Recombinant Human Bcl-2-Modifying Factor (BMF) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08753P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Bcl-2-Modifying Factor (BMF) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08753P
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Product Overview

Description Recombinant Human Bcl-2-Modifying Factor (BMF) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q96LC9
Target Symbol BMF
Synonyms Bcl 2 modifying factor; Bcl-2-modifying factor; Bcl2 modifying factor; Bmf; BMF_HUMAN; FLJ00065
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MEPSQCVEELEDDVFQPEDGEPVTQPGSLLSADLFAQSLLDCPLSRLQLFPLTHCCGPGLRPTSQEDKATQTLSPASPSPGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAVLPIGEQPPEGQWQHQAEVQIARKLQCIADQFHRLHVQQHQQNQNRVWWQILLFLHNLALNGEENRNGAGPR
Expression Range 1-184aa
Protein Length Full Length of BC069505
Mol. Weight 47.5kDa
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 May play a role in apoptosis. Isoform 1 seems to be the main initiator.
Protein Families Bcl-2 family
Database References

HGNC: 24132

OMIM: 606266

KEGG: hsa:90427

STRING: 9606.ENSP00000346697

UniGene: PMID: 27524613

  • Reciprocal regulation of BMF and BIRC5 is linked to Eomes overexpression in colorectal cancer. PMID: 27539959
  • Early generated B1 B cells with restricted BCRs become chronic lymphocytic leukemia with continued c-Myc and low Bmf expression PMID: 27899442
  • these findings suggest that p53-R273H can specifically drive AKT signaling and suppress BMF expression, resulting in enhanced cell survivability and anoikis resistance. PMID: 26181206
  • Overexpression of ApoL2 did not induce cell death on its own. ApoL2 did not sensitize or protect cells from overexpression of the BH3-only proteins Bmf or Noxa. PMID: 24901046
  • Diva binds peptides derived from the BH3 domain of several other proapoptotic Bcl-2 proteins, including mouse Harakiri, Bid, Bak and Bmf. PMID: 23192964
  • BMF is induced in human IEC by the loss of cell attachment and is likely to play an important role in the regulation of IEC survival PMID: 21673109
  • characterization of the bmf gene locus; molecular basis of the generation of the 2 major isoforms of Bmf; provide evidence that Bmf can act as a sensor for stress that associates with the repression of the conventional CAP-dependent translation machinery PMID: 20706276
  • Data show that hypoxic conditions inhibit anoikis and block expression of proapoptotic BH3-only family members Bim and Bmf in epithelial cells. PMID: 20861305
  • Bmf is upregulated by PS-341 and has a crucial role in PS-341-mediated glioma cell death through JNK phosphorylation. PMID: 19267218
  • Up or downregulation of Bmf isoforms may have a role in regulating growth and survival in B cells and leukemic B-CLL cells PMID: 14574334
  • histone hyperacetylation may enhance ionizing radiation-induced death via activation of Bmf transcription, thereby implying Bmf as a key molecule for HDAC inhibitors (FK228 and CBHA)-mediated enhancing effect on IR-induced cell death PMID: 16830229
  • Bmf is a central mediator of anoikis in mammary cells and a target of oncogenes that contribute to the progression of glandular epithelial tumors PMID: 17360431
  • arsenic trioxide upregulated expression of Bmf, Noxa, and Bim. Silencing of Bmf, Noxa, and Bim significantly protected MM cells from ATO-induced apoptosis PMID: 18354037
  • Our data indicate a synergistic role for both bim and Bmf in an apoptotic pathway leading to the clearance of Neisseria gonorrhoeae -infected cells. PMID: 19300516
  • Bmf supports Bim in regulating cell death processes in response to many stimuli. Review. PMID: 19641506
  • MicroRNA-221 targets Bmf in hepatocellular carcinoma and correlates with tumor multifocality. PMID: 19671867
  • FAQs

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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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