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RE

recombinant FSH (FostiRel)

✓ Approved

Reliance Life Sciences Private Limited · FSHR · Recombinant Proteins

What is recombinant FSH?

recombinant FSH is a recombinant proteins developed by Reliance Life Sciences Private Limited. It is approved for therapeutic indications via injectable (others) or subcutaneous injection.

Drug Profile

Brand NamesFostiRel
CompanyReliance Life Sciences Private Limited
Drug ClassRecombinant Proteins
Molecular TargetFSHR
RouteInjectable (Others), Subcutaneous Injection
StatusApproved
Sources: ClinicalTrials.gov, Reliance Life Sciences Private Limited

Mechanism of Action

Molecular Targets

recombinant FSH acts on 1 molecular target:

FSHRfollicle stimulating hormone receptor (FSHRO, ODG1)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

recombinant FSH is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Reproductive system and breast disordersInfertility female✓ Approved

Related Research Articles

PubMedJournal of invertebrate pathology2026-08-30

Bombyx mori lipase-1 reduces viral replication and proliferation by inhibiting the expression of the DNA-binding protein (dbp) gene.

Chen Haiyu H, Ding Xiangrui X, Wang Jinyang J, Zhao Qiaoling Q et al.

Bombyx mori lipase-1 (Bmlipase-1) has strong anti-BmNPV activity, but the mechanism by which Bmlipase-1 resists BmNPV invasion has not been elucidated so far. In this paper, based on the construction of recombinant viruses overexpressing Bmlipase-1, we analyzed the effects of the recombinant viruses on the genes related to recombinant virus replication as well as viral replication and proliferation after the recombinant viruses infected BmN cells. In the presence of the virus, Bmlipase-1 localizes to the cell nucleus. Quantitative polymerase chain reaction (qPCR), northern blotting and western blot analyses showed that Bmlipase-1 inhibited the expression of BmNPV DNA-binding protein (dbp) as well as the replication and proliferation of the recombinant virus. DBP is a key factor for normal viral DNA replication and for the stabilization of nascent viral DNA. A biotin-labeled probe was synthesized around the c-Myb transcription factor binding site in the upstream promoter region of dbp and analyzed by EMSA with prokaryotically expressed and purified Bmlipase-1. It was found that Bmlipase-1 could bind to CACTTCAATT in the dbp promoter region, while the activity of the dbp promoter lacking CACTTCAATT was significantly reduced. In conclusion, Bmlipase-1 can bind to the CACTTCAATT motif on the dbp promoter in vitro, and this motif contributes positively to the activity of the dbp promoter. Overexpression of Bmlipase-1 significantly downregulates dbp expression and inhibits viral replication. Based on these findings, we propose the following hypothesis: Bmlipase-1 may inhibit viral replication by binding to the CACTTCAATT motif and interfering with the transcriptional regulation of dbp. However, this regulatory model requires further validation in the context of viral infection. This paper provides a new theoretical basis for the prevention and control of lepidopteran insect viruses, and also opens up a new way to study the antiviral mechanism of the silkworm, Bombyx mori.

PMID 42669400
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PubMedActa tropica2026-08-30

Recombinant Toxoplasma gondii expressing FIPV spike protein S1 subunit: A proof-of-concept approach against toxoplasmosis and feline infectious peritonitis.

Xie Fujie F, Jiang Xinyu X, Yang Yilin Y, Xie Yuehua Y et al.

Feline infectious peritonitis virus (FIPV) is a lethal feline pathogen with no widely effective prophylactic vaccine available. To address this unmet need, we explored the feasibility of using Toxoplasma gondii (whose definitive host is felids) as a live delivery platform to develop a bivalent vector vaccine. We generated a transgenic T. gondii strain engineered to express and secrete the FIPV spike protein S1 subunit into the parasitophorous vacuole. Immunization in mice confirmed the immunogenicity of this recombinant parasite, which induced specific antibody responses targeting both the T. gondii vector and the FIPV S1 antigen. In vitro neutralization assays revealed limited FIPV-neutralizing capacity in immune sera, with only low-level inhibitory activity observed at the lowest serum dilution, which was markedly inferior to the neutralization potency induced by recombinant S1 protein vaccination. Collectively, these data preliminarily verify the potential of T. gondii as a multivalent antigen delivery vector. This work provides a proof-of-concept framework for a dual-target vaccination strategy intended to mitigate the epidemiological burden of both FIPV and T. gondii in cats, and underpins integrated One Health-oriented disease prevention and control efforts.

