Drug Database
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

PubMedBMC surgery2026-05-24

The influence of different bariatric surgeries on male sex hormones and semen parameters among infertile obese male patients: an observational study.

Azhary Mahmoud M, Ali Mohamed Hassan MH, AbdELsalam Mohamed Ahmed MA, Elshal Mohamed M et al.

This research examines the impact of bariatric procedures on male sex hormones and semen parameters in infertile men with obesity. Obesity adversely affects male fertility by causing hormonal imbalances and worsening semen quality. Metabolic and bariatric surgery (MBS) offers sustained weight loss and potential reversal of these abnormalities. This prospective case series included 43 infertile men with severe obesity who underwent sleeve gastrectomy, One-anastomosis gastric bypass (OAGB), or Roux-en-Y gastric bypass. All participants had a BMI ≥ 35 kg/m² and a history of infertility for over one year. Semen analysis and hormonal profiling (FSH, LH, total testosterone, estradiol [E2], and prolactin) were conducted preoperatively and at 3, 6, and 12 months postoperatively. Significant weight loss was observed at all follow-up points (p ≤ 0.003). Improvements were noted in semen motility, progressive motility, vitality, and abnormal forms (all p ≤ 0.003). Serum testosterone levels increased, while estradiol levels decreased significantly (p ≤ 0.003). Changes in FSH, LH, and prolactin were statistically insignificant. Metabolic and bariatric surgery (MBS) is associated with marked improvements in semen quality and serum testosterone levels, supporting its role as an effective therapeutic strategy for obesity-related male infertility. No pregnancies were recorded during the 12-month follow-up. Not applicable.

PMID 42177498
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PubMedThe protein journal2026-05-24

Cloning, Expression, Purification and Biochemical Characterization of Novel Thermostable Subtilisin-like Serine Protease from Thermococcus onnurineus NA1.

Jiddah Nafiu Usman NU, Ajingi Ya'u Sabo YS, Adam Abubakar Sunusi AS, Panbangred Watanalai W et al.

The persistent rise in demand for biocatalysts in industries has prompted the exploration of novel enzymes. Proteases are very important class of enzymes with many industrial applications. However, majority of the reported proteases are from mesophiles and exhibit low stability under harsh conditions limiting their potential applications. This study presents the expression and characterization of a novel thermostable recombinant subtilisin-like serine protease derived from Thermococcus onnurineus NA1. The subtilisin serine protease gene was successfully cloned and expressed in E. coli BL21. The recombinant protease was purified by affinity chromatography and has an estimated molecular mass of 29 kDa following SDS-PAGE analysis. It exhibited an optimal activity at a pH of 10 and temperature of 90 °C. The recombinant subtilisin-like serine protease maintained 96% of its activity at 100 °C. Additionally, Na+, Mg2+, Cu2+, and Mn2+ had minimal effect on the recombinant protease activity whereas the presence of Ca2+ significantly enhanced the enzyme activity. Interestingly, the recombinant protease was stable in the presence of different surfactants and inhibitors. These properties illustrate the potential of recombinant subtilisin-like serine protease for industrial applications.

PMID 42177730
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PubMedBiochemical and biophysical research communications2026-05-24

Adrenocorticotropin hormone regulates sphingosine-1-phosphate synthesis via cortisol in bovine adrenocortical cells.

Medina-Moctezuma Zaire Belen ZB, Guzmán-Sánchez Adrian A, González-Aretia David D, Gutiérrez Carlos G CG et al.

Follicle-stimulating hormone (FSH) and luteinizing hormone (LH) stimulate the synthesis of sphingosine-1 phosphate (S1P) in Gs-coupled receptors dependent manner, enabling S1P to mediate specific bioactivities of FSH and LH. Because adrenocorticotropic hormone (ACTH) also acts via a Gs-coupled receptor to regulate adrenal cortex function, we hypothesized that ACTH could induce S1P secretion in adrenocortical cells, which could then mediate the steroidogenic and number of viable cells effects associated with ACTH. Primary bovine adrenocortical cell cultures were treated with ACTH, and number of viable cells, as well as S1P and cortisol concentrations in the culture media were measured. The effects of exogenous cortisol on number of viable cells, S1P and phosphorylated SPHK1 concentrations were also determined. Results show that the addition of 0.001 μM and 0.1 μM ACTH to the culture medium increased the number of viable adrenocortical cells, and the concentration of cortisol in culture media, respectively. However, ACTH addition did not increase S1P concentrations. Interestingly, a negative correlation between S1P and cortisol concentrations in the culture medium was observed. Moreover, while addition of 0.1 ng/mL cortisol increased S1P and phosphorylated SPHK1 concentrations, increasing cortisol from 1 to 10 ng/mL did not affect phosphorylated SPHK1 but reduced S1P concentration. Thus, while our data suggest that ACTH does not promote S1P synthesis; by stimulating cortisol synthesis, ACTH could be involved in regulation of S1P levels in bovine adrenocortical cells.

PMID 42176386
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PubMedGynecological endocrinology : the official journal of the International Society of Gynecological Endocrinology2026-05-24

Restoring ovulation in functional hypothalamic amenorrhea: impact of polycystic ovarian morphology on hormonal response to pulsatile GnRH.

Boegl Magdalena M, Kasper Isabella I, Dewailly Didier D, Mayrhofer Daniel D et al.

