RBCK1 Antibody
(Synonyms: C20orf18, RNF54, UBCE7IP3, XAP3, XAP4, RBCK1, RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, Heme-oxidized IRP2 ubiquitin ligase 1, Hepatitis B virus X-associated protein 4, RING finger protein 54, RING-type E3 ubiquitin transferase HOIL-1, Ubiquitin-conjugating enzyme 7-interacting protein 3, HOIL-1)RBCK1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to RBCK1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Mouse
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 |
Product Details
RBCK1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to RBCK1.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 55 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 57 kDa
Synthetic peptide corresponding to the N-terminal region of human RBCK1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
RBCK1 is an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types[1][2][3][4][5][6][7][8][9][10][11].
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Expression
Induction: By viral transfection. -
Isoforms & Post-Translational Modification
RBCK1 has 3 isoforms, Q9BYM8-1: amino acid length is 510, molecular weight is 57572 Da (predicted); Q9BYM8-3: amino acid length is 468, molecular weight is 52936 Da (predicted); Q9BYM8-4: amino acid length is 230, molecular weight is 25654 Da (predicted).Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome (By similarity)
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Subunit
Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31.
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SwissProt ID
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Synonyms
C20orf18, RNF54, UBCE7IP3, XAP3, XAP4, RBCK1, RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, Heme-oxidized IRP2 ubiquitin ligase 1, Hepatitis B virus X-associated protein 4, RING finger protein 54, RING-type E3 ubiquitin transferase HOIL-1, Ubiquitin-conjugating enzyme 7-interacting protein 3, HOIL-1
Documentation
[1]. Yamanaka K, et al. Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2. Nat Cell Biol. 2003 Apr;5(4):336-40. [Content Brief]
[2]. Tian Y, et al. RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation. J Biol Chem. 2007 Jun 8;282(23):16776-82. [Content Brief]
[3]. Zhang M, et al. Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3. Cell Res. 2008 Nov;18(11):1096-104. [Content Brief]
[4]. Kirisako T, et al. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J. 2006 Oct 18;25(20):4877-87. [Content Brief]
[5]. Tokunaga F, et al. Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat Cell Biol. 2009 Feb;11(2):123-32. [Content Brief]
[6]. Gerlach B, et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature. 2011 Mar 31;471(7340):591-6. [Content Brief]
[7]. Tokunaga F, et al. SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex. Nature. 2011 Mar 31;471(7340):633-6. [Content Brief]
[8]. Ikeda F, et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis. Nature. 2011 Mar 31;471(7340):637-41. [Content Brief]
[9]. Noad J, et al. LUBAC-synthesized linear ubiquitin chains restrict cytosol-invading bacteria by activating autophagy and NF-κB. Nat Microbiol. 2017 May 8;2:17063. [Content Brief]
[10]. Rivkin E, et al. The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis. Nature. 2013 Jun 20;498(7454):318-24. [Content Brief]
[11]. Haas TL, et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol Cell. 2009 Dec 11;36(5):831-44. [Content Brief]