PMID 42669354
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PubMedMicrobial cell factories2026-08-30

Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.

El-Sayed Ghada M GM, Wehaidy Hala R HR, Kholif Adel M M AMM, Salama Walaa H WH et al.

Thermostable and alkaline lipases are of significant interest for industrial applications, particularly in detergents and food processing. This study aimed to isolate, clone, and express lipase-encoding genes from a potent bacterial source to produce a thermo-tolerant alkaline lipase with enhanced catalytic efficiency and practical applicability. Among several bacterial isolates, the most potent lipase producer was identified as Lysinibacillus fusiformis, and its 16 S rRNA sequence was deposited in GenBank (PP757498). Three lipase-encoding genes (est, est2, and lipA) were successfully isolated, cloned, and heterologously expressed in Escherichia coli BL21 (DE3). Their sequences were submitted to GenBank under accession numbers PX136937.1, PX136938.1, and PX136936.1, respectively. The recombinant lipase encoded by lipA (rLipase) exhibited the highest activity (150 U/mL) compared with the native enzyme (56.2 U/mL). Molecular docking analysis demonstrated strong binding affinity of rLipase toward major fatty acid derivatives in olive oil, with the highest affinity for linoleic acid (- 8.0 kcal/mol), followed by oleic acid (- 7.8 kcal/mol) and palmitic acid (- 7.3 kcal/mol). These interactions were stabilized by hydrophobic interactions and hydrogen bonding, with key contributions from critical amino acid residues, particularly VAL250. The partially purified recombinant lipase (rLipase) exhibited a maximum activity of 320 U/mL at 80 °C and pH 9, demonstrating remarkable thermostability and alkaline tolerance. Functional evaluation showed that rLipase improved the detergent efficiency for oil stain-removal from cotton fabrics. In addition, supplementation with 0.4% rLipase accelerated Ras cheese ripening by shortening the maturation period from 120 to 90 days with maintaining the desired ripening process. The recombinant lipase from Lysinibacillus fusiformis demonstrated high thermal stability, alkaline tolerance, and strong catalytic efficiency. Its effectiveness in detergent formulations and cheese ripening highlights its potential as a versatile industrial biocatalyst for lipid bioconversion and related applications.

PMID 42668381
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PubMedJournal of microbiological methods2026-08-30

Development of an A7G variant of recombinant human G-CSF for improved fibroblast-mediated wound healing.

Thota Sujani S, Myneni Praveen P, Venkateswarulu T C TC

Recombinant human granulocyte colony-stimulating factor (rh-G-CSF) is useful in tissue regeneration due to its angiogenic and anti-inflammatory actions. The current study focused on the downstream process of A7G mutant rh-G-CSF (m-rh-G-CSF) and the effects of m-rh-G-CSF on human fibroblasts. The m-rh-G-CSF was purified and had 97.24% purity, a final protein concentration of 0.814 g/L and a molecular weight of 18,784 Da. The addition of m-rh-G-CSF significantly elevated the ATP level in the treated cells in a concentration-dependent manner. The maximal ATP level was achieved at a concentration of 2.5 μg/mL and was 89% higher than in the control cells and 13% higher than in reference rh-G-CSF. In the scratch-wound assay, 92.67% and 98.69% wound closure were observed at 24 and 48 h after the addition of m-rh-G-CSF, respectively, compared with 49.93% in control cells at 48 h. These findings support the potential of m-rh-G-CSF as a therapeutic candidate for fibroblast-mediated wound healing.

PMID 42669396
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PubMedPediatric research2026-08-30

A recombinant fragment of human surfactant protein D reduces lung inflammation in preterm lambs.

Castillo-Hernandez Tania F TF, Finkielsztein Ariel A, Bhatt Reena R, Panichi Daniele D et al.

