Human Tetanus Toxoid IgG ELISA Kit

Name: Human Tetanus Toxoid IgG ELISA Kit
SKU: DEIA378
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Serum, plasma

Species Reactivity

Human

Detection Method

Indirect-ELISA

Intended Use

The ELISA test kit provides a quantitative in vitro assay for human antibodies of the immunoglobulin class IgG against tetanus toxoid in serum or plasma for the clarification of an unclear immune status.

Contents of Kit

No.	Components	Size	Storage Conditions
1	Microplate wells coated with antigens	12 × 8 wells	2-8°C
2	Calibrator 1	5 IU/ml, 1 × 2.0 ml	2-8°C
3	Calibrator 2	2 IU/ml, 1 × 2.0 ml	2-8°C
4	Calibrator 3	1 IU/ml, 1 × 2.0 ml	2-8°C
5	Calibrator 4	0.1 IU/ml, 1 × 2.0 ml	2-8°C
6	Calibrator 5	0.01 IU/ml, 1 × 2.0 ml	2-8°C
7	Positive control	1 × 2.0 ml	2-8°C
8	Negative control	1 × 2.0 ml	2-8°C
9	Enzyme conjugate	1 × 12 ml	2-8°C
10	Sample buffer	1 × 100 ml	2-8°C
11	Wash buffer, 10× concentrate	1 × 100 ml	2-8°C
12	Chromogen/substrate solution	1 × 12 ml	2-8°C
13	Stop solution	1 × 12 ml	2-8°C

Storage

The test kit has to be stored at a temperature between +2°C to +8°C. Do not freeze. Unopened, all test kit components are stable until the indicated expiry date.

Performance Characteristics

Calibration: The Anti-Tetanus Toxoid ELISA (IgG) was calibrated using the first international WHO standard preparation TE-3 (1^st International Standard for Tetanus Immunoglobulin, Human NIBSC Code TE-3).
For every group of tests performed, the extinction values of the calibrators and the international units determined for the positive and negative controls must lie within the limits stated for the relevant test kit lot. A quality control certificate containing these reference values is included. If the values specified for the controls are not achieved, the test results may be inaccurate and the test should be repeated.
The binding activity of the antibodies and the activity of the enzyme used are temperature-dependent. It is therefore recommended using a thermostat in all three incubation steps. The higher the room temperature (+18°C to +25°C) during the incubation steps, the greater will be the extinction values. Corresponding variations apply also to the incubation times. However, the calibrators are subject to the same influences, with the result that such variations will be largely compensated in the calculation of the result.
Antigen: The microtiter wells were coated with inactivated Tetanus toxoid antigen.

Detection Limit

The lower detection limit is defined as the mean value of an analyte-free sample plus three times the standard deviation and is the smallest detectable antibody titer. The lower detection limit of the Anti-Tetanus Toxoid ELISA (IgG) is 0.001 IU/ml.

General Description

The Anti-Tetanus Toxoid ELISA (IgG) is based on inactivated tetanus toxin and is designed for the quantitative determination of human IgG antibodies against tetanus toxoid in serum or plasma. This test is suited for both investigation the immune status and for vaccination control.

Standard Curve

The following plot is an example of a typical calibration curve. Please do not use this curve for the determination of antibody concentrations in patient samples.

Citations

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Bioengineered human tonsil organoids as an immuno-engineering platform for evaluating immune functions

Intan Rosalina Suhito, Donovan Eu Kum Chuen, Hong Sheng Cheng, Nguan Soon Tan, Zhe Zhang Ryan Lew, Kai Sen Tan, Justin Jang Hann Chu, Giselle G.K. Ng, Yvonne C.F. Su, Gavin J.D. Smith i, Chee Wah Tan, and Andy Tay

bioRxiv2025 October 6Read Article

Applications: ELISA
Reactive species: Tetanus Toxoid
"Abstract: Although animal models remain the preclinical gold standard, they are constrained by interspecies differences in adaptive immunity, including antibody class-switching, affinity maturation, and multicellular interactions. To address this gap, we established a more physiologically relevant platform, a bioengineered tonsil organoid (BTO) system that combines autologous tonsil-derived stromal cells with immune cells to generate highly uniform organoids, preserving multicellular complexity and sustained stromal-immune interactions. BTO cultures mounted robust, antigenspecific recall responses to influenza, tetanus, and COVID-19 antigens. Notably, stimulation with ovalbumin and SARS-CoV-1 spike protein expanded antigen-recognizing B cells, indicating capacity for naïve responses. Digital spatial transcriptomics and proteomics analysis confirmed immune-stromal crosstalk underpinning both humoral and cellular responses of BTO after challenge. These data highlight stromal cells as active scaffolds that not only maintain 3D architecture but also facilitate immune activation, memory recall, and recognition of naïve antigens. Together, BTO offers a human-relevant model for mechanistic immunology and for pre-clinical evaluation on immunotherapies and vaccines not achievable with 2D cultures or animal models."
Article snippet: For tetanus toxoid-specific IgG detection, culture supernatants were assayed by human tetanus toxoid IgG ELISA kit (Creative Diagnostics) following the manufacturer’s instructions.

