Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG1 |
clonality | monoclonal |
concentration | 1 mg/mL |
applications | ICC/IF, WB |
reactivity | cdc34 |
available sizes | 100 µg |
mouse anti-cdc34 monoclonal antibody (14B5) 7470
$503.00
Antibody summary
- Mouse monoclonal to cdc34
- Suitable for: WB,ICC/IF,IHC-P,IP
- Isotype: IgG1
- 100 µg
mouse anti-cdc34 monoclonal antibody (14B5) 7470
antibody |
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Tested applications WB,IHC,IHC,ICC/IF |
Recommended dilutions Immunoblotting and Immuno-precipitation: use at 1-5 ug/mL. Positive controls: 293 cells and recombinant fusion protein. |
Immunogen N-terminus 6x-His tagged fusion protein encoding full-length human Cdc34 expressed in E. coli. |
Size and concentration 100µg and lot specific |
Form liquid |
Storage Instructions This antibody is stable for at least one (1) year at -20°C. Avoid multiple freeze- thaw cycles. |
Storage buffer 10 mM PBS, pH 7.4. |
Purity immunogen affinty purifcation |
Clonality monoclonal |
Isotype IgG1 |
Compatible secondaries goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486 goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854 goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706 goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721 |
Isotype control Mouse monocolonal IgG1 - Isotype Control |
target relevance |
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Protein names Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1) |
Gene names CDC34,CDC34 UBCH3 UBE2R1 |
Protein family Ubiquitin-conjugating enzyme family |
Mass 26737Da |
Function Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:10329681, PubMed:10373550, PubMed:10871850, PubMed:11675391, PubMed:12037680, PubMed:15652359, PubMed:17461777, PubMed:17698585, PubMed:19112177, PubMed:19126550, PubMed:19945379, PubMed:20061386, PubMed:20347421). |
Catalytic activity CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence=; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.24; Evidence=; |
Pathway PATHWAY: Protein modification; protein ubiquitination. |
Subellular location Cytoplasm. Nucleus. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase. |
Tissues Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription. |
Structure Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened (PubMed:10918611, PubMed:11675391, PubMed:18851830, PubMed:19945379, PubMed:19112177, PubMed:24316736). When phosphorylated, interacts with beta-TrCP (BTRC) (PubMed:12037680). Interacts with human herpes virus 1 protein ICP0 and associates with the proteasome for degradation (PubMed:11447293, PubMed:11805320, PubMed:12060736). Interacts with casein kinase subunit CSNK2B (PubMed:11546811). Interacts with CNTD1; this interaction regulates the cell-cycle progression (By similarity). |
Post-translational modification Autoubiquitinated (PubMed:22496338, PubMed:11805320, PubMed:12060736). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736).; Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controls the nuclear localization. |
Target Relevance information above includes information from UniProt accession: P49427 |
The UniProt Consortium |
Publications
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Western blot IHC ICC |
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