Product Details
| Alternative Name: | TBP1, Tat-binding protein 1, 26S protease regulatory subunit 6A, Proteasome 26S subunit ATPase 3 |
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| Host: | Rabbit |
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| Immunogen: | Recombinant full length human His-FLAG-tagged Rpt5/S6a subunit. |
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| UniProt ID: | P17980 |
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| Species reactivity: | Human
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| Specificity: | Recognizes the Rpt5/S6a subunit of the 19S regulator complex. |
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| Applications: | WB
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| Formulation: | Liquid. In PBS containing 10mM sodium azide. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| 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 subunit 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. |
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| Regulatory Status: | RUO - Research Use Only |
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Luminograph of human placental proteasome preparation after SDS PAGE followed by blotting onto PVDF membrane and probing with antibody BML-PW8310. Antibody dilution 1:1000 using ECL procedure.
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Product Literature References
A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function: K.V. Ramachandran, et al.; Nat. Struct. Mol. Biol.
24, 419 (2017),
Abstract;
Full Text
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
Subunit arrangement in the human 20S proteasome.: F. Kopp; Proc. Natl. Acad. Sci. USA
94, 2939 (1997),
Abstract;
The 26S proteasome: subunits and functions.: K. Tanaka & C. Tsurumi; Mol. Biol. Rep.
24, 3 (1997),
Abstract;
