Human Ubiquitin+1 Biotinylated Antibody

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Product Details
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Human Ubiquitin+1 Biotinylated Antibody Summary

Species Reactivity
Detects human Ubiquitin+1 in direct ELISAs. This antibody recognizes an epitope from the carboxy-terminal segment that is unique to Ubiquitin+1. It does not cross-react with Ubiquitin.
Monoclonal Mouse IgG2B Clone # 83426
Protein A or G purified from hybridoma culture supernatant
E. coli-derived recombinant human Ubiquitin+1
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.


Recommended Concentration
Western Blot
1 µg/mL
Recombinant Human Ubiquitin+1 (Catalog # 703-UB)

Human Ubiquitin+1 Sandwich Immunoassay

Recommended Concentration
ELISA Detection (Matched Antibody Pair)
0.5-2.0 µg/mL 

Use in combination with:

Capture Reagent: Human Ubiquitin+1 Antibody (Catalog # MAB7031)

Standard: Recombinant Human Ubiquitin+1 Protein, CF (Catalog # 703-UB)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


Preparation and Storage

Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Ubiquitin+1

Ubiquitin (Ub) is a 6 - 7 kDa polypeptide whose name derives from the observation that Ubiquitin possesses a highly conserved structure that is found in virtually all plant and animal species (1, 2). Ubiquitin is globular in nature, 76 amino acids (aa) in length, contains multiple lysines plus two C‑terminal glycines. In human, there are at least four genes that code for Ubiquitin. Found on human chromosomes 17 (UbB), 2 (UbA-80), 19 (UbA-52) and 12 (UbC), all genes code for a Ubiquitin polymer that undergoes proteolytic processing to generate free, monoubiquitin (3 - 7). In general, about one-half of all Ubiquitin exists in a monomeric form within the cell (8). Ubiquitin can also be added posttranslationally to multiple cell proteins. In conjunction with Ubiquitin ligases E1, 2 and 3, Ubiquitin is covalently attached to amino groups on target molecules via its C-terminal glycines, either at the N-terminus, or on any exposed amino acid that precedes the target's C-terminus (9). Further structural complexity may be added through Ubiquitin binding to Ubiquitin. Depending upon the exact pattern created, cellular proteins possessing UAD (Ub‑associated domain) and UIM (Ub‑interacting motif) sequences will selectively bind ubiquitinated proteins and incorporate them into multiple signaling pathways or regulatory complexes (10, 11). The UbB gene codes for a 229 aa precursor. This precursor contains three contiguous head-to-tail, 76 aa Ub sequences that ends with a C-terminal cysteine. A truncated mutation for UbB, termed Ubiquitin+1, has now been reported, that shows a 20 aa substitution for the last Gly of the first Ub sequence, generating a 95 aa polypeptide (12). Although a mutation, this molecule is apparently commonly expressed (13). At low levels of expression, it is degraded in a proteosome-dependent manner. At high levels, it overwhelms the proteosome system and accumulates, inhibiting proteosome activity (13). This is suggested to contribute to pathology associated with polyglutamine diseases (14).  


  1. Rechsteiner, M. (1987) Annu. Rev. Cell Biol. 3:1.
  2. Hershko, A. and A. Ciechanover (1998) Annu. Rev. Biochem. 67:425.
  3. Kim, N-S. et al. (1998) J. Biochem. 124:35.
  4. Lund, P.K. et al. (1985) J. Biol. Chem. 260:7609.
  5. Redman, K.L. and M. Rechsteiner (1989) Nature 338:438.
  6. Monia, B.P. et al. (1989) J. Biol. Chem. 264:4093.
  7. Wiborg, O. et al. (1985) EMBO J. 4:755.
  8. Agell, N. et al. (1988) Proc. Natl. Acad. Sci. USA 85:3693.
  9. Ciechanover, A. and R. Ben-Saadon (2004) Trends Cell Biol. 14:103.
  10. Kim, H. T. et al. (2007) J. Biol. Chem. 282:17375.
  11. Ye, Y. and M. Rape (2009) Nat. Rev. Mol. Cell Biol. 10:755.
  12. van Leeuwen, F.W, et al. (1998) Science 279:242.
  13. van Tijn, P. et al. (2007) J. Cell Sci. 120:1615.
  14. de Pril, R. et al. (2004) Hum. Mol. Genet. 13:1803.
Long Name
frame shift mutant
Entrez Gene IDs
7314 (Human); 298693 (Rat)
Alternate Names
FLJ25987; MGC8385; polyubiquitin B; polyubiquitin-B; RPS27A; UBA52; UBC; ubiquitin B; Ubiquitin+1

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