Absea Biotechnology

Absea Biotechnology Ltd. is a global biotechnology company specializing in the development, engineering, and characterization of high-quality protein and antibody reagents. Established in 2001, Absea has rapidly expanded its operations, employing over 250 professionals across multiple international locations.

Global Presence:

Absea operates through several strategic centers worldwide:

Innovation Center: Berlin, Germany
Manufacturing and Business Centers: Beijing, Suzhou, Shanghai, and Shenzhen, China
Commercialization and Distribution Center: South San Francisco, California, USA

This extensive network enables Absea to cater effectively to the needs of protein scientists and industry partners involved in AI-driven protein design, diagnostics, and drug development.

Product and Service Portfolio:

Absea offers a comprehensive range of products and services, including:

Recombinant Proteins: With a library encompassing over 12,000 soluble proteins covering 60% of the human proteome, Absea continues to broaden its synthetic proteome portfolio.
Monoclonal Antibodies: Validated for diverse applications, these antibodies are readily available for widespread supply to the general market.
Custom Services:
Antibody Development: Comprehensive services from antigen preparation to antibody identification, including DNA synthesis, protein expression, peptide design, and various validation approaches.
Recombinant Protein Production: End-to-end solutions covering gene synthesis, vector construction, protein expression, and purification across multiple systems such as mammalian cells and E. coli.
Isotope-Labeled Proteins: Specialized production of proteins labeled with stable isotopes for advanced research applications.

Technological Capabilities:

Absea's cutting-edge platform facilitates unparalleled throughput, enabling up to 1,000 new development projects per month. Through dynamic collaborations with leaders in the life sciences, particularly in proteomics, Absea has built a robust library of recombinant standards to advance cross-linking mass spectrometry-based interactomics.

Browse Absea Biotechnology Products

4-1BBL Antibody

SKU: KC-30785-01|Size: 50 μL

53BP1 Antibody

SKU: KC-2548-01|Size: 50 μL

A1BG Antibody

SKU: KC-35387-01|Size: 50 μL

A2M Antibody

SKU: K11079M11H11C-01|Size: 50 ug

AAAS Antibody

SKU: KC-3215-01|Size: 50 μL

AACT Antibody

SKU: KC-1601-01|Size: 50 μL

AARSD1 Antibody

SKU: KC-2954-01|Size: 50 μL

ABCB5 Antibody

SKU: KC-6326-01|Size: 50 μL

ABCB5 Antibody (Biotin)

SKU: KB-23496-01|Size: 50 μL

ABCC3 Antibody

SKU: KC-2367-01|Size: 50 μL

ABI2 Antibody

SKU: KC-48309-01|Size: 50 μL

ABL1 Antibody

SKU: KC-13956-01|Size: 50 μL

ABRAXAS2 Antibody

SKU: K92017M03C10C-01|Size: 50 ug

ACAA1 Antibody

SKU: KC-30199-01|Size: 50 μL

ACAD8 Antibody

SKU: KC-42303-01|Size: 50 μL

ACAD9 Antibody

SKU: KC-2943-01|Size: 50 μL

ACAP1 Antibody

SKU: KC-3980-01|Size: 50 μL

ACE2 Antibody

SKU: KC-1951-01|Size: 50 μL

ACE2 Antibody (Biotin)

SKU: KB-2101-01|Size: 50 μL

ACLY Antibody

SKU: KC-3910-01|Size: 50 μL

ACLY Antibody (Biotin)

SKU: KB-30145-01|Size: 50 μL

ACOD1 Antibody

SKU: KC-3971-01|Size: 50 μL

ACP1 Antibody

SKU: KC-8135-01|Size: 50 μL

ACP1 Antibody (Biotin)

SKU: KB-8135-01|Size: 50 μL

ACP6 Antibody

SKU: KC-3871-01|Size: 50 μL

ACSL3 Antibody

SKU: KC-3186-01|Size: 50 μL

ACSM5 Antibody

SKU: KC-3104-01|Size: 50 μL

ACTA1 Antibody

SKU: KC-6235-01|Size: 50 μL

ACTB Antibody

SKU: K06211M11A03C-01|Size: 50 ug

ACTG2 Antibody

SKU: KC-2185-01|Size: 50 μL

ACTN1 Antibody

SKU: KC-4230-01|Size: 50 μL

ACY1 Antibody

SKU: KC-2946-01|Size: 50 μL

ACY1 Antibody (Biotin)

SKU: KB-21307-01|Size: 50 μL

ACYP2 Antibody

SKU: KC-45713-01|Size: 50 μL

ADAM12 Antibody

SKU: KC-28237-01|Size: 50 μL

ADAM22 Antibody

SKU: OC-632-01|Size: 50 μL

ADAM23 Antibody

SKU: KC-3979-01|Size: 50 μL

ADAM9 Antibody

SKU: KC-8411-01|Size: 50 μL

ADAMTS15 Antibody

SKU: KC-21633-01|Size: 50 μL

ADAMTS15 Antibody (Biotin)

