Recombinant Human Bcl-2-Related Protein A1 (BCL2A1) Protein (His-GST)

Name: Recombinant Human Bcl-2-Related Protein A1 (BCL2A1) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-06855P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Bcl-2-Related Protein A1 (BCL2A1) Protein (His-GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q16548
Target Symbol	BCL2A1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	VLFQGPLGSPEFRTMTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNVNVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEISYFVAEFIMNNTGEWIRQNGGWENGFVKKFEPKSGWMTFLEVTGKICEMLSLLKQYCGRTRAPPPPPLRSGCQSPKGSVGCCHRAITSITPWGLTGLEGVFCKENYIRIAWRHVADIDRGRCGDSPIRTGYS
Expression Range	1-175aa
Protein Length	Full Length
Mol. Weight	61.3 kDa
Research Area	Cell Biology
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	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	HGNC: 991 OMIM: 601056 KEGG: hsa:597 STRING: 9606.ENSP00000267953 UniGene: PMID: 29276033 Demonstrate immunohistochemical expression of Wnt11 and BCL2A1 in complete moles and normal villi. PMID: 27386628 Bfl-1 was mitochondrially resident in both resting and apoptotic cells and experienced regulation by the proteasome and NFkappaB pathways. PMID: 25486183 Bcl2a1 overexpressing granulocytic MDSCs demonstrated prolonged survival. PMID: 24810636 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 BCL2A1 is a novel marker associated with seizure prognosis following surgery for low-grade brain neoplasms. PMID: 23841872 MITF-BCL2A1 as a lineage-specific oncogenic pathway in melanoma and underscore its role for improved response to BRAF-directed therapy. PMID: 23447565 Bcl2a1 should be considered as a proto-oncogene with a potential role in both lymphoid and myeloid leukemogenesis PMID: 23118966 Mitochondrial antiapoptotic factor Bfl-1 is significantly reduced by suppressor of cytokine signaling (SOCS)1. PMID: 23152563 results highlight Bfl-1 as a major effector in activation-induced human mast cell survival PMID: 22720045 Data indicate that BCL2a1 expression enhances tumor cell survival in nervous system (CNS) leading to intracranial tumor growth. PMID: 22865454 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 neutrophils from patients with sepsis express reduced levels of antiapoptotic Mcl1 and A1 PMID: 22231730 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 The transcription factor Spi-B regulates human plasmacytoid dendritic cell survival through direct induction of the antiapoptotic gene BCL2-A1. PMID: 22510878 Inhibition of Mcl-1 and A1 strongly induced cell death in some melanoma cell lines. PMID: 22292048 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 Bfl-1 importantly regulates lung cancer cell sensitivity to gemcitabine. PMID: 21843371 Bfl-1/A1 negatively regulates autophagy and expression of Bfl-1/A1 in H37Rv infected macrophages PMID: 21167304 Defective ubiquitin-mediated degradation of antiapoptotic Bfl-1 predisposes to lymphoma. PMID: 20185581 role for NF-kappa B in bfl-1 transcription PMID: 12665576 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 identification of two novel minor histocompatibility antigens, encoded by two separate single nucleotide polymorphisms on a single gene, BCL2A1, and restricted by HLA-A2402 and B4403 PMID: 12771180 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 confers protection from hydrogen peroxide- and peroxynitrite- induced apoptosis in neutrophils and HL-60 cells PMID: 14966372 The expression of BCL2A1 was compared in two inbred strains of mice. PMID: 14981542 High expression of bfl-1 contributes to the apoptosis resistant phenotype in B-cell chronic lymphocytic leukemia PMID: 15499630 expression in urethral epithelium upregulated by Neisseria gonorrhoeae PorB IB and upregulation dependent on NF-kappaB activation PMID: 15501771 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 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 performed a Bfl-1 deletion study in order to elucidate the underlying mechanism of GFP-Bfl-1-induced cell death PMID: 15696550 A1 and A20 are both required for optimal protection from apoptosis (A1) and inflammation (A20) in conditions leading to renal damage PMID: 16164629 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 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 EBNA2 trans-activates bfl-1, which requires CBF1 (or RBP-J kappa). PMID: 16873269 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 Amphipathic tail-anchoring peptide (ATAP) targets specifically to mitochondria, and induces caspase-dependent apoptosis that does not require Bax or Bak. PMID: 17666431 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 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 While TNFalpha had no effect on MCL-1 transcription, it induced expression of another antiapoptotic molecule, BFL-1. PMID: 17942758 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 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 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 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 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.