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Proteasome 19S Rpt2/S4 subunit polyclonal antibody

BML-PW8305-0025 25 µl 110.00 USD
BML-PW8305-0100 100 µl 345.00 USD
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Replaces Prod. #: ALX-210-319

Product Details

Alternative Name:Proteasome 26S subunit ATPase 1, 26S protease regulatory subunit 4
Immunogen:Recombinant full length human proteasome 26S (19S regulator complex) (Rpt2/S4 subunit).
UniProt ID:P62191
Species reactivity:Human, Mouse, Rat
Specificity:Recognizes the Rpt2/S4 subunit of the 19S regulator complex.
Applications:IP, WB
Application Notes:Single dimension SDS-PAGE of human placental proteasome preparation followed by Western blotting gives a single band with a relative molecular weight of approximately 55kDa.
Formulation:Liquid. In PBS containing 10mM sodium azide.
Use/Stability:Dilute with PBS, pH 7.2-7.4 containing 1% normal goat serum (if a goat anti-rabbit IgG linker antibody is to be used). Store diluted antibody at +4°C (do not freeze) and use within 1 month.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
Scientific Background:The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation.  It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing.  The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation.  The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings.In addition to the 20S particle, the 26S complex contains over twenty additional proteins, ranging in molecular weight from 25 to 10kDa, located in a distinct complex called the ‘PA700 proteasome activator’ or the ‘19S complex’, and which determines substrate specificity and provides the multiple enzymatic functions necessary for proteolysis and viability. Systematic analysis of the sub-unit components have revealed at least six members to be ATPases belonging to a new family of ATP-binding proteins, together with a further fifteen sub-units that lack the capacity to bind ATP, isopeptidases and several other proteins thought to be responsible for the unfolding of a protein substrate prior to insertion into the proteolytic core of the 20S proteasome. Subunit roles and interactions are now being more fully defined.
Regulatory Status:RUO - Research Use Only
Proteasome 19S Rpt2/S4 subunit polyclonal antibody Western blot
Figure: Western blot analysis of human placental proteasome using Proteasome 19S Rpt2/S4 subunit, pAb (Prod. No. BML-PW8305).Method: SDS-PAGE was followed by blotting onto PVDF and probing with antibody BML-PW8305.  Antibody dilution 1:1000 using ECL procedure.
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Proteasome 19S Rpt2/S4 subunit polyclonal antibody Western blot

Product Literature References

The conserved RNA recognition motif and C3H1 domain of the Not4 ubiquitin ligase regulate in vivo ligase function: H. Chen, et al.; Sci. Rep. 8, 8163 (2018), Abstract; Full Text
Bortezomib Amplifies Effect on Intracellular Proteasomes by Changing Proteasome Structure: D.S. Pitcher, et al.; EBioMedicine 2, 642 (2015), Application(s): Western Blot, Abstract;
Nuclear proteasomes carry a constitutive posttranslational modification which derails SDS-PAGE (but not CTAB-PAGE): D.S. Pitcher, et al.; Biochim. Biophys. Acta 1844, 2222 (2014), Abstract;
TRIM5α associates with proteasomal subunits in cells while in complex with HIV-1 virions: Z. Lukic, et al.; Retrovirology 8, 93 (2011), Abstract; Full Text

General Literature References

Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7: C. Gorbea, et al.; J. Biol. Chem. 275, 875 (2000), Abstract; Full Text
Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases: N. Tanahashi, et al.; BBRC 243, 229 (1998), Abstract;
Subunit arrangement in the human 20S proteasome: F. Kopp, et al.; PNAS 94, 2939 (1997), Abstract; Full Text
The 26S proteasome: subunits and functions: K. Tanaka & C. Tsurumi; Mol. Biol. Rep. 24, 3 (1997), Abstract;

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