ELISA data of tonsil organoid stimulation with tetanus toxoid (TT) protein, showing an increase in tetanus-specific IgG. (Intan Rosalina Suhito, <i>et al</i>, 2025)

Figure 1. Tonsil organoids mount effective memory recall responses to previously exposed antigens.

Documents

pdf COA

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pdf Datasheet

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QA & Reviews

Customer Reviews

References

The role of proteases in excitation-contraction coupling failure in muscular dystrophy

AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY

Authors: Mazala, Davi A. G.; Grange, Robert W.; Chin, Eva R.

Abstract

Duchenne muscular dystrophy (DMD) is one of the most frequent types of muscular dystrophy. Alterations in intracellular calcium (Ca2+) handling are thought to contribute to the disease severity in DMD, possibly due to the activation of Ca2+-activated proteases. The purpose of this study was twofold: 1) to determine whether prolonged excitation-contraction (E-C) coupling disruption following repeated contractions is greater in animals lacking both dystrophin and utrophin (mdx/Utr(-/-)) compared with mice lacking only dystrophin (mdx); and 2) to assess whether protease inhibition can prevent E-C coupling failure following repeated tetani in these dystrophic mouse models. Excitation-contraction coupling was assessed using Fura-2 ratio, as an index of intracellular free Ca2+ concentration, in response to electrical stimulation of single muscle fibers from the flexor digitorum brevis muscle. Resting Fura-2 ratio was higher in dystrophic compared with control (Con) fibers, but peak Fura-2 ratios during stimulation were similar in dystrophic and Con fibers. One hour after a series of repeated tetani, peak Fura-2 ratios were reduced by 30 +/- 5.6%, 23 +/- 2%, and 36 +/- 3.1% in mdx, mdx/Utr(-/-), and mdx/Utr(-/-), respectively, with the greatest reduction in mdx/Utr(-/-) fibers (P < 0.05). Protease inhibition attenuated this decrease in peak Fura-2 ratio. These data indicate that E-C coupling impairment after repeated contractions is greatest in fibers lacking both dystrophin and utrophin and that prevention of protease activation can mitigate the prolonged E-C coupling impairment. These data further suggest that acute protease inhibition may be useful in reducing muscle weakness in DMD.

LIMITED PROTEOLYSIS OF TETANUS TOXIN - RELATION TO ACTIVITY AND IDENTIFICATION OF CLEAVAGE SITES

EUROPEAN JOURNAL OF BIOCHEMISTRY

Authors: KRIEGLSTEIN, KG; HENSCHEN, AH; WELLER, U; HABERMANN, E

Abstract

Tetanus toxin is synthesized by Clostridium tetani as a 151-kDa peptide chain. The primary gene product is processed post-translationally by removal of the initiating methionine residue, formation of disulfide bridges and limited proteolysis by bacterial or exogenous proteinases. The mature toxins consist of a 52-kDa light chain and a 98-kDa heavy chain, linked together by a disulfide bond. Proteolytic nicking is accompanied by increased pharmacological potency. To identify the structural alterations involved, single-chain toxin has been subjected to limited proteolysis with various enzymes. The new N-termini have been determined by Edman degradation and the C-termini by isolation of short C-terminal peptide fragments and subsequent analysis of the sequence and composition. All two-chain toxins result from proteolytic nicking within the 17-residue segment of residues 445-461. Thus, the protease(s) of the culture broth cleave on the C-terminal side of Glu449 and partially Ala456, giving rise to two heavy chain N-termini. Trypsin and clostripain first attack the C-terminal of Arg454 and later Arg448, whereas endoproteinase Arg-C cleaves the former bond only. Chymotrypsin and endoproteinase Glu-C each split a single peptide bond, i.e. that located after Tyr452 and Glu449, respectively. Papain gives rise to a large number of cleavages within the 17-residue segment, the new C-terminus being Thr445 or Asn446 and the new N-terminus being Asp460 or Leu461. Further papain digestion leads to an additional cleavage within the heavy chain between Ser863 and Lys864. The original N-terminal Pro1 and C-terminal Asp1314, predicted from the nucleotide sequence, are conserved in all proteolytic digests. The pharmacological activity of the various two-chain toxins was 5-11 times that of the single-chain toxin, as estimated from the inhibition of [H-3]noradrenaline release from rat-brain homogenate. The present data on the processing and activation by limited proteolysis prove the existence of several active tetanus isotoxins. These data, together with our previous data on the localization of disulfide bridges and sulfhydryl groups (Krieglstein, K., Henschen, A., Weller, U. & Habermann, E. (1990) Eur. J. Biochem. 188, 39-45), provide the detailed protein chemical characterization of the tetanus isotoxins.