Wuhan HealthCare Biotechnology

Wuhan HealthCare Biotechnology Co., Ltd. is a biotechnology company based in Wuhan, China, specializing in molecular diagnostics for medical research and clinical applications. Founded in 2013, the company operates as a National High-Tech Enterprise, focusing on the development, production, and marketing of innovative diagnostic products.

Core Products and Technologies

1. Ultra-Rapid Hybridization Time FISH probes

We utilize the DNA Nucleotides Sequence Deduplication Technology and feature a hybridization time as short as 1 hour (for hematological malignancies) and 2 hours (for solid tumor malignancies) than conventional probes requesting 16 to 24 hours—slashing hybridization time and cutting down the testing whole process turnaround time (TAT) up 68% (Tissue sample) and 88% (Blood cell sample); While delivering an Affordable, Thermostable, High specificity, High sensitivity, Low background noise, 8 months guaranteed Anti-quenching effects finished product, that ultimately increases laboratory Productivity and Profitability.

2. Comprehensive Automation Integration

We address the industry’s need for standardization and reproducibility through fully automated system platforms‌ consisting of:

TL101 System for high-throughput FISH slides automated pretreatment totally replacing manual pretreatment.
KL-200P System for FISH slides automated processing from pretreatment to staining.
FF-S2400 System for FISH slides automated scanning, analysis and imaging control.

3. Customization OEM & Multiplex Service Capabilities‌

Tailored probes design: OEM services for custom FISH kits and automation under your brand.

4. Online and Field Support Service Capabilities‌

We provide expert-support, online and on-site marketing support through our specialists to take part in webinars, master classes, forums, conferences, exhibitions, training, seminars, laboratory FISH practice training etc...

Browse Wuhan HealthCare Biotechnology Products

10q

SKU: FP-220|Size: 100 µL - 10 Tests

11p15.5

SKU: FP-142|Size: 100 µL - 10 Tests

11q13.3/CEP11

SKU: FP-427|Size: 100 µL - 10 Tests

11q22.2

SKU: FP-277|Size: 100 µL - 10 Tests

11q23.3/CEP11; 11q24.3/CEP11

SKU: FP-164|Size: 200 µL - 10 Tests

11q23/DLEU1

SKU: FP-194|Size: 100 µL - 10 Tests

12p11/CEP12

SKU: FP-117|Size: 100 µL - 10 Tests

16q13

SKU: FP-134|Size: 100 µL - 10 Tests

16q22 ;16q23

SKU: FP-273|Size: 100 µL - 10 Tests

17q12

SKU: FP-518|Size: 100 µL - 10 Tests

19p13.11 green probe

SKU: FP-472|Size: 100 µL - 10 Tests

19p13.3

SKU: FP-275|Size: 100 µL - 10 Tests

19q13/19p13

SKU: FP-274|Size: 100 µL - 10 Tests

1p32/1q21

SKU: FP-197|Size: 100 µL - 10 Tests

1p32/1q21 (labeling opposite of FP-197)

SKU: FP-359|Size: 100 µL - 10 Tests

1p36/1q25

SKU: FP-278|Size: 100 µL - 10 Tests

1p36/1q25; 19q13/19p13

SKU: FP-045|Size: 200 µL - 10 Tests

1q21

SKU: FP-022|Size: 100 µL - 10 Tests

1q21/1p36

SKU: FP-206|Size: 100 µL - 10 Tests

20p11/20q12/20q13 tricolor

SKU: FP-370|Size: 100 µL - 10 Tests

20q11

SKU: FP-283|Size: 100 µL - 10 Tests

20q12/20q13.1

SKU: FP-020|Size: 100 µL - 10 Tests

21q22.2/10p15.3

SKU: FP-334|Size: 100 µL - 10 Tests

SKU: FP-282|Size: 100 µL - 10 Tests

2q37.3/16p13.3

SKU: FP-371|Size: 100 µL - 10 Tests

3p22.1/3q2910q22.3/CEP10

SKU: FP-460|Size: 200 µL - 10 Tests

SKU: FP-219|Size: 100 µL - 10 Tests

4p16.3/CEP4

SKU: FP-429|Size: 100 µL - 10 Tests

4q12/CEP10

SKU: FP-030|Size: 100 µL - 10 Tests

4q12/CEP4

SKU: FP-505|Size: 100 µL - 10 Tests

5p15/9q22/15q22 tricolor

SKU: FP-401|Size: 100 µL - 10 Tests

5q31/5q33/5p tricolor

SKU: FP-373|Size: 100 µL - 10 Tests

5q33.3

SKU: FP-281|Size: 100 µL - 10 Tests

6p21.1/CEP6

SKU: FP-492|Size: 100 µL - 10 Tests

6q21

SKU: FP-374|Size: 100 µL - 10 Tests

6q21/14q24

SKU: FP-102|Size: 100 µL - 10 Tests

6q21/15q22

SKU: FP-195|Size: 100 µL - 10 Tests

6q23/6p25; 9p21/11q13; 8q24/10q23

SKU: FP-325|Size: 300 µL - 10 Tests

6q27 (MLLT4)

