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prolactin induction of VEGF-C and Runx2 was inhibited partly by Carboxypeptidase-D inhibitors, implicating nitric oxide , produced by PRL-regulated Carboxypeptidase-D, in breast cancer progression
Carboxypeptidase-D (CPD) overexpression coincides with high-grade lung cancer and the CPD overexpression could reverse the inhibitory effects of miR-214
The human carboxypeptidase D transthyretin-like domain forms amyloid under physiological conditions.
Prolactin and R1881, acting through Stat5 and androgen receptor, act cooperatively to stimulate CPD gene transcription in breast cancer cells.
CPD immunostaining and testosterone/prolactin-stimulated CPD expression were higher in prostate cancer than benign tissues/cells. Elevated CPD increased NO production, which was abolished when both androgen and prolactin receptors were inhibited.
Carboxypeptidase D (CPD) is frequently upregulated in hepatocellular carcinoma; targeting CPD inhibits hepatocellular carcinoma cell proliferation through induction of G1 cell-cycle arrest and apoptosis.
Either high glucose or insulin (with low glucose) up-regulates beta-cell CPD (but not CPE).
Palmitoylation of carboxypeptidase D has a role in intracellular trafficking
The isolation and characterization of CPD from several haematopoietic tumour cells are reported.
First report to demonstrate carboxypeptidase D as part of the transforming growth factor (TGF)-beta pathway as a TGF-beta target gene implicated in the pathogenesis of lupus erythematosus.
prolactin or E2 up-regulated CPD mRNA and protein expression in MCF-7 breast cancer cells promoting their survival
CPD releases C-terminal Arg from peptides to provide the precursor substrate for inducible nitric oxide synthase, which enhances nitric oxide synthesis in macrophages.
CPD localization to the TGN requires both static retention involving the C-terminal domain and phosphorylation at a CK2 site, which regulates the binding of adaptor proteins.
The carboxypeptidase D homolog silver regulates memory formation via insulin pathway in Drosophila.(
Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior.
DmCPD1Bs conforms to the structure of N/E-type funnelins/M14B metallopeptidases, but it has two unique structural elements potentially involved in regulation of its activity
the Drosophila silver gene corresponds to a Carboxypeptidase D-like protein with three carboxypeptidase-like domains, a transmembrane domain, and a cytosolic tail
The molecular basis for the phenotype of 3 carboxypeptidase D mutations are presented.
Data show that Drosophila S2 cells produce multiple forms of carboxypeptidase D with different intracellular distributions.
The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities. The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus-binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
, carboxypeptidase D
, carboxypeptidase E