Recombinant Human BMF protein(Met1-Arg184), His-tagged

• Cat.No.: BMF-515H
• Product Overview: Recombinant Human BMF (Q96LC9-1) (Met1-Arg184) was expressed in E. coli with a polyhistide tag at the N-terminus.

Specification

• Species: Human
• Source: E.coli
• Tag: His
• Protein Length: Met1-Arg184
• Form: Lyophilized from sterile 50mM Tris, 0.1% Brij35, pH 8.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human BMF consists of 199 amino acids and predicts a molecular mass of 22.3 KDa. It migrates as an approximately 25 KDa band in SDS-PAGE under reducing conditions.
• Purity: > 85 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: BMF Bcl2 modifying factor [ Homo sapiens ]
• Official Symbol: BMF
• Synonyms: BMF; Bcl2 modifying factor; bcl-2-modifying factor; FLJ00065
• Gene ID: 90427
• mRNA Refseq: NM_001003940
• Protein Refseq: NP_001003940
• MIM: 606266
• UniProt ID: Q96LC9

Case Study

Case 1: Morales AA, et al. Leukemia. 2004

Bmf is part of the Bcl-2 family and usually hangs out with myosin V motors by connecting to DLC2. When certain stress signals come in, Bmf gets freed up to bond with prosurvival Bcl-2 proteins, which kickstarts cell death. In a study of B-CLL cells, they identified two new versions of Bmf, named Bmf-II and Bmf-III. These variants lack the BH3 domain but still connect to DLC2. While Bmf-I triggers cell death and reduces growth in HeLa cells, Bmf-II and Bmf-III don't induce death and actually boost growth. Bmf-I is widespread but prominent in B lymphoid cells, while Bmf-II and Bmf-III appear mainly in B-CLL and normal B cells. Bmf-I increases in both healthy and cancerous B cells, whereas Bmf-III decreases in B-CLL cells without serum. This balance of Bmf forms might be key for controlling growth and survival in both normal and leukemic B cells.

Fig1. Apoptotic activity of Bmf-I, Bmf-II and Bmf-III.

Fig2. Expression of Bmf proteins in transiently transfected HEK 293T cells.

Case 2: Ma D, et al. J Cell Physiol. 2024

Cancer stem cells (CSCs) drive cancer progression and treatment resistance. Researchers used a pressure device to study how different IFP levels—5, 40, and 200 mmHg—impact LCSCs' characteristics. At 40 mmHg, LCSCs showed increased stem cell markers, sphere and colony formation abilities, and tumor potential, whereas 200 mmHg pressure reduced these traits. The study found that pressure influences LCSC stemness through the YAP/BMF signaling pathway. Modulating YAP and BMF levels affected the pressure-induced stemness and tumorigenic characteristics in LCSCs, highlighting the importance of this signaling axis.

Fig1. Representative Western blot analysis images of BMF in HCC cells and SFCs.

Fig2. Representative Western blot analysis images of stemness-associated markers in BMF-overexpressing LCSCs.

Application

Human BMF, or Bcl2 modifying factor, is a protein crucial in controlling apoptosis, the process of programmed cell death. In the research world, recombinant Human BMF (rhBMF) is a key player in studying this process. As part of the BCL2 family, this protein works by engaging with various anti-apoptotic proteins like MCL1 and BCL2, helping scientists dig into the intricate web of cell death regulation. By studying how rhBMF connects and functions in this pathway, researchers glean key insights for crafting treatments for conditions like cancer and neurodegenerative diseases where cell death is out of whack. Its role in juggling cell survival and death is crucial for investigating new treatment strategies.

On the industrial side, rhBMF is produced for drug discovery and development, especially in cancer treatment. Its involvement in apoptosis positions it as a promising target for therapeutic approaches aimed at controlling cell survival. Mass production of rhBMF aids in creating standard research reagents, ensuring scientific experiments are reliable and consistent. Moreover, producing this protein supports the development of antibodies and diagnostic tools necessary to detect and measure BMF in biological samples. These tools are not only critical for understanding BMF's function but also vital for shaping therapies that target this protein.

Fig1. The BH3-only proteins Bim and Bmf are subjected to multiple layers of regulation. (J D Piñon, 2009)