SKU: FP-291|Size: 100 µL - 10 Tests

7p11/CEP7

SKU: FP-344|Size: 100 µL - 10 Tests

7p12 (IKZF1)

SKU: FP-392|Size: 100 µL - 10 Tests

7q22/7q31.2

SKU: FP-019|Size: 100 µL - 10 Tests

7q22/7q36

SKU: FP-445|Size: 100 µL - 10 Tests

7q22/7q36/CEP7 tricolor

SKU: FP-386|Size: 100 µL - 10 Tests

7q32 (IRF5)

SKU: FP-390|Size: 100 µL - 10 Tests

8q24 (LINC00861) /MYC

SKU: FP-517|Size: 100 µL - 10 Tests

9p21/CEP9/CEP17 tricolor

SKU: FP-322|Size: 100 µL - 10 Tests

SKU: FP-218|Size: 100 µL - 10 Tests

ABL1

SKU: FP-188|Size: 100 µL - 10 Tests

ABL2

SKU: FP-189|Size: 100 µL - 10 Tests

ACTB/GLI1

SKU: FP-489|Size: 100 µL - 10 Tests

ALK

SKU: FP-002|Size: 100 µL - 10 Tests

ALK/EML4 tricolor

SKU: FP-426|Size: 100 µL - 10 Tests

ALK/LAF4

SKU: FP-250|Size: 100 µL - 10 Tests

AML1

SKU: FP-109|Size: 100 µL - 10 Tests

ANGPT4/SIRPB2

SKU: FP-515|Size: 100 µL - 10 Tests

API2/MALT1

SKU: FP-163|Size: 100 µL - 10 Tests

AR/CEPX

SKU: FP-114|Size: 100 µL - 10 Tests

ASPSCR1/TFE3

SKU: FP-152|Size: 100 µL - 10 Tests

ASS1/CEP9

SKU: FP-168|Size: 100 µL - 10 Tests

ATF1

SKU: FP-347|Size: 100 µL - 10 Tests

ATM/CEP11

SKU: FP-245-3|Size: 100 µL - 10 Tests

AURKA

SKU: FP-165|Size: 100 µL - 10 Tests

AURKB

SKU: FP-169|Size: 100 µL - 10 Tests

BAP1

SKU: FP-058|Size: 100 µL - 10 Tests

BCL10/IGH

SKU: FP-393|Size: 100 µL - 10 Tests

BCL11A

SKU: FP-407|Size: 100 µL - 10 Tests

BCL11B

SKU: FP-425|Size: 100 µL - 10 Tests

BCL2

SKU: FP-243-3|Size: 100 µL - 10 Tests

BCL2/CEP18

SKU: FP-313|Size: 100 µL - 10 Tests

BCL2/IGH

SKU: FP-242-4|Size: 100 µL - 10 Tests

BCL3

SKU: FP-379|Size: 100 µL - 10 Tests

BCL3/IGH

SKU: FP-363|Size: 100 µL - 10 Tests

BCL6

SKU: FP-243-2|Size: 100 µL - 10 Tests

BCL6/IGH

SKU: FP-240|Size: 100 µL - 10 Tests

BCOR

SKU: FP-128|Size: 100 µL - 10 Tests

BCOR/CCNB3

SKU: FP-156|Size: 100 µL - 10 Tests

BCR/ABL

SKU: FP-003|Size: 100 µL - 10 Tests

BCR/ABL/ASS tricolor

SKU: FP-320|Size: 100 µL - 10 Tests

BCR/JAK2

SKU: FP-436|Size: 100 µL - 10 Tests

BEND2

SKU: FP-280|Size: 100 µL - 10 Tests

BRAF

SKU: FP-016|Size: 100 µL - 10 Tests

BRAF/KIAA1549

SKU: FP-290|Size: 100 µL - 10 Tests

BRD4/NUT

SKU: FP-204|Size: 100 µL - 10 Tests

C-MET/CEP7

SKU: FP-046|Size: 100 µL - 10 Tests

C-MYC green probe

SKU: FP-494|Size: 100 µL - 10 Tests

C-MYC/CEP8

SKU: FP-015|Size: 100 µL - 10 Tests

C-MYC/IGH

SKU: FP-234-3|Size: 100 µL - 10 Tests

C11ORF95 (ZFTA)

