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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

PubMedMicrobial cell factories2026-10-15

RNA thermometers as temperature-dependent tools for enhanced recombinant protein production in precision fermentation.

Peternell Christina C, Noll Philipp P, Henkel Marius M

Precision fermentation is a key technology for the future sustainable production of food proteins, bulk ingredients, and high-value recombinant products. However, process efficiency is often limited by the coupling of biomass formation and recombinant protein synthesis, leading to substantial carbon losses into non-recyclable biomass. Particularly for cost-sensitive bulk products such as food proteins, economically viable production requires highly efficient and dynamically controllable bioprocesses. RNA thermometers (RNATs) offer a promising inducer-free strategy for temperature-dependent control of recombinant protein production and dynamic bioprocess regulation, with the potential to improve carbon efficiency and product yields. In this study, a fluorescent reporter protein (EmGFP) under the control of a fourU (4U) RNA thermometer was evaluated in E. coli BL21 across a temperature range of 25-40 °C. Temperature-dependent regulation enabled maximal recombinant protein production at 35 °C, resulting in a 2.6-fold higher specific productivity compared to the derepressed control. The strongest RNAT-mediated regulatory effect was observed at 35.5 °C, highlighting the relevance of precise temperature control for recombinant protein production. Evaluation of altered carbon partitioning revealed a substantially increased carbon allocation toward product formation, while carbon partitioning into biomass and CO2 remained largely unchanged. Furthermore, the product-per-acetate yield increased more than threefold at induction temperature, indicating controllable carbon partitioning and reveals potential for decoupling approaches of biomass formation from recombinant protein production. This study demonstrates the successful implementation of an RNAT-controlled recombinant expression system enabling temperature-dependent regulation of protein production in E. coli. Quantitative analysis revealed controllable carbon partitioning toward recombinant protein synthesis and defined target temperatures for future process induction and switching. In contrast to conventional inducer-based systems, RNAT-mediated regulation enables dynamic control without chemical additives, supporting more resource-efficient bioprocess operation. However, fully exploiting RNAT-based process control will require advanced model-based strategies integrating temperature and feeding regimes, particularly for cost-sensitive precision fermentation processes such as food protein production. Overall, RNATs represent promising molecular control elements for future high-efficiency precision fermentation processes.

PMID 42875774
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PubMedPakistan journal of biological sciences : PJBS2026-10-15

Molecular Engineering of the Thioredoxin (trxA) Gene in Chryseobacterium proteolyticum Enhanced its Keratinase Bioconversion of Chicken Feathers.

Mpaka Lindelwa L, Nnolim Nonso E NE, Nwodo Uchechukwu U UU

<b>Background and Objective:</b> Keratinases are gaining traction in green technology and the bio-economy due to their ability to convert keratinous biomass into valuable products, such as animal feed. However, improving their output remains challenging. This study investigated genetic engineering approaches to increase keratinase production. <b>Materials and Methods:</b> The genome of the keratinolytic bacterium, <i>C. proteolyticum,</i> was sequenced using the Ion GeneStudio<sup>™</sup> S5 Prime System, covering 2,484,843 reads, and sequence reads generated were assembled using SPAdes 3.13.0. The quality of the reads was assessed with QUAST V4.1, and the obtained sequences were annotated with Prokka 1.14.6, which revealed that trxA is associated with keratinolytic activity. The nucleotide sequence obtained was uploaded to the NCBI database and was assigned the accession number JBJLWK000000000. The <i>trxA</i> gene was amplified with primers from NCBI Primer-BLAST, cloned into a p-GEM<sup>®</sup>-T Easy vector, and transformed into <i>E. coli</i> JM109, and expressed using IPTG and SDS-PAGE analysis. The effects of pH and temperature on enzyme production were studied, and the recombinant strain's thermostability and tolerance to commercial laundry detergents were assessed. <b>Results:</b> The gene was successfully cloned and expressed, with SDS-PAGE showing a clear band at 11 kDa, matching trxA's molecular weight. The pGEM-trxA construct demonstrated high keratinase activity across various pH and temperature conditions. Additionally, the recombinant strain showed excellent thermostability and detergent tolerance. <b>Conclusion:</b> These findings highlight the potential of recombinant technology to boost keratinase yields and support the sustainable recycling of keratinous waste.

PMID 42876176
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PubMedThe International journal of artificial organs2026-10-15

In vitro replication of relationship between α1-microglobulin reduction rate and albumin leakage in post-dilution hemodiafiltration.

Li Maozhen M, Inoue Hiroyuki H, Yamaguchi Satoru S, Sunohara Takashi T et al.

Efficient removal of middle-to-large molecules, such as α1-microglobulin (α1-MG, 33 kDa), is essential for mitigating long-term complications in patients undergoing hemodiafiltration (HDF). However, objective evaluation of diafilter performance requires standardized laboratory systems that can reproduce clinical transport characteristics while monitoring albumin leakage. This study established an in vitro experimental system utilizing recombinant α1-MG to evaluate post-dilution on-line HDF. Two configurations were compared: Circuit#1, featuring an auxiliary pump at the blood outlet, and Circuit#2, where the pump was removed to optimize flow regulation. Results demonstrated that Circuit#1 significantly deviated from clinical benchmarks due to internal pressure accumulation. Conversely, Circuit#2 successfully mirrored clinical trends, showing a strong positive correlation between α1-MG removal and albumin leakage. Observed clearances in Circuit#2 were slightly higher than clinical averages, likely due to the smaller molecular weight of the recombinant solute (31 vs. 33 kDa), reduced circulation volume, and the absence of α1 in vitro-MG-IgA dimer binding complexes. This validated model provides a robust and reliable platform for the standardized assessment and development of next-generation blood purification devices.

