Proteasome19SRpt4/S10bsubunit,pAb正品原装,其它生化试剂

BML-PW8220-0100 100 µl
BML-PW8220-0025 25 µl
Product Specification
Alternative Name: Proteasome subunit p42
Formulation: Liquid. In PBS containing 10mM sodium azide.
Immunogen: Recombinant full length human p42.
Source/Host: From rabbit.
Specificity: Recognizes human and yeast proteasome 26S (19S regulator complex) (Rpt4/S10b subunit). Detects a band of ~44kDa 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. 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 ubstrate prior to insertion into the proteolytic core of the 20S proteasomes.
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