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Mouse Anti-CSAD Recombinant Antibody (P8G6) (CBMAB-C5916-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
P8G6
Antibody Isotype
IgG1
Application
ELISA, IHC, IF, IP, FuncS

Basic Information

Immunogen
IL-1beta activated HUVEC (human)
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Cysteine Sulfinic Acid Decarboxylase
Introduction
CSAD (Cysteine Sulfinic Acid Decarboxylase) is a Protein Coding gene. Diseases associated with CSAD include Disuse Amblyopia and Stiff-Person Syndrome. Among its related pathways are Viral mRNA Translation and Metabolism. Gene Ontology (GO) annotations related to this gene include pyridoxal phosphate binding and carboxy-lyase activity. An important paralog of this gene is GADL1.
Entrez Gene ID
51380
UniProt ID
Q9Y600
Alternative Names
Cysteine Sulfinic Acid Decarboxylase; P-Selectin Cytoplasmic Tail-Associated Protein; Cysteine-Sulfinate Decarboxylase; Sulfinoalanine Decarboxylase; EC 4.1.1.29; CSD; Cysteine Sulfinic Acid Decarboxylase-Related Protein; EC 4.1.1; PCAP;
Function
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. Does not exhibit any decarboxylation activity toward glutamate.
Biological Process
L-cysteine catabolic process to hypotaurine Source: UniProtKB
L-cysteine catabolic process to taurine Source: UniProtKB
Taurine biosynthetic process Source: UniProtKB-UniPathway
Cellular Location
Cytoplasm
More Infomation

Abbasian, N., Ghaderi-Najafabadi, M., Watson, E., Brown, J., Bursnall, D., Pawluczyk, I., ... & Bevington, A. (2021). Hepatic cysteine sulphinic acid decarboxylase depletion and defective taurine metabolism in a rat partial nephrectomy model of chronic kidney disease. BMC nephrology, 22(1), 1-12.

Tramonti, A., Contestabile, R., Florio, R., Nardella, C., Barile, A., & Di Salvo, M. L. (2021). A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase. Life, 11(5), 438.

Mahootchi, E., Raasakka, A., Luan, W., Muruganandam, G., Loris, R., Haavik, J., & Kursula, P. (2021). Structure and substrate specificity determinants of the taurine biosynthetic enzyme cysteine sulphinic acid decarboxylase. Journal of Structural Biology, 213(1), 107674.

Tevatia, R., Payne, S., Allen, J., White, D., Clemente, T. E., Cerutti, H., ... & Blum, P. (2019). A synthetic cdo/csad taurine pathway in the green unicellular alga Chlamydomonas reinhardtii. Algal Research, 40, 101491.

Wang, Y., Matye, D., Nguyen, N., Zhang, Y., & Li, T. (2018). HNF4α regulates CSAD to couple hepatic taurine production to bile acid synthesis in mice. Gene Expression, 18(3), 187.

Raasakka, A., Mahootchi, E., Winge, I., Luan, W., Kursula, P., & Haavik, J. (2018). Structure of the mouse acidic amino acid decarboxylase GADL1. Acta Crystallographica Section F: Structural Biology Communications, 74(1), 65-73.

Park, E., Park, S. Y., Cho, I. S., Kim, B. S., & Schuller-Levis, G. (2017). A novel cysteine sulfinic acid decarboxylase knock-out mouse: immune function (II). In Taurine 10 (pp. 449-460). Springer, Dordrecht.

Park, E., Park, S. Y., Cho, I. S., Kim, B. S., & Schuller-Levis, G. (2017). A novel cysteine sulfinic acid decarboxylase knock-out mouse: taurine distribution in various tissues with and without taurine supplementation. In Taurine 10 (pp. 461-474). Springer, Dordrecht.

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For research use only. Not intended for any clinical use.

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