Canine Recombinant IL33 protein (V2LY-0526-LY1285)

Name: Canine Recombinant IL33 protein
SKU: V2LY-0526-LY1285
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

E. coli

Protein Species

Canine

Protein Construction

This product is Canine Recombinant IL33 protein consist of Amino Acid: 110-263 and predicts a molecular mass of 17.8 kDa.

Molecule Mass

17.8 kDa

Sequence

Amino Acid: 110-263

Species

Canine

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

Purity

≥90% as determined by SDS-PAGE.

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile PBS

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

Interleukin 33

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Alternative Versions

Cynomolgus Recombinant IL33 protein (CAT#: V2LY-0526-LY1572)

Human Recombinant IL33 protein, His & AVI Tag (CAT#: V2LY-0526-LY4897)

Human Recombinant IL33 protein (CAT#: V2LY-0526-LY4898)

Mouse Recombinant IL33 protein, His Tag (CAT#: V2LY-0526-LY8537)

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Isotype control

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

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