PMID 42876027
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PubMedFrontiers in immunology2026-10-15

Hemin suppresses interferon responses in periodontal cell models through JAK2-STAT1 inhibition.

Huang Xiaoyu X, Gruber Reinhard R, Panahipour Layla L

Hemin, an oxidized heme species released during erythrocyte breakdown, is detectable in gingival crevicular fluid during periodontal inflammation, but its effects on local immune signaling remain unclear. We investigated whether hemin modifies cytokine-induced interferon responses in HSC-2 oral squamous cell carcinoma cells and primary human gingival fibroblasts. Cells were stimulated with interleukin-1β and tumor necrosis factor-α, or with interferon-γ, in the presence or absence of hemin. Transcriptomic changes were assessed by RNA sequencing and pathway analysis, and selected transcripts and proteins were validated by reverse-transcription quantitative PCR, enzyme-linked immunosorbent assay, immunoblotting, and immunofluorescence. Ligand-kinase interactions were examined by molecular docking and molecular dynamics simulations, and recombinant Janus kinase 2 activity was measured in a cell-free assay. Hemin preferentially suppressed an interferon-associated gene network, including CXCL10, CXCL11, MX1, OAS1, IFIT1, IFIT3, and ISG15, while nuclear factor κB-associated responses were comparatively preserved. Hemin also reduced signal transducer and activator of transcription 1 Tyr701 phosphorylation and nuclear accumulation induced by either the cytokine combination or interferon-γ. Computational analyses predicted stable hemin interactions within conserved ATP-binding pockets of Janus kinases, and the cell-free assay demonstrated inhibition of recombinant Janus kinase 2. Together, these findings show that hemin attenuates interferon-associated transcription in periodontal cell models, consistent with inhibition of the Janus kinase 2-signal transducer and activator of transcription 1 axis. This mechanism may enable blood-derived hemin to modify local mucosal immune signaling, although its relevance to periodontal tissues and antiviral defense requires confirmation in organotypic, infection, and in vivo models.

PMID 42876722
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PubMedFrontiers in cellular and infection microbiology2026-10-15

Immunogenicity and protective efficacy of recombinant BCG expressing a multi-epitope vaccine against mycobacterium tuberculosis.

Zhang Xuan-Ji XJ, Luo Jia-Rui JR, Tian Ting-Ting TT, Shi Juan J et al.

Mycobacterium tuberculosis (Mtb) infects approximately one-quarter of the global population, of whom 5%-10% develop active tuberculosis (TB). Although Bacillus Calmette-Guérin (BCG) remains the cornerstone vaccine against severe infant TB, its efficacy in adults is limited, underscoring the need for novel TB vaccines. This study aimed to design a multi-epitope vaccine, tMEV, and validate its protective potential through bioinformatic prediction and in vivo experiments. tMEV was constructed from dominant T- and B-cell epitopes derived from Mtb ESAT-6, PE35, PPE38, and PE4 proteins, fused with an adjuvant. Its vaccine candidacy was assessed via physicochemical and solubility profiling, secondary and tertiary structure modeling, TLR-4 molecular docking, molecular dynamics simulation, and immune simulation. The tMEV coding sequence was cloned into pMV361 and transformed into BCG to generate recombinant BCG (rBCG-tMEV). Immunogenicity, antigenicity, and protective efficacy were evaluated in mouse immunization and Mtb challenge models. tMEV exhibited favorable vaccine-like properties in silico. In mice, both tMEV and rBCG-tMEV induced Mtb-specific immune responses. Compared with PBS, tMEV significantly enhanced cellular and humoral immunity with a Th2-biased profile. Relative to conventional BCG, rBCG-tMEV elicited a superior mixed Th1-Th2 response and higher antigen-specific immunity, accompanied by increased secretion of IFN-γ, IL-2, TNF-α, granzyme B, and perforin. Moreover, rBCG-tMEV markedly reduced bacterial loads in the lungs and spleens of Mtb-infected mice, conferring partial protection. These findings demonstrate that tMEV and rBCG-tMEV possess robust immunogenicity and protective potential against Mtb, representing promising novel TB vaccine candidates and providing a rationale for future vaccine development and optimization.

PMID 42876677
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PubMedBiotechnology journal2026-10-15

Efficient and High-Resolution Separation of Partial, Empty, and Full AAV Capsids by Optimized Iodixanol Density Gradient Ultracentrifugation.

Fang Shan S, Wu Jun J, Shen Yanfang Y, Qi Dandan D et al.

Recombinant adeno-associated virus (rAAV) vectors are essential for gene therapy, but their production generates empty and partial capsids as product-related impurities that can compromise efficacy and safety. While empty capsids have been partially characterized, the isolation and study of partial capsids remain hindered by a lack of robust separation methods. Here, we present an optimized iodixanol density gradient ultracentrifugation strategy enabling high-resolution separation and enrichment of empty, partial, and full AAV capsids. Key innovations include expanding the 40% iodixanol layer to create a broader intermediate-density zone and implementing controlled bottom-puncture fractionation. Applied to a rAAV2 preparation, this method enriched partial capsids from 18.9% in the starting material to approximately 94.9% in the target fraction (determined by AUC integration under the equal response assumption). For a rAAV2 variant with a low baseline of partial capsids (1.3%), over 20-fold enrichment was achieved, reaching 30.1% purity as determined by AUC integration under the equal response assumption. This approach provides partial-capsid-enriched fractions, enabling detailed characterization of partial capsids, supporting critical quality attribute assessment, and facilitating the development of safer, more effective rAAV-based therapeutics.

PMID 42875965
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