Bronchopulmonary dysplasia (BPD), the major chronic respiratory morbidity in extremely preterm infants, is largely driven by inflammation. Preterm lungs are deficient of surfactant protein D (SP-D), an immunomodulatory protein absent in current commercial surfactant preparations. We hypothesised that using a recombinant fragment of human SP-D (rfhSP-D) as an adjuvant to exogenous surfactant therapy would reduce ventilator-induced inflammation. We utilised a preterm lamb model of ventilator-associated lung injury. Mechanically ventilated preterm lambs were randomised into control and two treated groups, receiving endotracheal surfactant at 15 min post-delivery. Physiological parameters were measured throughout the experiment. Lung tissue was analysed for changes in alveolar architecture and expression levels of pro-inflammatory cytokines. Bronchioalveolar lavage (BAL) was analysed for SP-D concentration, and inflammatory cells. Intratracheal administration of rfhSP-D improved respiratory outcomes, significantly increased airspace and lung compliance in treated groups. Treated lambs also showed a reduction in lung tissue gene expression of inflammatory cytokines and inflammatory cell counts. Intratracheal administration of rfhSP-D did not negatively impact standard surfactant therapy and appeared to complement it. The administration of rfhSP-D as an adjuvant to standard surfactant therapy effectively reduced lung inflammation supporting the potential therapeutic use of rfhSP-D for preterm infants at risk of developing BPD. We have successfully developed and tested a novel recombinant fragment of human surfactant protein D (rfhSP-D) capable of reducing ventilator-associated lung inflammation in a pre-term lamb model. These results suggest rfhSP-D may be a novel potentially useful therapy for Bronchopulmonary dysplasia (BPD) in combination with currently available surfactant replacement therapies and serves as justification for a first in human clinical trial in mechanically ventilated infants. If successful, rfhSP-D could become a therapeutic candidate to mitigate pulmonary inflammation and improve lung outcomes, potentially offering a novel therapeutic avenue in the prevention or management of BPD.

PMID 42668280
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PubMedBiochemistry. Biokhimiia2026-08-30

Structural and Functional Analysis of the Recombinant Aureobasidium pullulans Cutinase Variants for Efficient Polycaprolactone Degradation.

Ermilov Filipp K FK, Eneiskaya Elena V EV, Panasenko Svetlana A SA, Zhurishkina Elena V EV et al.

Polycaprolactone (PCL) is a biodegradable polyester widely used in industry, but it degrades slowly in the environment. Enzymatic hydrolysis catalyzed by cutinases represents a promising approach for PCL waste utilization. Through screening, we selected the Aureobasidium pullulans VKM 1116 strain capable of degrading PCL. We amplified the ApCUT1 cutinase gene from the A. pullulans VKM 1116 genomic DNA. Heterologous expression in Komagataella phaffii yielded ~60 mg/L of the target protein. The recombinant enzyme exhibited maximum activity at pH 6.0-6.5 and 30-40°C. Using site-directed mutagenesis, we generated single mutants (Y58W and L186F) and a double mutant (Y58W/L186F). The double mutant demonstrated the highest catalytic efficiency toward the model substrate 4-nitrophenyl 16-methylsulfonyl hexadecanoate (4-NP-(16-MS-C16)), exhibiting a two-fold increase in the hydrolysis rate compared to the wild-type enzyme. During PCL hydrolysis, the Y58W mutant showed the highest activity, providing a 1.8-fold increase in the suspension degradation rate and complete polymer granule degradation at a rate of 1 mg/h per 1 mg of protein. Our molecular modeling suggests that the hydrophobic bridge at the entrance to the active site functions as a "molecular trap." For the low-molecular-weight substrate (4-NP-(16-MS-C16)), enzymatic activity is limited by the kinetics of the substrate retention step, which is consistent with the maximum catalytic efficiency of the Y58W/L186F mutant with a closing trap. Conversely, activity toward PCL is limited by the initial adsorption stage, for which an open conformation of the free enzyme - as observed in the Y58W variant - is critically important. These results demonstrate the potential of the ApCUT1_Y58W cutinase for developing advanced PCL recycling technologies.

PMID 42669564
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