|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||22407 Da|
|Other Names||Ubiquitin-conjugating enzyme E2 K, 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||A synthetic peptide corresponding to residues of human UBC1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||UBC-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|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.
The covalent attachment of ubiquitin to cellular proteins is catalyzed by members of a family of ubiquitin-conjugating enzymes, including UBC1 (E2). These enzymes participate in a variety of cellular processes, including selective protein degradation, DNA repair, cell cycle control, and sporulation (1). In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes (E1 and E3, respectively) functionally linked by ubiquitin carrier protein UBC1 (E2). Carrier protein has been proposed to constitute a family of isozymes having molecular masses of 14, 17, 20, 24, and 32 kDa whose role is to shuttle activated polypeptide in the form of a high-energy thiol ester intermediate to the carboxyl terminus of ubiquitin (2). The order of ubiquitin transfer is from E1 to E2, from E2 to E6-AP, and finally from E6-AP to a substrate (3).
1. Seufert W, et al. EMBO J., 9(13):4535-41, 1990.
2. Haas AL, et al. J Biol Chem, 263(26):13258-67, 1988.
3. Scheffner M, et al. Nature, 373(6509):81-3, 1995.
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