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Wählen Sie konfigurierbare Panels & Premixed-Kits - ODER - Kits für die zelluläre Signaltransduktion & MAPmates™
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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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48-602MAG
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Anti-BIRC2/IAP-2 antibody, clone 1E1-1-10 is an antibody against BIRC2/IAP-2 for use in western blotting.
More>>Anti-BIRC2/IAP-2 antibody, clone 1E1-1-10 is an antibody against BIRC2/IAP-2 for use in western blotting. Less<<
Anti-BIRC2/IAP-2, clone 1E1-1-10 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
BRC2/IAP-2, also known as IAP homolog B, Inhibitor of apoptosis protein 2 and Baculoviral IAP repeat-containing protein 2, and encoded by the gene BIRC2/API1/IAP2/MIHB/ RNF48, is a 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. BIRC2/IAP-2 also acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical pathways. Additionally, BIRC2/IAP-2 acts as an important regulator of innate immune signaling, and finally, BIRC2/IAP-2 plays an important role in the modulation of the cell cycle. BIRC2/IAP-21 is localized to nucleus except during apoptotic events. BIRC2/IAP-2 is expressed in fetal and adult tissues with a strong emphasis found in adult skeletal muscle, thymus, testis, ovary and pancreas with low or absent expression in blood and brain.
References
Product Information
Format
Purified
Presentation
Purified rat monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Anti-BIRC2/IAP-2 antibody, clone 1E1-1-10 is an antibody against BIRC2/IAP-2 for use in western blotting.
Key Applications
Western Blotting
Application Notes
Western Blotting Analysis: 2 µg/mL from a representative lot detected BIRC2/IAP-2 in C2C12 cell lysate.
Western Blotting Analysis: A representative lot from an independent laboratory detected BIRC2/IAP-2 in HeLa and Raji cell lysate (Gerlach, B., et al. (2011). Nature. 471(7340):591-596.).
Western Blotting Analysis: A representative lot from an independent laboratory detected BIRC2/IAP-2 in MEF cell lysate (Gerlach, B., et al. (2011). Nature. 471(7340):591-596.).
Western Blotting Analysis: A representative lot from an independent laboratory detected BIRC2/IAP-2 in stable cell lines expressing EYFP cIAP1 RING, or EYFP cIAP1 RING (Silke, J., et al. (2005). Proc Natl Acad Sci USA. 102(45):16182-16187.).
Biological Information
Immunogen
Linear peptide corresponding to the BIR 2 repeat region of mouse BIRC2/IAP-2.
Epitope
This antibody recognizes the BIR 2 repeat region of BIRC2/IAP-2.
Clone
1E1-1-10
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
~65 kDa observed. The calculated molecular weight of this protein is 70 kDa; however, this protein has been observed at lower molecular weights (Gerlach, B., et al. (2011). Nature. 471(7340):591-596.; Silke, J., et al. (2005). Proc Natl Acad Sci USA. 102(45):16182-16187.).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in NIH/3T3 cell lysate.
Western Blotting Analysis: 2 µg/mL of this antibody detected BIRC2/IAP-2 in 10 µg of NIH/3T3 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Members of the tumour necrosis factor (TNF) receptor superfamily have important functions in immunity and inflammation. Recently linear ubiquitin chains assembled by a complex containing HOIL-1 and HOIP (also known as RBCK1 and RNF31, respectively) were implicated in TNF signalling, yet their relevance in vivo remained uncertain. Here we identify SHARPIN as a third component of the linear ubiquitin chain assembly complex, recruited to the CD40 and TNF receptor signalling complexes together with its other constituents, HOIL-1 and HOIP. Mass spectrometry of TNF signalling complexes revealed RIP1 (also known as RIPK1) and NEMO (also known as IKKγ or IKBKG) to be linearly ubiquitinated. Mutation of the Sharpin gene (Sharpin(cpdm/cpdm)) causes chronic proliferative dermatitis (cpdm) characterized by inflammatory skin lesions and defective lymphoid organogenesis. Gene induction by TNF, CD40 ligand and interleukin-1β was attenuated in cpdm-derived cells which were rendered sensitive to TNF-induced death. Importantly, Tnf gene deficiency prevented skin lesions in cpdm mice. We conclude that by enabling linear ubiquitination in the TNF receptor signalling complex, SHARPIN interferes with TNF-induced cell death and, thereby, prevents inflammation. Our results provide evidence for the relevance of linear ubiquitination in vivo in preventing inflammation and regulating immune signalling.
Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance. Silke, John, et al. Proc. Natl. Acad. Sci. U.S.A., 102: 16182-7 (2005)
2004
Inhibitor of apoptosis (IAP) proteins, which bind to caspases via their baculoviral IAP repeat domains, also bear RING domains that enable them to promote ubiquitylation of themselves and other interacting proteins. Here we show that the RING domain of cIAP1 allows it to bind directly to the RING of X-linked IAP, causing its ubiquitylation and degradation by the proteasome, thus revealing a mechanism by which IAPs can regulate their abundance. Expression of a construct containing the RING of cellular IAP1 was able to deplete melanoma cells of endogenous X-linked IAP, promoted apoptosis, and also markedly reduced their clonogenicity when treated with cisplatin. Cross control of protein levels by RING domains may therefore enable their levels to be manipulated therapeutically.
