Recombinant Human Bcl-2-Like Protein 2 (BCL2L2) Protein (His-SUMO)

Name: Recombinant Human Bcl-2-Like Protein 2 (BCL2L2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09852P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Bcl-2-Like Protein 2 (BCL2L2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q92843
Target Symbol	BCL2L2
Synonyms	Apoptosis regulator BCL W; Apoptosis regulator Bcl-W; B2CL2_HUMAN; BCL 2 Like 2; Bcl 2 like 2 protein; Bcl 2L2; BCL W; Bcl-2-like protein 2; Bcl2 L2; BCL2 like 2; BCL2 like 2 protein; Bcl2-L-2; Bcl2l2; BCLW; KIAA0271; PPP1R51; Protein phosphatase 1 regulatory subunit 51
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK
Expression Range	2-193aa
Protein Length	Full Length of Mature Protein
Mol. Weight	36.6kDa
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	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	HGNC: 995 OMIM: 601931 KEGG: hsa:599 STRING: 9606.ENSP00000250405 UniGene: PMID: 29358307 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 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 BCL-W contributes to the threshold of anti-apoptotic activity during mitosis PMID: 27231850 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 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 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 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 Data show that BCL2-like 2 protein (BCL2L2) is a direct target of micrRNA miR-29b. PMID: 26155940 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 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 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 Bcl-w-induced Sp1 activation is a potential marker for aggressiveness of glioblastoma multiforme. PMID: 24552705 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 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 MiR-335 lacks of expression brings about the abnormal accumulation of Bcl-w. PMID: 23708561 Expression of miR-214 reduces cell survival, induces apoptosis and enhances sensitivity to cisplatin through directly inhibiting Bcl2l2 expression. PMID: 23337879 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 These findings indicate that miR-29c-mediated BCL2L2 suppression is involved in influenza virus-induced cell death in A549 cells. PMID: 22850539 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 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 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 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 The alpha4-alpha5 hinge region is required for dimerization of BCL-W, and functioning of both pro- and antiapoptotic BCL-2 proteins. PMID: 22000515 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 structure of reveals a role for the C-terminal residues in modulating biological activity PMID: 12660157 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 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 overexpressed BCL2L2, through amplification or other mechanisms, promotes the growth of a non-smalll cell lung caner cell line. PMID: 17459056 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 both uPA and MMP-2 contribute to Bcl-w-induced invasion via the stimulation of the FAK-dependent migratory pathway. PMID: 19097687 Bcl-w is a new member of the Akt pathway PMID: 19114998 BCL-W may function as a downstream effector of inappropriate WNT/beta-catenin signalling. PMID: 19124064 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 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.