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July 2006 |
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| Featured Products |
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DPPIV Activity Assay and Reagents
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Representation of DPPIV structure complexed with diprotin A |
 Kinetics of H-Gly-Pro-pNA cleavage by DPPIV
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DPPIV is a dipetidyl peptidase responsible for degradation of the peptide hormone GLP-1, an incretin hormone that stimulates insulin secretion and biosynthesis. DPPIV inhibitors, which lead to an increase in circulating levels of GLP-1, are being tested for the treatment of type II diabetes. The DPPIV Drug Discovery Kit is an activity assay designed to identify DPPIV inhibitors. The kit includes recombinant DPPIV, chromogenic and fluorogenic substrates, control inhibitor, assay buffer and detailed instructions.
DPPIV Drug Discovery Kit (Cat. # AK-499) Contains reagents sufficient for 96 assays |
Additional DPPIV reagents
DPPIV (human, recombinant) (Cat. # SE-434) Comprises residues Asn29-Pro766 and represents a naturally-occurring soluble form of DPPIV |
GP-AMC, Fluorogenic Substrate (Cat. # P-189) Fluorogenic substrate for DPPIV (kcat/Km=2.6 x 105 s-1M-1) |
GP-pNA, Chromogenic Substrate (Cat. # P-188) Chromogenic substrate for DPPIV |
DPPIV, rabbit pAb (Cat. # SA-451) Recognizes latent, active, and soluble forms from human, rat and mouse. Applications: WB |
P32/98 (Ile-thiazolidide) (PI-142) A competitive transition-state substrate analog inhibitor of DPPIV (Ki=30 nM). Has been used in vivo and in tissue culture |

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For related products: |
| GLP-1 peptides & antibodies | FAP antibody | proteases | protein tyrosine phosphatases | |
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| Dopamine Biosynthesis and Transporter Antibodies |
| Useful markers for dopaminergic, noradrenergic, and serotonergic neurons and for applications in depression, schizophrenia, Parkinson's disease and drug abuse research. |
DOPA Decarboxylase (bovine), rabbit pAb (Cat. # SA-487) Species reactivity: rat and bovine. Applications: WB |
 Western Blot analysis of bovine adrenal medulla lysate using the human DOPA decarboxylase (DDC) antibody (SA-505). |
DOPA Decarboxylase (bovine), sheep pAb (Cat. # SA-505) Species reactivity: human, rat, rabbit, canine, guinea pig, bovine and ovine. Applications: WB |
DOPA Decarboxylase (human), rabbit pAb (Cat. # SA-504) Species reactivity: human, rat, rabbit, canine, guinea pig, bovine and ovine. Applications: WB |
Dopamine Beta-Hydroxylase, N-terminus (human), sheep pAb (Cat. # SA-507) Species reactivity: human and primate. Applications: WB |
Dopamine Beta-Hydroxylase, C-terminus (human), sheep pAb (Cat. # SA-506) Species reactivity: human and mouse. Applications: WB |
Dopamine Transporter, Extracellular Loop (human), rabbit pAb (Cat. # SA-509) Species reactivity: human, mouse and primate. Applications: WB, IHC |
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Dopamine Transporter, C-terminus (human) rabbit pAb (Cat. # SA-508) Species reactivity: human, mouse and primate. Applications: WB, IHC |
| Ubiquitin-binding motifs conjugated to agarose useful for isolating and identifying ubiquitinylated proteins. |
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Dsk2 UBA-Agarose Conjugate (Cat. # UW9835) Efficiently captures K48-linked and K63-linked polyubiquitin chains. |
 UQ1-agarose binding of K48- and K63-linked ubiquitin chains analyzed by immunoblotting with an ubiquitinylated protein reactive antibody (PW8805).
Lane 1: Multi-ubiquitin chains (Ub2-7, K48-linked) (UW8860); Lane 2: Bound; Lane 3: Unbound; Lane 4: Multi-ubiquitin chains (Ub2-7, K63-linked) (UW9570); Lane 5: Bound; Lane 6: Unbound. |
UQ1 UBA Domain, Agarose Conjugate (Cat. # UW9830) Efficiently captures mono-ubiquitin and ubiquitin conjugates including free chains in a linkage independent manner. |
VPS9-derived CUE Domain, Agarose Conjugate (Cat. # UW9450) Vps9p is a S.cerevisiae exchange factor for the yeast Rab5 GTPase homolog Vps21p. The CUE domain. The isolated CUE domain can bind multi-ubiquitin chains and ubiquitylated substrates |
| Additional Ubiquitin-binding Protein Agarose Conjugates: |
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Request our new Ubiquitons & Zomes Product Guide
Contains over 250 products for ubiquitin and proteasome research, a useful guide to proteasome subunit nomenclature, and review articles by R.J. Mayer, University of Nottingham and B. Dahlmann, Institute of Biochemistry, Berlin. | |

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