BML-PW8355-0100 100 µl
BML-PW8355-0025 25 µl
Product Specification
Formulation: Liquid. Antiserum containing 10mM sodium azide.
Immunogen: Synthetic peptide corresponding to aa 262-276 (T262DVSDLLHQYREANQ276) of human proteasome 20S (β5i subunit).
Source/Host: From rabbit.
Specificity: Recognizes human proteasome 20S (β5i subunit). Detects bands of ~25kDa (mature proteasome 20S β5i subunit) and of ~29kDa (precursor) by Western blot.
Application: Immunohistochemistry
Western Blot
Shipping: SHIPPED ON BLUE ICE
Long Term Storage: -20°C
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: After opening, prepare aliquots and store at -20°C.
Avoid freeze/thaw cycles.
Miscellaneous/General: 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.
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