Buforin IIb TFA
Based on 1 Customer Validation
Buforin IIb TFA (BF2-B TFA) is an anticancer peptide, as well as an Antibacterial and Antifungal agent. Buforin IIb TFA is derived from histone H2A. Buforin IIb TFA activates SAPK/JNK and p38 MAPK. Buforin IIb TFA induces mitochondria-dependent Apoptosis. Buforin IIb TFA achieves selective targeting by interacting with gangliosides on the surface of cancer cells, and can penetrate cancer cell membranes without causing damage. Buforin IIb TFA exhibits antibacterial activity against Gram-negative bacteria, Gram-positive bacteria and fungi. Buforin IIb TFA can be used in the research of cervical cancer, as well as cancers including leukemia, central nervous system cancer, ovarian cancer, breast cancer, melanoma, colon cancer, non-small cell lung cancer, renal cancer and prostate cancer.
For research use only. We do not sell to patients.
- Purity : 98.01%
- Formula: C115H207N43O23·xC2HF3O2
- Molecular Weight:2560.15 (free base)
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Storage:
Sealed storage, away from moisture.
Powder -80°C, 2 years , -20°C, 1 year* In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Biological Activity
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Chemical Information
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Solvent & Solubility
- Protocols
- Purity & Documentation
- References
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Help & FAQs
Biological Activity
Description
In Vitro
Buforin IIb (4 μM; 3-24 h) TFA induces time-dependent activation of SAPK/JNK and p38 MAPK in HeLa cells, which is downstream of ER stress and Ca2+ release from the ER[1].
Buforin IIb (4 μM; 3-24 h) TFA induces time-dependent dysregulation of Bcl-2 family proteins, mitochondrial translocation of Bax, and cytochrome c release in HeLa cells, which are downstream of ER stress and MAPK activation[1].
Buforin IIb (0-200 μg/mL; 48 h) TFA potently and selectively kills cancer cells, with IC50 values of 6 μg/mL for Jurkat cells, 12 μg/mL for HeLa cells, 7.2-23.9 μg/mL for 60 diverse human tumor cell lines, and ~350 μg/mL for normal human fibroblasts, mouse embryonic fibroblasts, and peripheral blood lymphocytes[2].
Buforin IIb (20 μg/mL; 24 h) TFA induces mitochondria-dependent apoptosis in Jurkat and HeLa cancer cells, as shown by annexin V/PI staining, DNA fragmentation, and activation of caspase-9, caspase-3, and PARP cleavage[2].
Buforin IIb (24 h) TFA inhibits growth of Escherichia coli K12D31 (MIC 0.4 μM), Bacillus subtilis CGMCC 1.1087, and Saccharomyces cerevisiae CGMCC 2.399 (MIC 1.5 μM) with activity comparable to synthetic buforin IIb[3].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.
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Cell Line:human cervical adenocarcinoma HeLa cells
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Concentration:4 μM
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Incubation Time:3 h, 6 h, 12 h, 24 h
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Result:Caused a time-dependent increase in protein levels of phosphorylated protein kinase-like endoplasmic reticulum kinase (p-PERK, Thr980), phosphorylated inositol-requiring protein 1 (p-IRE1, Ser724), 78 kDa glucose-regulated protein (GRP78), and C/EBP homologous protein (CHOP), a hallmark of ER stress-mediated apoptosis.\nActivated stress-activated protein kinase/Jun-amino-terminal kinase (SAPK/JNK) and p38 mitogen-activated protein kinase (MAPK), with increased phosphorylation detected from 6 h onward.
Blocked activation of both kinases when cells were pretreated with specific MAPK inhibitors (SP600125 for SAPK/JNK, SB203580 for p38 MAPK), as well as by pretreatment with ER stress inhibitor PBA or Ca2+ chelator BAPTA/AM.\nCaused time-dependent downregulation of anti-apoptotic Bcl-xL and Bcl-2.
Increased translocation of pro-apoptotic Bax from the cytosol to mitochondria.
Induced time-dependent release of cytochrome c from mitochondria to the cytosol.
Abolished these effects when cells were pretreated with SAPK/JNK inhibitor SP600125, p38 MAPK inhibitor SB203580, or ER stress inhibitor PBA.
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Cell Line:Jurkat human leukemia cells, HeLa human cervical cancer cells, human fibroblasts, mouse embryonic fibroblasts, peripheral blood lymphocytes, 60 diverse human tumor cell lines (leukemia, CNS cancer, ovarian cancer, breast cancer, melanoma, colon cancer, non-small cell lung cancer, renal cancer, prostate cancer)
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Concentration:0-200 μg/mL
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Incubation Time:48 h
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Result:Exhibited selective cytotoxicity with IC50 values of 6 μg/mL for Jurkat cells, 12 μg/mL for HeLa cells.
Showed potent cytotoxicity against 60 human tumor cell lines with IC50 values ranging from 7.2 μg/mL (HOP-92 non-small cell lung cancer) to 23.9 μg/mL (T-47D breast cancer).
