resistant phenotype in B-cell chronic lymphocytic leukemia PMID: 15499630
  28. expression in urethral epithelium upregulated by Neisseria gonorrhoeae PorB IB and upregulation dependent on NF-kappaB activation PMID: 15501771
  29. Oxidative stress induces the expression of Bfl-1 via NF-kappaB activation, and this early-response gene protects cells from Fas-mediated apoptosis. PMID: 15592513
  30. results suggest that Anaplasma phagocytophilum inhibits human neutrophil apoptosis via transcriptional upregulation of bfl-1 and inhibition of mitochondria-mediated activation of caspase 3 PMID: 15617521
  31. performed a Bfl-1 deletion study in order to elucidate the underlying mechanism of GFP-Bfl-1-induced cell death PMID: 15696550
  32. A1 and A20 are both required for optimal protection from apoptosis (A1) and inflammation (A20) in conditions leading to renal damage PMID: 16164629
  33. The C terminus of A1 did not function as a membrane anchor; it serves a dual function by controlling the stability of A1 and by amplifying the capacity of the protein to protect cells against apoptosis. PMID: 16551634
  34. Bfl-1/A1 mRNA is not expressed in these cell lines, however, its expression is markedly induced by ATRA treatment in NB4 and HL-60 cells, but not in R4 or HL-60/Res cells, which correlates with inhibition of apoptosis. PMID: 16572199
  35. EBNA2 trans-activates bfl-1, which requires CBF1 (or RBP-J kappa). PMID: 16873269
  36. the known polymorphisms of exon 1 and a novel polymorphism in the promoter region provide evidence for an association between bfl-1 polymorphisms and genetic predisposition to atopic dermatitis PMID: 17121585
  37. Amphipathic tail-anchoring peptide (ATAP) targets specifically to mitochondria, and induces caspase-dependent apoptosis that does not require Bax or Bak. PMID: 17666431
  38. Bfl-1 associates with tBid to prevent activation of proapoptotic Bax and Bak, and it also interacts directly with Bak to antagonize Bak-mediated cell death, similar to myeloid cell factor (Mcl)-1. PMID: 17724464
  39. Specific downregulation of bfl-1 using siRNA induced apoptosis in resistant cells. Our data suggest that bfl-1 contributes to chemoresistance and might be a therapeutic target in B-CLL. PMID: 17726463
  40. While TNFalpha had no effect on MCL-1 transcription, it induced expression of another antiapoptotic molecule, BFL-1. PMID: 17942758
  41. Results clearly indicated that differential expression of bfl-1/A1 in M. tuberculosis H37Rv and M. tuberculosis H37Ra infected THP-1 cells probably account for the difference in infection outcome. PMID: 18206119
  42. targeting mHags encoded not only by HMHA1, whose aberrant expression in solid tumors has been reported, but also BCL2A1 may bring about beneficial selective graft-versus-tumor effects PMID: 18414982
  43. C/EBP beta overexpression significantly upregulated promoter activities of IL-8, COX-2, and anti-apoptotic Bfl-1 genes in prostate cancer cells. PMID: 18512730
  44. The crystal structure of Bfl-1, the last anti-apoptotic Bcl-2 family member to be structurally characterized, in complex with a peptide corresponding to the BH3 region of the pro-apoptotic protein Bim is presented. PMID: 18812174
  45. the amphipathic character of Bfl-1 C-terminal helix alpha9 is required for the anchorage of Bfl-1 to the mitochondria and regulation the antiapoptotic function Bfl-1 PMID: 19759007


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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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