SKU: FP-279|Size: 100 µL - 10 Tests

C11orf95/MKL2

SKU: FP-133|Size: 100 µL - 10 Tests

C11orf95/RELA

SKU: FP-017|Size: 100 µL - 10 Tests

C19MC/19p13

SKU: FP-124|Size: 100 µL - 10 Tests

CAMTA1

SKU: FP-145|Size: 100 µL - 10 Tests

CBFA2T3/GLIS2

SKU: FP-398|Size: 100 µL - 10 Tests

CBFB

SKU: FP-027|Size: 100 µL - 10 Tests

CBFB/MYH11

SKU: FP-028|Size: 100 µL - 10 Tests

CCND1

SKU: FP-042|Size: 100 µL - 10 Tests

CCND1/CEP11

SKU: FP-041|Size: 100 µL - 10 Tests

CCND1/IGH

SKU: FP-233-1|Size: 100 µL - 10 Tests

CCND1/IGK

SKU: FP-457|Size: 100 µL - 10 Tests

KL200P-Intro Video

FF-S2400

Resources & Documents

WHBTC Product Catalogue

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Base

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Brochure - Probes ; TL101 ; KL-200P

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Recent Breakthroughs

Design, synthesis, and antidiabetic activity of new furan-clubbed 1,2,3-triazole derivatives as <i>α</i>-glucosidase inhibitors.

Devi P, Maity S, Singh A, Mehan S, Singh G, Asati V.

Future Med Chem

PMID:41994872

Free PMC article

Aim The study aims to design, synthesize, and evaluate novel furan-clubbed 1,2,3-triazole derivatives as potential α-glucosidase inhibitors for the management of diabetes mellitus. Materials and methods Ten furan-clubbed-1,2,3-triazole derivatives PD(1-10) were synthesized and characterized through sophisticated instrumentation techniques, including FT-IR, 1 H NMR, 13 C NMR, and LC-MS. The compounds were assessed in vitro for their ability to inhibit the α-glucosidase enzyme. The in vivo antidiabetic effect of the best molecules was evaluated using STZ-nicotinamide induced diabetic mouse model. The observed results were further supported by molecular docking against α-glucosidase (PDB ID: 3L4U) and histopathological examinations. Results The results of in vitro studies showed that the test compound PD-10 exhibited the strongest α-glucosidase inhibition (IC 5 0 = 13.82 μM), outperforming acarbose (IC 5 0 = 32.03 μM), followed by PD-1 and PD-6 . Further, the in vivo antidiabetic evaluation of the best compounds adjudged compound PD-10 as the best molecule among the series. Docking analyses indicated a significant binding affinity of PD-10 (-4.34 kcal/mol). Conclusions The research highlights PD-10 as a promising α-glucosidase inhibitor with strong in vitro and in vivo antidiabetic effects, supported by favorable molecular docking interactions, and emphasizes its potential for development as an antidiabetic lead for further studies and evaluations.

Mechanistic perspectives on antimalarial agents: from FDA-approved drugs to next-generation candidates.

Monika, Sharma B, Awasthi SK.

RSC Adv

PMID:42006802

Free PMC article

Malaria is a major global health challenge, demanding continued innovation in drug discovery and development. This review gives a comprehensive overview of FDA-approved antimalarial drugs and emerging clinical candidates, focusing their chemical structures, mechanisms of action, and molecular targets such as PfATP4, DHFR, DHODH, and PfCRT. The discussion showcases structure-activity relationships, mechanisms underlying drug resistance, and recent advances in structure-guided design of next-generation antimalarials. The review also summarizes the year of approval, mechanistic class, and synthetic origin of key therapeutic agents. Moreover, novel molecules currently in preclinical and clinical trials are discussed in the context of their mode of action, efficacy, and potential for overcoming resistance. Collectively, this article bridges medicinal chemistry insights with biological mechanisms, outlining future directions in the rational design of potent, resistance-resilient antimalarial drugs.

Total chemical synthesis of pentameric cholera toxin subunit B.

