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Human FGF basic (154aa) Protein, premium grade

分子别名(Synonym)

FGF2,BFGF,FGFB,FGF basic,HBGF-2

表达区间及表达系统(Source)

Human FGF basic (154aa) Protein, premium grade (BFF-H5115) is expressed from E. coli cells. It contains AA Ala 135 - Ser 288 (Accession # NP_001997.5).

Predicted N-terminus: Met

It is produced under our rigorous quality control system that incorporates a comprehensive set of tests including sterility and endotoxin tests. Product performance is carefully validated and tested for compatibility for cell culture use or any other applications in the early preclinical stage. When ready to transition into later clinical phases, we also offer a custom GMP protein service that tailors to your needs. We will work with you to customize and develop a GMP-grade product in accordance with your requests that also meets the requirements for raw and ancillary materials use in cell manufacturing of cell-based therapies.

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蛋白结构(Molecular Characterization)

FGF basic Structure

This protein carries no "tag".

The protein has a calculated MW of 17.3 kDa. The protein migrates as 15-17 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

内毒素(Endotoxin)

Less than 0.01 EU per μg by the LAL method.

宿主蛋白残留(Host Cell Protein)

<0.5 ng/µg of protein tested by ELISA.

宿主核酸残留(Host Cell DNA)

<0.02 ng/μg of protein tested by qPCR.

无菌(Sterility)

Negative

支原体(Mycoplasma)

Negative.

纯度(Purity)

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

FGF basic SDS-PAGE

Human FGF basic (154aa) Protein, premium grade on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

FGF basic SEC-MALS

The purity of Human FGF basic (154aa) Protein, premium grade (Cat. No. BFF-H5115) is more than 90% and the molecular weight of this protein is around 15-25 kDa verified by SEC-MALS.

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活性(Bioactivity)-ELISA

FGF basic ELISA

Immobilized Human FGF basic (154aa) Protein, premium grade (Cat. No. BFF-H5115) at 2 μg/mL (100 μL/well) can bind Human FGF R2 (IIIb), Fc Tag (Cat. No. FGB-H5256) with a linear range of 0.2-8 ng/mL (QC tested).

Protocol

FGF basic ELISA

Immobilized Human FGF basic (154aa) Protein, premium grade (Cat. No. BFF-H5115) at 2 μg/mL (100 μL/well) can bind Human Glypican 3 Protein, Fc Tag (Cat. No. GP3-H5258) with a linear range of 0.2-8 ng/mL (Routinely tested).

Protocol

FGF basic ELISA

Immobilized Human FGF basic (154aa) Protein, premium grade (Cat. No. BFF-H5115) at 2 μg/mL (100 μL/well) can bind Human Glypican 1, Fc Tag (Cat. No. GP1-H5254) with a linear range of 0.2-8 ng/mL (Routinely tested).

Protocol

 
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背景(Background)

FGF basic (also known as FGF2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3). Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4 - 6). The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9). The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss). It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10). In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11). Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12). The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13). There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7). Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14).

 

