Recombinant Human Ubiquitin+1 Protein, CF

Catalog # Availability Size / Price Qty
703-UB-025
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Ubiquitin+1 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Activity
Bioassay data are not available.
Source
E. coli-derived human Ubiquitin+1 protein
ATVID 10-His tagSS Ubiquitin
(Met1 – Gly75)
Accession # CAA44911
YADLREDPDRQDHHPGSGAQ
N-terminus C-terminus

The italicized carboxyl terminal sequence is generated by a frameshift in the mRNA.
Accession #
N-terminal Sequence
Analysis
Ala
Predicted Molecular Mass
13 kDa
SDS-PAGE
13 kDa, reducing conditions

Product Datasheets

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703-UB

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

703-UB

Formulation Supplied as a 0.2 μm filtered solution in PBS.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
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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).  

 

References
  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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