Up to 50% of women with functional hypothalamic amenorrhea (FHA) exhibit polycystic ovarian morphology (PCOM) on ultrasound. We aimed to compare the hormonal response to ovulation induction with pulsatile GnRH therapy in FHA patients with and without PCOM. In this single-center observational study, 41 patients with FHA underwent 3 months of pulsatile GnRH therapy to induce ovulation. Patients were categorized into a PCOM group (n = 24) and a non-PCOM group (n = 17). Serum levels of Anti-Muellerian-hormone (AMH), follicle-stimulating hormone (FSH), luteinizing hormone (LH), estradiol, prolactin, sex hormone-binding globulin (SHBG), testosterone, and thyroid-stimulating hormone (TSH) were assessed at baseline and after 3 months of treatment. At baseline, median AMH levels were significantly higher in the PCOM group (6.21 ng/ml [IQR 4.03-8.87]) compared to the non-PCOM group (1.7 ng/ml [IQR 1.14-2.20]; p < 0.001). After 3 months of pulsatile GnRH therapy, AMH levels significantly increased in the non-PCOM group (1.94 [IQR 1.39-2.49], p < 0.001), whereas no significant change was observed in the PCOM group (p = 0.218). LH, FSH, and estradiol levels increased in both groups. Pulsatile GnRH therapy effectively induced ovulation (1 dominant follicle in each patient), irrespective of ovarian morphology. The significant AMH rise in women with FHA without PCOM likely reflects restored folliculogenesis. In contrast, the absence of an AMH rise in the PCOM group was expected, given their already elevated baseline levels. Importantly, these findings suggest that pulsatile GnRH therapy does not exacerbate AMH levels in most patients.

PMID 42176250
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PubMedVeterinary parasitology2026-05-24

Recombinant PsoSP4 confers superior 80% protection against psoroptic mange in rabbits in association with a Th1-biased immune response.

Gu X B XB, Wu F Y FY, Hao G Y GY, JiPo E H Z EHZ et al.

Psoroptic mange, caused by Psoroptes ovis, is a severe global ectoparasitic disease for which no commercial vaccine is available. Here, we evaluated four recombinant P. ovis proteins (rPsoSP4, rPsoPRF, rPsoMIF, and rPsoSP5) as subunit vaccine candidates in a rabbit model. Three antigens conferred significant and graded protection, with final protection rates of 80% (rPsoSP4), 60% (rPsoPRF) and 20% (rPsoMIF), compared to 0% in the control and rPsoSP5-vaccinated groups. The lead candidate, rPsoSP4, reduced ear lesion scores, crust weights, and mite burden by up to 88.57%, 88.30%, and 81.80%, respectively. To our knowledge, rPsoSP4 is the most efficacious defined antigen against psoroptic mange reported to date, outperforming the previously tested single recombinant antigen and even a seven-protein cocktail vaccine. Mechanistically, protection correlated with a balanced, Th1-skewed immune signature. The high-level protection conferred by rPsoSP4 was characterized by elevated IFN-γ coupled with restrained Th-17A levels. In contrast, the non-protective rPsoSP5 vaccine elicited a singularly skewed Th17 response. Furthermore, antigen-specific IgG levels did not always correlate positively with protection (rPsoSP5), but a moderate yet significant elevation in total IgE was observed in the protected groups (rPsoPRF, rPsoMIF). This suggests a potential contributory role for IgE-mediated effector mechanisms in the anti-mite response. Our results identify rPsoSP4 as a highly efficacious single-antigen vaccine candidate and validate rPsoPRF and rPsoMIF as viable alternatives.

PMID 42176370
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PubMedVaccine2026-05-24

Evaluation of EcoCRM, virus-like particles, and mRNA as vaccine platforms against Borrelia burgdorferi.

Rocuskie-Marker Carleena M CM, Huckaby Annalisa B AB, Conaway Olivia M OM, Pyles Gage M GM et al.

Lyme disease (LD) is the most prevalent vector-borne disease in the United States, impacting ∼476,000 individuals annually with increasing incidence. Prevention relies on personal protective measures such as insecticides and tick checks, underscoring the need for new preventatives such as vaccines. In this work, the importance of vaccine platform in LD vaccine development efforts was evaluated using non-lipidated OspA as model antigen. Recombinant OspA conjugated to CRM197 (EcoCRM OspA), a virus-like particle vaccine utilizing SpyTag and SpyCatcher (OspA-SpyVLP), and an mRNA-based vaccine construct (OspA mRNA) were evaluated and compared in C3H mice using the needle injection challenge model. To determine immunogenicity, anti-OspA and anti-B. burgdorferi antibodies were quantified via ELISA and further assessed by measuring IgG subclass, antibody avidity, and presence of antibody secreting cells. All vaccine formulations were immunogenic and led to the release of similar levels of antigen-specific IgG in serum during the duration of the experiment. However, there were significant differences around two week post-boost in the presence of antibody secreting cells, ratio of IgG1/IgG2 subclasses, and antibody avidity between platforms. Protection was measured using PCR and darkfield microscopy to determine organ positivity post-challenge. Vaccination with recombinant non-lipidated OspA and OspA-SpyVLP significantly reduced the number of positive organs compared to the PBS challenged control group. Lastly, in vitro borreliacidal activity was quantified via darkfield microscopy and the highest borreliacidal activity was observed using OspA-SpyVLP sera, with titers 16-fold higher than recombinant OspA. Altogether, these data indicated that selection of vaccine platform/formulation influenced the immunogenicity and efficacy of OspA-based LD vaccines and should be considered during development.

PMID 42176436
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