Anti-Carboxypeptidase D, Domain 1 Antibody

This polyclonal antibody was generated against a purified His-tagged 15 kDa fragment of CPD (second half of the first, N-terminal carboxypeptidase domain) expressed in E. Coli and is specific for the C-terminal half of human CPD Domain 1.

Carboxypeptidase D (CPD) is a membrane glycoprotein with a single hydrophobic transmembrane anchor near the C-terminus and three tandem carboxypeptidase homology domains. Domains 1 and 2 are catalytically active but domain 3 is not. CPD cleaves only C-terminal Arg or Lys residues from proteins and has an acidic pH optimum of ~ 6.0. CPD is ubiquitously expressed and is especially high in macrophages. CPD is predominantly localized in the trans-Golgi and is involved in peptide and protein processing in the constitutive secretory pathway after initial furin cleavage and is also involved in processing microbial toxins such as Pseudomonas exotoxin. Drosophila lacking CPD die in the larval stage and CPD is an important target gene of TGF-ß in macrophages that is downregulated in lupus erythematosus. CPD-mediated generation of L-Arg enhances iNOS-dependent NO generation in mouse macrophages and promote NO production and cell survival in breast cancer cells.

From the laboratory of Randal A. Skidgel, PhD, University of Illinois at Chicago.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EB5002
Anti-Carboxypeptidase D, Domain 1 Antibody, 50uL
50uL In stock
Price: $350.00
Specifications
Product Type: Antibody
Accession ID: O75976, U65090
Antigen: Carboxypeptidase D (CPD)
Molecular Weight: 180 kDa
Isotype: Antiserum
Clonality: Polyclonal
Reactivity: Human (other species not tested)
Immunogen: purified His-tagged 15 kDa fragment of CPD (second half of the first, N-terminal carboxypeptidase domain) expressed in E. Coli
Species Immunized: Rabbit
Epitope: CPD domain 1, C-terminal half
Buffer: Serum
Tested Applications: WB (1:1000)
Storage: -20C
Shipped: Cold packs
Provider
From the laboratory of Randal A. Skidgel, PhD, University of Illinois at Chicago.
References
  1. McGwire, G. B., Tan, F., Michel, B., Rehli, M., and Skidgel, R. A. Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein. (1997) Life Sci. 60, 715-724.
  2. Tan, F., Rehli, M., Krause, S. W., and Skidgel, R. A. Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. (1997) Biochem. J. 327, 81-87.
  3. Hadkar, V., and Skidgel, R. A. Carboxypeptidase D is up-regulated in RAW 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium. (2001) Mol. Pharmacol. 59, 1324-1332.
  4. Sangsree, S., Brovkovych, V., Minshall, R. D., and Skidgel, R. A. Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor agonists. (2003) Am J Physiol Heart Circ Physiol 284, H1959-1968.
  5. Skidgel, R. A., and Erdös, E. G. Cellular carboxypeptidases. (1998) Immunol. Rev. 161, 129-141.

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