Anti-CSAD Rabbit Polyclonal Antibody for WB and ELISA - Q9Y600

Core Product Specifications and Parameters

Biological Background: CSAD Function and Localization

• Cysteine sulfinic acid decarboxylase (CSAD), also known as aspartate 1-decarboxylase, cysteine-sulfinate decarboxylase, or sulfinoalanine decarboxylase, is a pyridoxal phosphate-dependent enzyme.
• It catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine, and taurine, respectively; the preferred substrate is 3-sulfino-L-alanine.
• CSAD does not exhibit decarboxylation activity toward glutamate.
• The enzyme is expressed in liver and brain, with expression in both astrocytes and neurons (lower levels in astrocytes).
• Alternative splicing generates multiple isoforms of CSAD.
• The protein is a reference proteome component and has been identified in mass spectrometry-based proteomics.

Experimental Guidance and Technical Tips

• The immunogen spans amino acids 371-520 of human CSAD, a region likely responsible for the observed cross-reactivity with mouse and rat proteins.
• For Western blot, a major band around 55 kDa is predicted; however, isoform-specific expression or post-translational modifications may cause slight shifts in migration.
• ELISA procedures may benefit from optimization of coating antigen concentration and blocking conditions; consider validating with recombinant CSAD or tissue lysates from liver/brain.
• When working with novel sample types, perform pilot experiments to confirm specificity and optimize detection parameters.

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