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Mouse Anti-IL33 Recombinant Antibody (2D8) (CBMAB-A4407-LY)

The product is antibody recognizes IL33. The antibody 2D8 immunoassay techniques such as: WB, ELISA.
See all IL33 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
2D8
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
IL33 (NP_254274.1, 171 a.a. ~ 269 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Interleukin 33
Entrez Gene ID
90865
UniProt ID
O95760
Alternative Names
C9orf26; DKFZp586H0523; DVS27; NF-HEV; NFEHEV; RP11-575C20.2
Function
Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells (PubMed:16286016).
Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury (PubMed:17853410, PubMed:18836528).3 Publications
In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets (PubMed:21734074).
This form is rapidely lost upon angiogenic or proinflammatory activation (PubMed:18787100).
Biological Process
Interleukin-33-mediated signaling pathwayISS:ARUK-UCL
Negative regulation of macrophage proliferationISS:ARUK-UCL
Negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:CACAO
Positive regulation of CD80 productionISS:ARUK-UCL
Positive regulation of CD86 productionISS:ARUK-UCL
Positive regulation of cellular defense responseISS:ARUK-UCL
Positive regulation of chemokine productionManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cytokine productionManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of gene expressionISS:ARUK-UCL
Positive regulation of inflammatory responseBy SimilarityISS:BHF-UCL
Positive regulation of interleukin-6 productionISS:ARUK-UCL
Positive regulation of macrophage activationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of neuroinflammatory responseManual Assertion Based On ExperimentTAS:ARUK-UCL
Positive regulation of nitric-oxide synthase biosynthetic processISS:ARUK-UCL
Positive regulation of transcription by RNA polymerase IIBy SimilarityISS:BHF-UCL
Positive regulation of tumor necrosis factor productionISS:ARUK-UCL
Cellular Location
Nucleus; Chromosome; Cytoplasm; Cytoplasmic vesicle, secretory vesicle; Secreted. Associates with heterochromatin and mitotic chromosomes (PubMed:17185418).
The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059).
PTM
The full-length protein can be released from cells and is able to signal via the IL1RL1/ST2 receptor. However, proteolytic processing by CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal peptides that are more active than the unprocessed full length protein. May also be proteolytically processed by calpains (PubMed:19596270).
Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation (PubMed:19559631).
In vitro proteolytic cleavage by CASP1 was reported (PubMed:16286016) but could not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is probably not a direct substrate for that caspase.

Widjaja, A. A., Chothani, S., Viswanathan, S., Goh, J. W. T., Lim, W. W., & Cook, S. A. (2022). IL11 stimulates IL33 expression and proinflammatory fibroblast activation across tissues. International Journal of Molecular Sciences, 23(16), 8900.

Aneas, I., Decker, D. C., Howard, C. L., Sobreira, D. R., Sakabe, N. J., Blaine, K. M., ... & Nóbrega, M. A. (2021). Asthma-associated genetic variants induce IL33 differential expression through an enhancer-blocking regulatory region. Nature Communications, 12(1), 6115.

Ketelaar, M. E., Portelli, M. A., Dijk, F. N., Shrine, N., Faiz, A., Vermeulen, C. J., ... & Nawijn, M. C. (2021). Phenotypic and functional translation of IL33 genetics in asthma. Journal of Allergy and Clinical Immunology, 147(1), 144-157.

Eissmann, M. F., Buchert, M., & Ernst, M. (2020). IL33 and mast cells—the key regulators of immune responses in gastrointestinal cancers?. Frontiers in immunology, 11, 1389.

Shani, O., Vorobyov, T., Monteran, L., Lavie, D., Cohen, N., Raz, Y., ... & Erez, N. (2020). Fibroblast-derived IL33 facilitates breast cancer metastasis by modifying the immune microenvironment and driving type 2 immunity. Cancer research, 80(23), 5317-5329.

Chen, L., Sun, R., Xu, J., Zhai, W., Zhang, D., Yang, M., ... & Lu, B. (2020). Tumor-Derived IL33 promotes tissue-resident CD8+ T cells and is required for checkpoint blockade tumor immunotherapy. Cancer immunology research, 8(11), 1381-1392.

Kudo-Saito, C., Miyamoto, T., Imazeki, H., Shoji, H., Aoki, K., & Boku, N. (2020). IL33 is a key driver of treatment resistance of cancer. Cancer Research, 80(10), 1981-1990.

Brandt, E. B., Bolcas, P. E., Ruff, B. P., & Khurana Hershey, G. K. (2020). IL33 contributes to diesel pollution‐mediated increase in experimental asthma severity. Allergy, 75(9), 2254-2266.

Chan, B. C., Lam, C. W., Tam, L. S., & Wong, C. K. (2019). IL33: roles in allergic inflammation and therapeutic perspectives. Frontiers in immunology, 10, 364.

Tonacci, A., Quattrocchi, P., & Gangemi, S. (2019). IL33/ST2 axis in diabetic kidney disease: a literature review. Medicina, 55(2), 50.

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For research use only. Not intended for any clinical use.

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