UBA5 Antibody
(Synonyms: UBE1DC1, UBA5, Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1)UBA5 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to UBA5.
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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, Rat
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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
UBA5 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to UBA5.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 45 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: 44 kDa
Synthetic peptide corresponding to the C-term region of human UBA5.
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
UBA5 is an E1-like enzyme which specifically catalyzes the first step in ufmylation. Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP. Activates UFM1 via a trans-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer. Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding. Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism. Ufmylation plays a key role in various processes, such as ribosome recycling, response to DNA damage, interferon response or reticulophagy (also called ER-phagy). Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes (By similarity)[1][2][3][4][5][6][7][8][9][10][11][12][13][14].
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Subcellular Localization
Cytoplasm; Nucleus; Endoplasmic reticulum membrane; Golgi apparatus
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Expression
Tissue_Specificity: Widely expressed. -
Isoforms & Post-Translational Modification
UBA5 has 2 isoforms, Q9GZZ9-1: amino acid length is 404, molecular weight is 44863 Da (predicted); Q9GZZ9-2: amino acid length is 348, molecular weight is 38537 Da (predicted).UBA5 存在 2 个异构体,Q9GZZ9-1:氨基酸个数为 404 个,分子量为 44863 Da (预测);Q9GZZ9-2:氨基酸个数为 348 个,分子量为 38537 Da (预测)。
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Subunit
Homodimer; homodimerization is required for UFM1 activation.
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SwissProt ID
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Synonyms
UBE1DC1, UBA5, Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1
Documentation
[1]. Komatsu M, et al. A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. EMBO J. 2004 May 5;23(9):1977-86. [Content Brief]
[2]. Zheng M, et al. UBE1DC1, an ubiquitin-activating enzyme, activates two different ubiquitin-like proteins. J Cell Biochem. 2008 Aug 15;104(6):2324-34. [Content Brief]
[3]. Bacik JP, et al. Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme. J Biol Chem. 2010 Jun 25;285(26):20273-80. [Content Brief]
[4]. Yoo HM, et al. Modification of ASC1 by UFM1 is crucial for ERα transactivation and breast cancer development. Mol Cell. 2014 Oct 23;56(2):261-274. [Content Brief]
[5]. Habisov S, et al. Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. J Biol Chem. 2016 Apr 22;291(17):9025-41. [Content Brief]
[6]. Muona M, et al. Biallelic Variants in UBA5 Link Dysfunctional UFM1 Ubiquitin-like Modifier Pathway to Severe Infantile-Onset Encephalopathy. Am J Hum Genet. 2016 Sep 1;99(3):683-694. [Content Brief]
[7]. Colin E, et al. Biallelic Variants in UBA5 Reveal that Disruption of the UFM1 Cascade Can Result in Early-Onset Encephalopathy. Am J Hum Genet. 2016 Sep 1;99(3):695-703. [Content Brief]
[8]. Oweis W, et al. Trans-Binding Mechanism of Ubiquitin-like Protein Activation Revealed by a UBA5-UFM1 Complex. Cell Rep. 2016 Sep 20;16(12):3113-3120. [Content Brief]
[9]. Soudah N, et al. An N-Terminal Extension to UBA5 Adenylation Domain Boosts UFM1 Activation: Isoform-Specific Differences in Ubiquitin-like Protein Activation. J Mol Biol. 2019 Feb 1;431(3):463-478. [Content Brief]
[10]. Walczak CP, et al. Ribosomal protein RPL26 is the principal target of UFMylation. Proc Natl Acad Sci U S A. 2019 Jan 22;116(4):1299-1308. [Content Brief]
[11]. Kumar M, et al. Structural basis for UFM1 transfer from UBA5 to UFC1. Nat Commun. 2021 Sep 29;12(1):5708. [Content Brief]
[12]. Mashahreh B, et al. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding. FASEB J. 2018 May;32(5):2794-2802. [Content Brief]
[13]. Liang JR, et al. A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation. Cell. 2020 Mar 19;180(6):1160-1177.e20. [Content Brief]
[14]. Snider DL, et al. Signaling from the RNA sensor RIG-I is regulated by ufmylation. Proc Natl Acad Sci U S A. 2022 Apr 12;119(15):e2119531119. [Content Brief]