Technical Data
P4355-01
POH1 (Rpn11)
Description:
The 26S proteasome is responsible for most intracellular proteolysis in eukaryotes. POH1 (also known as Rpn11 in yeast) subunit of the 19S complex is responsible for substrate deubiquitination during proteasomal degradation. POH1 appears to be a Zn21-dependent protease, unlike all other known deubiquitinating enzymes (DUBs) that are cysteine proteases. POH1 was first identified as the human functional homolog of the S. pombe pad1 gene, which confers moderate resistance to chemotherapeutic drugs, and also to ultraviolet light when transiently overproduced in mammalian cells. Poh1-induced drug resistance is mediated through AP-1 transcription factors.

Applications:
Suitable for use in Western Blot and Immunoprecipitation. Other applications have not been tested.

Recommended Dilution:
Western Blot: 1-3ug/ml
Immunoprecipitation (Mouse): 7ug/IP reaction
Optimal dilutions to be determined by the researcher.

Positive Controls:
HeLa and NIH3T3

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

TypeIsotypeCloneGrade
PabAffinity Purified
SizeStorageShippingSourceHost
100ug4°C (-20°C Glycerol)Blue IceHumanRabbit
Concentration:
~0.25mg/ml
Immunogen:
Synthetic peptide derived from C-terminal region of POH1 (26S proteosome-associated pad1 homolog/ non-ATPase subunit also known as Rpn11 in yeast.
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.4, 0.1% sodium azide.
Specificity:
Recognizes the human and mouse POH1 proteins at ~35kD.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Hershko A, et al. Annu Rev Biochem 67:425-479, 1998. 2. Zwickl P, et al. Curr Opin Struct Biol 10:242-250, 2000. 3. Yao T, et al. Nature 419:403-407, 2002. 4. Amerik AY, et al. Biol Chem 381:981-992, 2000. 5. D’Andrea A, et al. Crit Rev Biochem MolBiol 33:337-352, 1998. 6. Sptaro V, et al. J Biol Che 272:30470-30475, 1997.