前沿进展

In vitro performance of a charcoal capturing device with desflurane
Hoffmann, Jouwena, De Wolf et al
Anesthesiology (2025)
Abstract: The use of capturing devices may become required for the continued use desflurane. We tested the percentage of desflurane captured by a charcoal filter (CONTRAfluran)-workstation (Aisys) combination in vitro.Desflurane in O2/air was administered via an Aisys workstation into a 2 L test lung that was insufflated with CO2 (160 mL/min). First, to confirm all vaporized desflurane reached the capturing device, the amount of desflurane collected in a Douglas bag attached to the machine exhaust was compared to the vaporized amount during 15 min runs with the following fresh gas flow (FGF)//vaporizer setting combinations: (L/min // %): 0.3//8, 0.5//8, 1//6, 2//6, 3//6, 4//6, 5//6, and 6//6. Next, to determine the effect of CO2, the capturing device weight gain was measured with the same FGF ran over 1 hour but without desflurane. Finally, the ratio of the capturing device weight gain / vaporizer weight loss (= performance, expressed in %) was determined for the same 15 min runs with desflurane vaporizer settings described above. All experiments were arbitrarily repeated five times.The amount of vaporized desflurane did not differ from the amount collected in the Douglas bag. When CO2, O2, and air were delivered without desflurane, the capturing device lost a relatively small amount of weight (<5 g), especially with FGF ≤ 1 L/min. Finally, performance with 0.3, 0.5-2 and 3-6L/min FGF was 103, 100, and 95 - 93 %, respectively.CONTRAfluran charcoal filter in vitro performance for desflurane in O2/air combined with the Aisys workstation ranged from 93-103 % with FGF of 0.3 to 3-6 L/min with vaporizer settings that reflect clinical conditions. Defining the place of charcoal filters in clinical practice requires full life cycle analysis of both the charcoal and inhaled agent.Copyright © 2025 American Society of Anesthesiologists. All Rights Reserved.
Human-induced pluripotent stem cell-derived exosomes promote skin wound healing through activating FGF2-mediated p38 pathway
Zhang, Wu, Peng et al
Mol Cell Biochem (2025)
Abstract: The acute and large area skin healing has been an intractable problem for both clinician and patient. Exosomes derived from human-induced pluripotent stem cells (hiPSC-Exos) have been a novel promising cell-free treatment on skin damage repair. In this study, in vivo skin trauma model of full-layer skin damage on mouse back and in vitro skin-like trauma model of human keratinocytes (HaCaT) scratches were established to investigate the effects of hiPSC-Exos on the acute wound healing, and its potential regulation mechanism would be tried to explore. Our in vivo results showed that hiPSC-Exos labeled with PKH26 could be well taken up by cells in the wound area, and could effectively accelerate acute skin wound healing by inhibiting the mRNA expressions of inflammation factors and chemokines such as Il-1β, Ccl2, Cxcl5, Ccl7 as well as promoting PCNA positive cell ratio. The in vitro data showed that hiPCS-Exos could markedly increase the numbers of EdU positive keratinocytes and expedite keratinocyte migration, which could be reversed by fibroblast growth factor receptor 3 (FGFR3) antagonist AZD4547 and p38 inhibitor SB203580. In addition, fibroblast growth factor 2 (FGF-2) was existent in hiPSC-Exos, and hiPSC-Exos could upregulate the p-p38/p38 level, which could be significantly reversed by AZD4547, but not affect the p-ERK/ERK and p-JNK/JNK levels in wound model tissues and cells. In conclusion, hiPSC-Exos may have the potential to promote wound healing by inhibiting cell inflammation as well as promoting cell proliferation and migration based on inherent FGF-2 targeting to FGFR3 to activate p38 pathway, which may serve as a promising candidate for skin healing.© 2025. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
Anti-Osteoporosis and Bone Protective Effects of Resveratrol in Rats With Chronic Kidney Disease-Induced Osteoporosis
Zhao, Zhu, Hao et al
Mol Nutr Food Res (2025)
Abstract: Chronic kidney disease (CKD)-induced osteoporosis is a new concept that implies CKD-related impaired bone quality. Resveratrol (RES) is a natural component, known for its anti-inflammatory and anti-osteoporotic effects. In the present study, we aimed to investigate the bone-protective and anti-osteoporotic effects of resveratrol in rats with chronic kidney disease-induced osteoporosis. The 5/6th nephrectomy (Nx) model of CKD was established. Resveratrol and alendronate (ALN), as standard drug, were administered for 45 days. Blood samples and femurs were collected and subjected to molecular analysis, micro-CT, and bone mechanical tests. The results showed a significant decrease in Ca levels but no significant changes in 1,25 vitamin D and phosphorus levels in untreated and treated CKD groups. Treatment with RES and ALN did not reverse the increase of serum parathyroid hormone while reducing the elevated FGF-23 levels. Unlike ALN, RES had no significant effect on increased alkaline phosphatas levels or decreased osteocalcin and OPG levels in CKD rats. Moreover, results showed that RES reversed the increase of RANKL and TRAP in serum and femur tissue close to the control level, leading to an improvement in bone strength and microarchitecture. In conclusion, the present study showed beneficial anti-osteoporotic effects of RES on CKD-induced osteoporosis.© 2025 Wiley‐VCH GmbH.
Efficacy of Human Dental-Pulp MSCs Modified by Double-genes on Wound Healing in Diabetic-Foot Model
Zhu, Meng, Yang et al
Curr Stem Cell Res Ther (2025)
Abstract: Diabetic foot (DF) poses a great challenge to us due to its poor therapeutic effect. To seek a new cure, the human dental pulp mesenchymal stem cells (hDP-MSCs) were modified by vascular endothelial growth factor A (VEGFA) and basic fibroblast growth factor (bFGF) (hEDP-MSCs) to investigate their curative effect on DF wound in animal models.Forty-eight rats with DF constructed with streptozotocin and ligation of femoral arteries, were randomly divided into six equal groups, which respectively received an intramuscular injection of normal saline (Control group), hDP-MSCs, VEGFA-modified hDP-MSCs, bFGF-- modified hDP-MSCs, hEDP-MSCs, and Ad.VEGF.FGF (Ad.FV). The tissues around DF wound were collected to investigate the level of CD31, alpha-smooth muscle actin (α-SMA), and cytokines. The expression of Notch1, Hes1, and CD105 were assessed via Quantitative Real-Time Polymerase Chain Reaction (qRT-PCR) after administration.The hEDP-MSCs increased capillaries and decreased wound area (%). QRT-PCR showed that hEDP-MSCs over-expressed the mRNA of Notch1, hairy and enhancer of split 1 and CD105 in peri-wound tissue post-treatment. Meanwhile, the hEDP-MSCs expressed more CD31 and α-SMA than other groups. The hEDP-MSCs expressed more VEGFA and bFGF than hDP-MSCs, and yet less than Ad.FV. Compared with hDP-MSCs, the hEDP-MSCs down-regulated the expressions of interleukin-1 beta (IL-1β), interleukin (IL-6), and tissue necrosis factor α (TNF-a) post-treatment.This study highlights the curative effect of hEDP-MSCs in the wound healing process, and demonstrates the decisive function of hEDP-MSCs in promoting angiogenesis and reducing inflammation.Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
Showing 1-4 of 3877 papers.
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FGF basic靶点信息
英文全称:Fibroblast growth factor 2
中文全称:成纤维细胞生长因子2
种类:Homo sapiens
上市药物数量:1详情
临床药物数量:3详情
最高研发阶段:批准上市
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