Proteasome activator 11S γ subunit polyclonal antibody



BML-PW8190-0025	25 µl	160.00 USD

BML-PW8190-0100	100 µl	481.00 USD
Do you need bulk/larger quantities?

Replaces Prod. #: ALX-210-297

Product Details

Alternative Name:	Proteasome activator complex subunit 3, PA28γ

Host:	Rabbit

Immunogen:	Synthetic peptide corresponding to aa 70-85 of human and mouse Ki autoantigen/PA28γ.

UniProt ID:	P61289 (human), P61290 (mouse)

Species reactivity:	Human, Mouse

Specificity:	Recognizes the γ subunit of proteasome activator 11S.

Applications:	IHC, WB

Application Notes:	Detects a band of ~31kDa by Western blot.

Formulation:	Liquid. Antiserum 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:	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. 20S Proteasomes degrade only unfolded proteins in an energy-independent manner, whereas 26S proteasomes degrade native and ubiquitinylated proteins in an ATP-dependent manner. The native protein substrates are recognised by subunits, some with ATP binding sites, of the outer 19S caps of the 26S proteasome.A second activator which can associate with the 20S proteasome in the absence of ATP is known as PA28 or the 11S regulator. The pure PA28 activator is a complex of two alternating subunits, PA28α and PA28β, which share approximately 50% homology but also show considerable similarity (30-40%) to a nuclear protein of unknown function, the Ki autoantigen (now referred to as PA28γ). These subunits, with an apparent relative molecular weight of approximately 29kDa, form ringlike heteromeric complexes of ~200kDa possibly with an α₃β₃ stoichiometry. Electron microscopic studies have shown PA28 to be a ring shaped particle which, like the 19S, caps the 20S proteasome, by binding to the α-rings, at both or either end. The complex may, however, be readily dissociated. The finding that PA28 modulates the proteasome-catalysed production of antigenic peptides presented to the immune system on MHC class I molecules indicates a cellular function of this activator in antigen processing.

Regulatory Status:	RUO - Research Use Only

Proteasome activator 11S γ subunit polyclonal antibody Western blot

Figure: Western blot analysis of HeLa cell lysate using Proteasome activator 11S gamma subunit, pAb (Prod. No. BML-PW8190).Method: SDS-PAGE was followed by blotting onto nitrocellulose and probing with antibody BML-PW 8190. Antibody dilution 1:1000 using ECL procedure (1 min exposure).

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Product Literature References

Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes: S. Meiners, et al.; J. Biol. Chem. 278, 21517 (2003), Abstract;

General Literature References

Molecular properties of the proteasome activator PA28 family proteins and gamma-interferon regulation: N. Tanahashi, et al.; Genes Cells 2, 195 (1997), Abstract;

PA28 subunits of the mouse proteasome: primary structures and chromosomal localization of the genes: E. Kandil, et al.; Immunogenetics 46, 337 (1997), Abstract;

Structural and functional properties of proteasome activator PA28: L. Kuehn & B. Dahlmann; Mol. Biol. Rep. 24, 89 (1997), Abstract;

A role for the proteasome regulator PA28alpha in antigen presentation: M. Groettrup, et al.; Nature 381, 166 (1996), Abstract;