In Vivo
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Animal Model:BALB/c (nu/nu)[2]
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Dosage:5 mg/kg; 10 mg/kg; 20 mg/kg
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Administration:i.v.; days 1, 2, 4, 8
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Result:Suppressed tumor growth compared to PBS controls.
Reduced mean tumor volume substantially relative to control group (~1000 mm3) by study completion (day 20).
Induced statistically significant difference (P < 0.05) in tumor volume compared to controls starting on day 8 through study end.
Chemical Information
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Appearance Solid
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Molecular Weight 2560.15 (free base)
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Formula C115H207N43O23·xC2HF3O2
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Color White to off-white
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SMILES
O=C(N[C@@H](C)C(NCC(N[C@@H](CC(C)C)C(N[C@@H](CCC(N)=O)C(N[C@@H](CC1=CC=CC=C1)C(N2[C@@H](CCC2)C(N[C@@H](C(C)C)C(NCC(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(C)C)C(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(C)C)C(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(C)C)C(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)[C@H](CCCNC(N)=N)N.OC(C(F)(F)F)=O.[x]
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Synonyms
BF2-B TFA
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Sequence
Arg-Ala-Gly-Leu-Gln-Phe-Pro-Val-Gly-Arg-Leu-Leu-Arg-Arg-Leu-Leu-Arg-Arg-Leu-Leu-Arg
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Sequence Shortening
RAGLQFPVGRLLRRLLRRLLR
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Sealed storage, away from moisture
Powder -80°C 2 years -20°C 1 year * In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
Solvent & Solubility
In Vitro:
DMSO : 50 mg/mL (Need ultrasonic; Hygroscopic DMSO has a significant impact on the solubility of product, please use newly opened DMSO)
In Vivo:
Select the appropriate dissolution method based on your experimental animal and administration route.
- For the following dissolution methods, please ensure to first prepare a clear stock solution using an In Vitro approach and then sequentially add co-solvents:
- To ensure reliable experimental results, the clarified stock solution can be appropriately stored based on storage conditions. As for the working solution for In Vivo experiments, it is recommended to prepare freshly and use it on the same day.
- The percentages shown for the solvents indicate their volumetric ratio in the final prepared solution. If precipitation or phase separation occurs during preparation, heat and/or sonication can be used to aid dissolution.
Add each solvent one by one: 10% DMSO 40% PEG300 5% Tween-80 45% Saline
Solubility: ≥ 2.5 mg/mL; Clear solution
This protocol yields a clear solution of ≥ 2.5 mg/mL (saturation unknown).
Taking 1 mL working solution as an example, add 100 μL DMSO stock solution (25.0 mg/mL) to 400 μL PEG300, and mix evenly; then add 50 μL Tween-80 and mix evenly; then add 450 μL Saline to adjust the volume to 1 mL.
Preparation of Saline: Dissolve 0.9 g sodium chloride in ddH₂O and dilute to 100 mL to obtain a clear Saline solution.
Add each solvent one by one: 10% DMSO 90% (20% SBE-β-CD in Saline)
Solubility: ≥ 2.5 mg/mL; Clear solution
This protocol yields a clear solution of ≥ 2.5 mg/mL (saturation unknown).
Taking 1 mL working solution as an example, add 100 μL DMSO stock solution (25.0 mg/mL) to 900 μL 20% SBE-β-CD in Saline, and mix evenly.
Preparation of 20% SBE-β-CD in Saline (4°C, storage for one week): 2 g SBE-β-CD powder is dissolved in 10 mL Saline, completely dissolve until clear.
In Vivo Dissolution Calculator
Please enter the basic information of animal experiments:
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Recommended: Prepare an additional quantity of animals to account for potential losses during experiments.
Please enter your animal formula composition:
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%DMSO +
Recommended: Keep the proportion of DMSO in working solution below 2% if your animal is weak.
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%+
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+%Tween-80 + +
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%Saline +
The co-solvents required include: DMSO, . All of co-solvents are available by MedChemExpress (MCE). , Tween 80. All of co-solvents are available by MedChemExpress (MCE).
Working solution concentration: 0.22 mg/mL
Method for preparing stock solution: mg drug dissolved in μL DMSO. Stock solution concentration: mg/mL. * In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
1. Take μL DMSO stock solution;
2. Add μL .
μL , mix evenly;
3. Then add μL Tween 80, mix evenly;
4. Then add μL
Please ensure that the stock solution in the first step is dissolved to a clear state, and add co-solvents in sequence. You can use ultrasonic heating (ultrasonic cleaner, recommended frequency 20-40 kHz), vortexing, etc. to assist dissolution.
Protocols
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Research Protocol for Infectious Diseases
Infectious-disease experiments test how pathogens interact with host barriers, innate immune receptors, inflammatory signaling, pathogen replication, and tissue injury; pattern-recognition receptors such as TLRs, RIG-I-like receptors, NOD-like receptors, and inflammasomes detect microbial molecules and activate NF-κB, interferon, and cytokine responses. The central hypothesis is that infection severity reflects the balance between pathogen burden and host response: protective inflammation restricts pathogen growth, whereas excessive or mislocalized inflammation contributes to tissue damage and disease phenotype. Unresolved questions include which host pathways are protective versus pathogenic, why some infection models fail to translate to human disease, and which combined readouts best predict clinically relevant infection outcomes.