Spaltenstein P, Scherer SR, Jones TE, Giesler RJ, Kay MS.

Chem Commun (Camb)

PMID:41891529

Free PMC article

Vibrio cholerae annually infects millions worldwide, causing intense and life-threatening diarrheal disease. The pentameric cholera toxin subunit B (CtxB) binds to the ganglioside GM1 on epithelial cells, initiating endocytosis and downstream toxicity. We present the total chemical protein synthesis of L-CtxB and mirror-image D-CtxB using a three-segment N-to-C native chemical ligation approach. Oxidative folding produced the desired 62 kDa pentameric proteins, with L-CtxB capable of binding native GM1 ligand. Synthetic D-CtxB is now ready to serve as a target in mirror-image phage display, representing a significant milestone for the discovery of toxin-neutralizing D-peptides to treat and prevent cholera.

Can amoxicillin be detected in the aquatic environment? A critical assessment.

Hernández F, Botero-Coy AM, Bijlsma L, Fabregat-Safont D.

Environ Int

PMID:42001666

Free PMC article

Amoxicillin is a broad-spectrum β-lactam antibiotic widely used in both human and veterinary medicine. Following administration, approximately 60-80% of the dose is excreted, largely unmetabolized, via urine within a few hours. Consequently, environmental contamination with amoxicillin, especially in aquatic systems, is a significant concern. Due to its potential ecological risks and the current scarcity of data required for a full assessment, it was included in two consecutive European Union Watch Lists (2018, 2020) of substances for comprehensive monitoring to inform water policy. However, data on amoxicillin levels in aquatic environments are contradictory, ranging from high concentrations in some studies to non-detection in others. The presence of intact amoxicillin in aquatic environments is inherently transient, and the risk of substantial analytical errors in its detection, identification, and quantification is considerable unless stringent methodological precautions are applied. Driven by the need for reliable environmental data, inconsistencies in the existing literature and our own extensive analytical experience, we comprehensively investigated amoxicillin degradation in surface water, influent and effluent wastewater under various conditions. Experiments were conducted under both dark and sunlight conditions using water samples spiked with amoxicillin at 5 μg/L and 50 μg/L. The parent compound was quantified by liquid chromatography-tandem mass spectrometry, whereas transformation products were identified by high-resolution mass spectrometry. By critically assessing the factors that influence the analysis and environmental occurrence of amoxicillin, this study resolves discrepancies in prior reports and clarifies the realistic prospects for its detection. We demonstrate that the parent antibiotic should be rarely found in water samples due to its rapid degradation. Therefore, future monitoring efforts should be focused on its primary degradation product, amoxicillin penicilloic acid, as more reliable indicator of contamination in aquatic environments.

Characterising the urinary metabolome in HIV/TB coinfection and the impact of antiretroviral treatment.

Allen B, Wood R, Luies L.

BMC Infect Dis

PMID:41992151

Free PMC article

Background HIV/TB coinfection poses significant challenges due to complex interactions between both pathogens and the metabolic disruptions they induce. Although antiretroviral treatment (ART) has transformed disease management, its impact on metabolism is not fully understood. Metabolomics offers an in-depth approach to explore the metabolic changes in this coinfected population, providing information into disease mechanisms and the effects of ART. Methods This exploratory study used untargeted urine gas chromatography mass spectrometry metabolomics to profile metabolic alterations in treatment-naïve HIV/TB coinfected patients and those on ART. Healthy controls were included for comparison. Metabolite changes were analysed using univariate statistical methods, including Kruskal-Wallis tests and pairwise comparisons, to identify key metabolites associated with coinfection and ART. Results Findings revealed significant disruptions in several metabolic pathways. Mitochondrial dysfunction was evident, contributing to altered lipid metabolism, impaired energy production, and increased cardiovascular risk. Disruptions in glucose metabolism, including compromised insulin secretion, were observed, alongside evidence of gut dysbiosis linked to inflammation and microbial imbalance. These metabolic disturbances were also associated with increased oxidative stress, reflected in changes to protein metabolism and the development of cachexia. Although ART partially alleviated some metabolic alterations, disruptions remained evident in treated patients. Conclusion This study provides a comprehensive view of the metabolic disturbances in HIV/TB coinfection and the impact of ART. Our findings suggest that persistent mitochondrial dysfunction, altered lipid metabolism, and gut dysbiosis contribute to ongoing metabolic imbalances, underscoring the need for targeted therapeutic strategies to address these challenges.