PSMB2 Polyclonal Antibody, FITC Conjugated


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Cat.No.:  EAb-1179
Product Name:  PSMB2 Polyclonal Antibody, FITC Conjugated
Antibody Type:  Polyclonal
Conjugate:  FITC
Host:  Rabbit
Isotype:  IgG
Purification:  Protein G Purified
Appearance:  Liquid
Formulation:  0.03% Proclin 300, 50% Glycerol, 0.01M PBS, PH 7.4.
Applications:  ELISA
Species Reactivity:  Human
Storage:  -20°C
Warning:  For Research Use Only! Not For Use in Humans.
Alternative Name:  Macropain subunit C7-I, Multicatalytic endopeptidase complex subunit C7-I, Proteasome component C7-I
Scientific Background:  The proteasome is a multicatalytic proteinase complex with a highly ordered ring shaped 20S core structure. The core structure is composed of 4 rings of 28 non identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB2 is a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with a highly ordered ring shaped 20S core structure. The core structure is composed of 4 rings of 28 non identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin dependent process in a non lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B type family, also known as the T1B family, that is a 20S core beta subunit. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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