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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 |
|---|---|
| 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 |
|---|---|
| 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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Provided below are standard protocols that you may find useful for product applications.
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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