UBE2K / LIG Antibody (C-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
---|---|
Primary Accession | P61086 |
Reactivity | Human, Mouse, Rat, Rabbit, Zebrafish, Hamster, Monkey, Pig, Chicken, Goat, Horse, Xenopus, Bovine, Dog |
Host | Goat |
Clonality | Polyclonal |
Calculated MW | 22kDa |
Dilution | ELISA (1:2000), IHC-P (3.75 µg/ml), WB (1:2000) |
Gene ID | 3093 |
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Other Names | Ubiquitin-conjugating enzyme E2 K, 6.3.2.19, Huntingtin-interacting protein 2, HIP-2, Ubiquitin carrier protein, Ubiquitin-conjugating enzyme E2-25 kDa, Ubiquitin-conjugating enzyme E2(25K), Ubiquitin-conjugating enzyme E2-25K, Ubiquitin-protein ligase, UBE2K, HIP2, LIG |
Target/Specificity | Human UBE2K / HIP2. This antibody is expected to recognise isoform 1 (NP_005330.1), isoform 2 (NP_001104582.1) and isoform 3 (NP_001104583.1). |
Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
Precautions | UBE2K / LIG Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | UBE2K |
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Synonyms | HIP2, LIG |
Function | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1. |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:P61085}. |
Tissue Location | Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem. |
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Background
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein- dependent degradation of RB1.
References
Kalchman M.A.,et al.J. Biol. Chem. 271:19385-19394(1996).
Kikuchi J.,et al.Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000).
Furukawa Y.,et al.Electrophoresis 21:338-346(2000).
Li W.B.,et al.Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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