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Ubiquitin Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 2
- PROTOCOLS
- BACKGROUND
Application 
| IF, IHC-P, WB, E |
|---|---|
| Primary Accession | P0CG48 |
| Other Accession | P62975, P62972, P0CG69, P62976, P0CG71, P0CG63, Q63429, P0CG68, P0CG50, P0CH28, P0CG51, P0CG49, P0CG47, P0CG62, P0CG53, P05759, P62982, P62983, P62979, P15357, P79781, P62992, P62986, P63053, P62984, P0C273, P62987, P18101, P49632, P63048, P0CH09, P0CH08 |
| Reactivity | Human |
| Predicted | Yeast, Bovine, C.Elegans, Drosophila, Monkey, Mouse, Pig, Rabbit, Rat, Sheep, Chicken, Horse, Hamster, Xenopus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 77039 Da |
| Antigen Region | 36-66 aa |
| Gene ID | 7316 |
|---|---|
| Other Names | Polyubiquitin-C, Ubiquitin, UBC |
| Target/Specificity | This Ubiquitin antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 36-66 amino acids of human Ubiquitin. |
| Dilution | IF~~1:10~50 WB~~1:1000 IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Ubiquitin Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | UBC |
|---|---|
| Function | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. |
| Cellular Location | [Ubiquitin]: Cytoplasm. Nucleus. Mitochondrion outer membrane; Peripheral membrane protein |
Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein has been noticed in patients with Alzheimer's and Down syndrome.
References
Chan, Y.L., et al., Biochem. Biophys. Res. Commun. 215(2):682-690 (1995).
Cook, W.J., et al., J. Mol. Biol. 236(2):601-609 (1994).
Hubbard, M.J., et al., Biochim. Biophys. Acta 1200(2):191-196 (1994).
Wajih, N., et al., Protein Seq. Data Anal. 5(1):31-32 (1992).
Cook, W.J., et al., J. Biol. Chem. 267(23):16467-16471 (1992).
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