SKU: KB-21634-01|Size: 50 μL

ADAMTS4 Antibody

SKU: KC-3796-01|Size: 50 μL

ADAMTS4 Antibody (Biotin)

SKU: KB-27451-01|Size: 50 μL

ADAMTS8 Antibody

SKU: KC-3316-01|Size: 50 μL

ADAMTS8 Antibody (Biotin)

SKU: KB-7497-01|Size: 50 μL

ADAR1 Antibody

SKU: OC-027-01|Size: 50 μL

ADD1 Antibody

SKU: KC-2620-01|Size: 50 μL

ADGRB1 Antibody

SKU: KC-3773-01|Size: 50 μL

ADGRB1 Antibody (Biotin)

SKU: KB-8140-01|Size: 50 μL

ADGRE2 Antibody

SKU: KC-3323-01|Size: 50 μL

ADGRF1 Antibody

SKU: KC-2427-01|Size: 50 μL

ADGRF2P Antibody

SKU: KC-43029-01|Size: 50 μL

ADGRF4 Antibody

SKU: KC-33324-01|Size: 50 μL

ADK Antibody

SKU: KC-3450-01|Size: 50 μL

ADK Antibody (Biotin)

SKU: KB-27375-01|Size: 50 μL

ADSS1 Antibody

SKU: KC-34957-01|Size: 50 μL

AFAP1 Antibody

SKU: KC-44775-01|Size: 50 μL

AFAP1L2 Antibody

SKU: KC-42698-01|Size: 50 μL

AFP Antibody

SKU: K06092M06C05C-01|Size: 50 ug

AGBL1 Antibody

SKU: KC-39937-01|Size: 50 μL

AGFG1 Antibody

SKU: OC-2377-01|Size: 50 μL

AGR3 Antibody

SKU: K1E028M18C10C-01|Size: 50 ug

AGR3 Antibody (Biotin)

SKU: KB-8143-01|Size: 50 μL

AHCTF1 Antibody

SKU: KC-30687-01|Size: 50 μL

AHCY Antibody

SKU: KC-43109-01|Size: 50 μL

AHI1-DT Antibody

SKU: KC-36216-01|Size: 50 μL

AHNAK Antibody

SKU: KC-2360-01|Size: 50 μL

AHSG Antibody

SKU: K56007M03H02C-01|Size: 50 ug

AIF Antibody

SKU: KC-6313-01|Size: 50 μL

AK5 Antibody

SKU: KC-8400-01|Size: 50 μL

AKAP10 Antibody

SKU: KC-31756-01|Size: 50 μL

AKAP12 Antibody

SKU: KC-45668-01|Size: 50 μL

AKAP7 Antibody

SKU: KC-43974-01|Size: 50 μL

AKAP8 Antibody

SKU: KC-2598-01|Size: 50 μL

AKR1B1 Antibody

SKU: K92029C01D04C-01|Size: 50 ug

AKR7L Antibody

SKU: KC-3255-01|Size: 50 μL

AKT1 Antibody

SKU: KC-4368-01|Size: 50 μL

AKT1/AKT2/AKT3 Antibody

SKU: KC-6276-01|Size: 50 μL

AKT3 Antibody

SKU: KC-2766-01|Size: 50 μL

ALB Antibody

SKU: K02001M08H05C-01|Size: 50 ug

ALB Antibody (HRP)

SKU: K02001M08H05H-01|Size: 50 ug

ALCAM Antibody

SKU: KC-8490-01|Size: 50 μL

ALDH1A1 Antibody

SKU: K92024C06C11C-01|Size: 50 ug

ALDH1A3 Antibody

SKU: OC-696-01|Size: 50 μL

ALDH1B1 Antibody

SKU: KC-32252-01|Size: 50 μL

ALDH1L1 Antibody

SKU: KC-8402-01|Size: 50 μL

ALDH2 Antibody

SKU: KC-6146-01|Size: 50 μL

ALDH3A1 Antibody

SKU: K1E028M07C05C-01|Size: 50 ug

ALDH3A2 Antibody

SKU: KC-6112-01|Size: 50 μL

ALDOB Antibody

SKU: KC-3172-01|Size: 50 μL

ALK Antibody

SKU: K40048M08D10C-01|Size: 50 ug

ALPP Antibody

SKU: KC-6299-01|Size: 50 μL

AMACR Antibody

SKU: KC-3085-01|Size: 50 μL

AMBP Antibody

SKU: K16092M14F04C-01|Size: 50 ug

AMDHD2 Antibody

SKU: KC-32470-01|Size: 50 μL

AMF Antibody

SKU: KC-123-01|Size: 50 μL

AMFR Antibody

SKU: KC-29602-01|Size: 50 μL

AMIGO3 Antibody

SKU: OC-873-01|Size: 50 μL

AMN Antibody

SKU: KC-3851-01|Size: 50 μL

AMPK alpha 1 Antibody

SKU: KC-3132-01|Size: 50 μL

AMPK beta 1 Antibody

SKU: KC-6143-01|Size: 50 μL

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.