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Mouse Anti-BIRC3 Recombinant Antibody (2B2) (CBMAB-C4677-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
2B2
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Human recombinant protein fragment corresponding to amino acids 255-529 of human BIRC3 produced in E.coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:2,000

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

Format
Liquid
Buffer
PBS, pH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
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
Baculoviral IAP Repeat Containing 3
Introduction
This gene encodes a member of the IAP family of proteins that inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. It contains 3 baculovirus IAP repeats and a ring finger domain. Transcript variants encoding the same isoform have been identified. [provided by RefSeq, Aug 2011]
Entrez Gene ID
330
UniProt ID
Q13489
Alternative Names
Baculoviral IAP Repeat Containing 3; Inhibitor Of Apoptosis Protein 1; Apoptosis Inhibitor 2; RING-Type E3 Ubiquitin Transferase BIRC3; TNFR2-TRAF-Signaling Complex Protein 1; TNFR2-TRAF Signaling Complex Protein; Cellular Inhibitor Of Apoptosis 2; Mammalian IAP Homolog C; RING Finger Protein 49; IAP Homolog C; C-IAP2; HIAP1; RNF49;
Function
Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.
Biological Process
Cell surface receptor signaling pathway Source: ProtInc
I-kappaB kinase/NF-kappaB signaling Source: Reactome
MyD88-independent toll-like receptor signaling pathway Source: Reactome
Negative regulation of apoptotic process Source: GO_Central
Negative regulation of necroptotic process Source: GO_Central
NIK/NF-kappaB signaling Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of protein ubiquitination Source: UniProtKB
Protein deubiquitination Source: Reactome
Regulation of apoptotic process Source: UniProtKB
Regulation of cell cycle Source: GO_Central
Regulation of cysteine-type endopeptidase activity Source: UniProtKB
Regulation of inflammatory response Source: UniProtKB
Regulation of innate immune response Source: UniProtKB
Regulation of necroptotic process Source: UniProtKB
Regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
Regulation of RIG-I signaling pathway Source: UniProtKB
Regulation of toll-like receptor signaling pathway Source: UniProtKB
Regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Tumor necrosis factor-mediated signaling pathway Source: Reactome
Cellular Location
Cytoplasm; Nucleus
Involvement in disease
A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.
PTM
Auto-ubiquitinated and degraded by the proteasome in apoptotic cells.
More Infomation

Cai, M., Shao, J., Yung, B., Wang, Y., Gao, N. N., Xu, X., ... & Yao, D. B. (2022). Baculoviral inhibitor of apoptosis protein repeat-containing protein 3 delays early Wallerian degeneration after sciatic nerve injury. Neural Regeneration Research, 17(4), 845.

Makuch-Kocka, A., Kocki, J., Brzozowska, A., Bogucki, J., Kołodziej, P., Płachno, B. J., & Bogucka-Kocka, A. (2021). The BIRC Family Genes Expression in Patients with Triple Negative Breast Cancer. International journal of molecular sciences, 22(4), 1820.

Li, S., Yang, P., Xu, L., & Li, M. (2021). Blocking of Birc3/TLR4/Myd88 signaling protects carbapenem-resistant klebsiella pneumoniae in a mouse model of infection. Transplant Immunology, 101464.

Frazzi, R. (2021). BIRC3 and BIRC5: multi‐faceted inhibitors in cancer. Cell & Bioscience, 11(1), 1-14.

Rath-Deschner, B., Nogueira, A. V. B., Memmert, S., Nokhbehsaim, M., Augusto Cirelli, J., Eick, S., ... & Damanaki, A. (2021). Regulation of anti-apoptotic SOD2 and BIRC3 in periodontal cells and tissues. International Journal of Molecular Sciences, 22(2), 591.

Chen, H. D., Guo, N., Song, S. S., Chen, C. H., Miao, Z. H., & He, J. X. (2020). Novel mutations in BRCA2 intron 11 and overexpression of COX-2 and BIRC3 mediate cellular resistance to PARP inhibitors. American journal of cancer research, 10(9), 2813.

Carusone, T. M., Cardiero, G., Cerreta, M., Mandrich, L., Moran, O., Porzio, E., ... & Manco, G. (2020). WTAP and BIRC3 are involved in the posttranscriptional mechanisms that impact on the expression and activity of the human lactonase PON2. Cell death & disease, 11(5), 1-17.

Fu, P. Y., Hu, B., Ma, X. L., Yang, Z. F., Yu, M. C., Sun, H. X., ... & Zhou, J. (2019). New insight into BIRC3: a novel prognostic indicator and a potential therapeutic target for liver cancer. Journal of cellular biochemistry, 120(4), 6035-6045.

Cao, J., Qiu, J., Wang, X., Lu, Z., Wang, D., Feng, H., ... & Wang, L. (2018). Identification of microRNA-124 in regulation of Hepatocellular carcinoma through BIRC3 and the NF-κB pathway. Journal of Cancer, 9(17), 3006.

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

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