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Apoptosis
Apoptosis, also called programmed cell death, is generally characterized by distinct morphological characteristics.
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TUNEL staining for apoptotic DNA fragmentation
TUNEL staining detects DNA strand breaks by using terminal deoxynucleotidyl transferase to add labeled nucleotides to exposed 3′-OH DNA termini, generating either microscopic staining in fixed cells or tissue sections, or fluorescence/cytometric signal in cell suspensions. TUNEL positivity reflects DNA fragmentation but should not be interpreted alone as definitive apoptosis, because TUNEL can also label necrotic, autolytic, mechanically damaged, or DNA-repair-associated DNA breaks.
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Annexin V plus membrane-impermeant dye apoptosis staining
Annexin V-based apoptosis assays rely on the detection of phosphatidylserine (PS) externalization from the inner leaflet of the plasma membrane to the outer leaflet, an early biochemical hallmark of apoptosis. Fluorescently labeled Annexin V binds PS in a calcium-dependent manner, enabling identification of early apoptotic cells by flow cytometry or fluorescence microscopy. When combined with a membrane-impermeant DNA-binding dye (e. g. , propidium iodide), this approach allows discrimination between viable (Annexin V−/dye−), early apoptotic (Annexin V+/dye−), and late apoptotic or necrotic (Annexin V+/dye+) cell populations by assessing membrane integrity and PS exposure.
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Apoptosis Solutions
Apoptosis is a regulated, generally non-lytic cell-death pathway that removes unwanted, damaged, infected, or abnormal cells through coordinated morphological changes, caspase activation, DNA fragmentation, and membrane remodeling. The intrinsic apoptosis pathway is controlled mainly by mitochondrial outer membrane permeabilization, BCL-2 family proteins, cytochrome c release, apoptosome formation, caspase-9 activation, and downstream executioner caspase-3/7 activation. The extrinsic apoptosis pathway is initiated by death receptors such as Fas, TNFR, and TRAIL receptors, which recruit adaptor proteins and activate caspase-8 before engaging executioner caspases or mitochondrial amplification through BID cleavage. Apoptosis is linked to many phenotypes, including cancer cell killing, tissue homeostasis, immune regulation, neurodegeneration, infection response, and treatment-induced cytotoxicity; unresolved questions include how apoptosis interacts with necroptosis, pyroptosis, ferroptos
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Gram Staining of Tissue Sections
Gram staining of tissue sections is a histochemical technique used to differentiate Gram-positive and Gram-negative bacteria within histological specimens based on differences in bacterial cell wall structure and dye retention, adapted from classical bacteriological Gram staining into tissue-compatible “histological Gram stain” variants. In tissue applications, modifications of the Brown-Hopps and Brown-Brenn methods are commonly used to improve differentiation of microorganisms embedded within host connective tissue and to reduce overstaining or loss of Gram-negative signal, which are known limitations of earlier approaches. The principle relies on crystal violet-iodine complex retention in Gram-positive organisms and subsequent decolorization and counterstaining steps that allow contrast visualization of Gram-negative organisms against tissue background.
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Bacterial live/dead nucleic-acid viability staining
The LIVE/DEAD bacterial viability staining method is based on differential permeability of nucleic-acid-binding fluorescent dyes, most commonly SYTO 9 and propidium iodide (PI), which enables discrimination of bacterial populations with intact versus compromised cytoplasmic membranes. SYTO 9 penetrates both intact and damaged bacterial membranes and binds nucleic acids to produce green fluorescence, whereas propidium iodide penetrates only cells with compromised membranes and fluoresces red while also reducing SYTO 9 signal through competitive binding and fluorescence interactions. The resulting fluorescence pattern is interpreted as a proxy for membrane integrity, which is widely used as an indicator of bacterial viability in microscopy, flow cytometry, and spectroscopic platforms. However, mechanistic studies show that SYTO 9 and PI interactions involve displacement and fluorescence resonance energy transfer effects, which can influence signal interpretation depending on dye ratios a
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Breast Cancer Modeling
Breast cancer is a heterogeneous cancer, and it has been distinguished into four subtypes: luminal A, luminal B, HER2-positive and basal-like. Molecular mutations, epigenetic alterations, hormone exposure and immune microenvironment are related to the progression of breast cancer.
Purity & Documentation
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Data Sheet (293 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[2]. Lee HS, et al. Mechanism of anticancer activity of buforin IIb, a histone H2A-derived peptide. Cancer letters. 2008 Nov 18;271(1):47-55. [Content Brief]
[3]. Wang Q, et al. Expression and purification of antimicrobial peptide buforin IIb in Escherichia coli. Biotechnology letters. 2011 Nov;33(11):2121-6. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Buforin IIb TFA Related Classifications
HY-P12127A Related Classifications
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