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Anti-Human IL-12 / IL-23 (Ustekinumab Biosimilar)

Cat # Size Price Quantity
5066011 mg$190
5066025 mg$590
50660320 mg$2000

  Bulk/Custom

Product Details

CloneUstekinumab
ApplicationNeutralization, Intracellular Flow cytometry, animal model study
Host SpeciesMammalian cells
ReactivityHuman
FormatLiquid
Product DescriptionUstekinumab Biosimilar, Human IL-12 / IL-23 Monoclonal Antibody
IsotypeHuman IgG1
Regulatory StatusRUO
ClonalityRecombinant
ImmunogenHuman IL-12 / IL-23
Species specificityHuman
Purity>95% by reducing SDS-PAGE
GradeIn vivo
Min Sample Size1 mg
Storage Conditions4ºC
Maximal Shelf Life12 months
Synonymsp40
Target NameIL-12/IL-23
Research AreasCytokines, Inflammation
See All FormatsClone Ustekinumab

Background Information

Ustekinumab is a fully human monoclonal antibody that belongs to the immunoglobulin G1 kappa (IgG1κ) subclass, designed to target the p40 subunit shared by two interleukins, interleukin‑12 (IL‑12) and interleukin‑23 (IL‑23). Structurally, Ustekinumab is a glycoprotein with a molecular weight of approximately 148 kilodaltons (kDa) and is composed of two identical heavy chains and two identical light chains connected by disulfide bonds, forming the characteristic Y‑shaped quaternary structure typical of IgG antibodies. Each heavy chain contains one variable (VH) and three constant (CH1–CH3) domains, while each light chain contains one variable (VL) and one constant (CL) domain. It is produced in mammalian expression systems, such as Chinese Hamster Ovary (CHO) cells, allowing proper folding, disulfide linkage formation, and glycosylation necessary for structural and functional stability.

The antigen‑binding regions of Ustekinumab are located within the complementarity‑determining regions (CDRs) of the VH and VL domains, which confer high‑affinity and specific binding to the p40 subunit. This epitope is the structural component common to both IL‑12 and IL‑23, which interact with their respective receptors to activate downstream signaling pathways. By binding to p40, Ustekinumab prevents IL‑12 from associating with the IL‑12 receptor β1/β2 complex and IL‑23 from associating with the IL‑23 receptor complex. This blockade inhibits receptor dimerization and subsequent activation of Janus kinase (JAK)–signal transducer and activator of transcription (STAT) signaling cascades, particularly those involving STAT4 (for IL‑12) and STAT3 (for IL‑23). In cell‑based assays, this interference results in reduced transcription of inflammatory cytokine genes and modulation of T‑helper (Th1 and Th17) differentiation pathways.

The Fc (fragment crystallizable) region of Ustekinumab, derived from the IgG1 isotype, contributes to molecular stability and long‑term persistence via engagement with the neonatal Fc receptor (FcRn) for recycling. While capable of limited Fc‑mediated effector interactions, Ustekinumab primarily functions through targeted ligand neutralization. Overall, it exemplifies precise antibody engineering that integrates structural stability with selective cytokine pathway inhibition, serving as a model for studying interleukin signaling and immune modulation mechanisms.

Data Sheets

Anti-Human IL-12 / IL-23 (Ustekinumab Biosimilar) TDS

Related Products

Anti-Human IL-12 / IL-23 (Briakinumab Biosimilar), Clone Briakinumab

Frequently Asked Questions

What are InnoCyto Biosimilar products?
InnoCyto biosimilars are research-grade recombinant antibodies or proteins engineered to closely replicate the sequence, structure, and target-binding activity of approved or well-characterized therapeutic antibodies (e.g., checkpoint inhibitors, anti-cytokine biologics). They are intended for research use to study the mechanism of action, efficacy, and combination potential of these therapeutic classes without the cost or access restrictions of clinical-grade material.
How similar are these biosimilars to the original therapeutic antibody?
Each biosimilar is produced using the published or inferred variable region sequence of the reference therapeutic and is expressed recombinantly to match the parent antibody's target specificity, isotype, and general binding profile. While designed for high functional similarity, InnoCyto biosimilars are for research use only and are not clinically validated equivalents of the approved drug product.
Are these antibodies suitable for in vivo studies?
Yes. InnoCyto biosimilars are manufactured with the same low-endotoxin, azide-free, carrier-free standards used across our in vivo product lines, making them suitable for animal efficacy, combination, and mechanism-of-action studies. Product pages indicate whether a given biosimilar is validated for in vivo use, in vitro use, or both.
What is the difference between a biosimilar and a recombinant "research antibody" targeting the same protein?
A biosimilar is specifically designed to mimic a known, named therapeutic antibody (matching its clinical target epitope and mechanism), whereas a general recombinant research antibody may target the same protein but bind a different epitope or lack the same functional properties. Biosimilars are the right choice when your study is benchmarking against, or modeling the action of, an approved or clinically studied biologic.
What quality and purity standards do biosimilar antibodies meet?
All biosimilars undergo the same rigorous QC pipeline as our other antibody lines: ≥95% purity by SDS-PAGE/SEC-HPLC, low-endotoxin testing via LAL assay, and binding/functional validation against the intended target. Certificates of Analysis (CoA) are provided per lot with full specifications.
Which therapeutic targets and mechanisms are covered in the Biosimilar line?
The line spans major immuno-oncology and immunology targets, including immune checkpoint pathways (e.g., PD-1/PD-L1, CTLA-4), cytokine and cytokine-receptor blockers, and other clinically relevant mechanisms. See each product page for the specific reference therapeutic and mechanism of action represented.

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