BIRC3 Proteins

BIRC3 (Baculoviral IAP Repeat Containing 3) is a Protein Coding gene. Diseases associated with BIRC3 include Lymphoma, Mucosa-Associated Lymphoid Type and Marginal Zone B-Cell Lymphoma. Among its related pathways are Metabolism of proteins and ERK Signaling. Gene Ontology (GO) annotations related to this gene include ligase activity and cysteine-type endopeptidase inhibitor activity involved in apoptotic process. An important paralog of this gene is BIRC2.

The following recombinant BIRC3 proteins are manufactured in house under a complete QC system by CUSABIO. They are expressed by Yeast, E.coli, Baculovirus, Mammalian cell, In Vivo Biotinylation in E.coli. Highlights of these recombinant BIRC3 proteins as follow:
High purity, Low endotoxin, Multiple Tags, Animal-free, Wide applications (Cell assay, Protein-protein interaction, Drug-related studies, Enzymatic activity in vitro, Protein structure analysis, etc.)
In addition, various options on sizes, excellent technical support, and recombinant BIRC3 proteins custom service will be also offered.

BIRC3 Proteins Catalog

BIRC3 Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

BIRC3 Proteins for Mus musculus (Mouse)

BIRC3 Proteins for Homo sapiens (Human)

BIRC3 Background

Baculoviral inhibitors of apoptosis repeat-containing protein 3 (BIRC3), also called cellular inhibitors of apoptosis 2 (cIAP2), is a protein in humans that is encoded by BIRC3 gene [1][2]. The cIAP2 protein contains three BIR domains (BIR1-BIR3), a CARD (caspase-recruitment) domain and a RING (really interesting new gene) zinc-finger domain [3]. The RING domain of cIAP2 possesses E3 ubiquitin ligase activity, which directly regulates auto- or trans-ubiquitination and protein degradation [4][5]. The BIR1 domains of cIAP2 play a role in tumor necrosis factor (TNF) receptor-associated factor (TRAF) interactions and ubiquitination reactions [5][6]. Conze DB et al. demonstrated that cIAP1 ubiquitination of cIAP2 leads to low protein levels of cIAP2 in normal conditions by validating cIAP1 E3 ligase function with the cIAP1-null mouse [7]. Increased BIRC3, in combination with BIRC2, acts simultaneously as a positive factor for NF-kappa B signaling [8][9], but also as a molecular brake that provides modulatory control over the JNK signaling axis [10]. In the absence of both cIAP1 and cIAP2, TNF alpha-mediated NF- kappa B signaling is dramatically attenuated in many cells, including normal primary cells as well as transformed cancer cells [11]. Consequently, the dual loss of cIAP1 and cIAP2 greatly sensitizes cells to TNF alpha-mediated apoptosis. A recent report also suggests that cIAP1 and cIAP2 promote cancer cell survival by ubiquitinating RIP1, leading to constitutive RIP1 and NF-kappa B activity [12]. High expression of XIAP or cIAP2 is associated with shorter overall survival, and lower complete response rates for AML [13].

[1] Liston P, Roy N, et al. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes [J]. Nature. February 1996, 379 (6563): 349-53.
[2] Rothe M, Pan MG, et al. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins [J]. Cell. February 1996, 83 (7): 1243-52.
[3] Hinds MG, Norton RS, et al. Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat [J]. Nat Struct Biol 1999, 6: 648-651.
[4] Yang Y, Fang S, Jensen JP, et al. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli [J]. Science 2000, 288: 874-877.
[5] Vaux DL, Silke J. IAPs, RINGs and ubiquitylation [J]. Nat Rev Mol Cell Biol 2005, 6: 287-297.
[6] Samuel T, Welsh K, et al. Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases [J]. J Biol Chem 2006, 281: 1080-1090.
[7] Conze DB, Albert L, et al. Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo [J]. Mol Cell Biol 2005, 25: 3348-3356.
[8] Mahoney DJ, Cheung HH, et al. Both cIAP1 and cIAP2 regulate TNFalpha-mediated NF-kappaB activation.[J] Proc Natl Acad Sci U S A, 2008, 105:11778-11783.
[9] Varfolomeev E, Goncharov T, et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor-alpha (TNFalpha)-induced NF-kappaB activation [J]. J Biol Chem 2008, 283:24295-24299.
[10] B. M. Tan, N. W. Zammit, et al. Baculoviral inhibitors of apoptosis repeat containing (BIRC) proteins fine-tune TNF-induced nuclear factor κB and c-Jun N-terminal kinase signaling in mouse pancreatic beta cells [J]. Diabetologia volume 2013, 56, pages520-532 (2013).
[11] Varfolomeev E, Wayson SM, et al. The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kappaB activation independently of TRAF1 AND TRAF2 [J]. J Biol Chem 2006, 281: 29022- 29029.
[12] Bertrand MJ, Milutinovic S, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination [J]. Mol Cell 2008, 30: 689-700.
[13] Hess CJ, Berkhof J, et al. Activated intrinsic apoptosis pathway is a key related prognostic parameter in acute myeloid leukemia [J]. J Clin Oncol 2007, 25: 1209-1215.

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