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Proteasome 20S β1i subunit monoclonal antibody (LMP2 - 13)

BML-PW8840-0025 25 µl 157.00 USD
BML-PW8840-0100 100 µl 453.00 USD
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Product Details

Alternative Name:Proteasome subunit β type-9, RING12 protein, LMP2
Immunogen:Recombinant human β1i protein.
UniProt ID:P28065 (human), P28077 (rat)
Gene/Protein Identifier:PSMB9 (gene name)
Source:Purified from ascites.
Species reactivity:Human, Rat
Specificity:Recognizes the β1i subunit of proteasome 20S.
Applications:IHC, WB
Application Notes:The serum was characterised by single dimension SDS-PAGE using a HeLa cell lysate both with and without prior stimulation with γ-interferon. The mature LMP2 protein of ~22kDa was detected by Western blotting in the γ-interferon stimulated cells and additionally the precursor form at ~25kDa.
Not suitable for immunoprecipitation.
Purity Detail:Protein G-affinity purified ascites.
Formulation:Liquid. In PBS containing 10mM sodium azide.
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. 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. Lmp2, Lmp7 and MECL are interferon gamma-inducible catalytic subunits of the 20S proteasome which may replace the constitutive catalytic subunits, delta, X and Z respectively, during proteasome biogenesis. Lmp2 and Lmp7 alter the cleavage site specificity of the 20S proteasome and are required for the efficient generation of T cell epitopes from a number of viral proteins and for optimal MHC class I cell surface expression.
Technical Info/Product Notes:Various systems for the nomenclature of the proteasome subunits have been established. This may be a source of confusion as the system on UniProt differs from "standard" nomenclature as described in the literature. The UniProt ID and Gene Name will help to clearly identify the proteins.
Regulatory Status:RUO - Research Use Only

Product Literature References

A therapeutic T cell receptor mimic antibody targets tumor-associated PRAME peptide/HLA-I antigens: A.Y. Chang, et al.; J. Clin. Invest. 127, 2705 (2017), Abstract;
Detection of active proteasome structures in brain extracts: proteasome features of August rat brain with violations in monoamine metabolism: P.A. Erokhov, et al.; Oncotarget 8, 70695 (2017), Abstract; Full Text
Ubiquitin-independent proteosomal degradation of myelin basic protein contributes to development of neurodegenerative autoimmunity: A. Belogurov Jr, et al.; FASEB J. 29, 1901 (2015), Abstract; Full Text
Gene expression of catalytic proteasome subunits and resistance toward proteasome inhibition of B lymphocytes from patients with primary Sjögren syndrome: L. Martinez-Gamboa, et al.; J. Rheumatol. 40, 663 (2013), Application(s): Western blot, Abstract;
Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC-MS: V. Dechavanne, et al.; Protein Exp. Purif. 87, 100 (2013), Application(s): Western blot, Abstract;
Immunoproteasome expression is induced in mesial temporal lobe epilepsy: M. Mishto, et al.; Biochem. Biophys. Res. Commun. 408, 65 (2011), Application(s): Immunohistochemistry and Western blot, Abstract;
Studies on immunoproteasome in human liver. Part I: absence in fetuses, presence in normal subjects, and increased levels in chronic active hepatitis and cirrhosis: F. Vasuri, et al.; Biochem. Biophys. Res. Commun. 397, 301 (2010), Application(s): Immunohistochemistry and Western blot, Abstract;
The proteasome load versus capacity balance determines apoptotic sensitivity of multiple myeloma cells to proteasome inhibition: G. Bianchi, et al.; Blood 113, 3040 (2009), Application(s): Immunofluorescence and Western blot, Abstract; Full Text

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