|Tested species reactivity||Human, Mouse|
|Published species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Raised against the C-term of human PA28-alpha.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes, and the endoplasmic reticulum. The 26S proteasome is an ATP-dependent, multisubunit (~31), barrel-shaped molecular machine with an apparent molecular weight of ~2.5 MDa. It consists of a 20S proteolytic core complex which is crowned at one or both ends by 19S regulatory subunit complexes. The 19S regulatory subunits recognize ubiquitinated proteins and play an essential role in unfolding and translocating targets into the lumen of the 20S subunit. An enzymatic cascade is responsible for the attachment of multiple ubiquitin molecules to lysine residues of proteins targeted for degradation. Several genetic diseases are associated with defects in the ubiquitin-proteasome pathway. Some examples of affected proteins include those linked to cystic fibrosis, Angelman and quote;s syndrome, and Liddle syndrome.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Spectroimmunohistochemistry: a novel form of MALDI mass spectrometry imaging coupled to immunohistochemistry for tracking antibodies.
38-2400 was used in immunohistochemistry to evaluate a new MALDI mass spectrometry technique for analyzing antibody staining
|Longuespée R,Boyon C,Desmons A,Kerdraon O,Leblanc E,Farré I,Vinatier D,Day R,Fournier I,Salzet M||Omics : a journal of integrative biology (18:132)||2014|
MALDI imaging mass spectrometry in ovarian cancer for tracking, identifying, and validating biomarkers.
38-2400 was used in immunohistochemistry to test if mass spectroscopy can be used to track ovarian carcinoma biomarkers using cancer-antigen 125
|El Ayed M,Bonnel D,Longuespée R,Castelier C,Franck J,Vergara D,Desmons A,Tasiemski A,Kenani A,Vinatier D,Day R,Fournier I,Salzet M||Medical science monitor : international medical journal of experimental and clinical research (16:BR233)||2010|