D1445
Anti-DPP4 (61-75) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Sinônimo(s):
Anti-ADABP, Anti-ADCP2, Anti-CD26, Anti-DPPIV, Anti-Dipeptidyl peptidase 4, Anti-TP103
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About This Item
Código UNSPSC:
12352203
NACRES:
NA.41
conjugado:
unconjugated
application:
WB
clone:
polyclonal
reatividade de espécies:
human
citations:
4
técnica(s):
western blot: 1:500-1:2,000
Produtos recomendados
fonte biológica
rabbit
conjugado
unconjugated
forma do anticorpo
IgG fraction of antiserum
tipo de produto de anticorpo
primary antibodies
clone
polyclonal
Formulário
buffered aqueous solution
peso molecular
antigen ~88 kDa
reatividade de espécies
human
técnica(s)
western blot: 1:500-1:2,000
nº de adesão UniProt
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... DPP4(1803)
Imunogênio
synthetic peptide corresponding to amino acids 61-75 of human DPP4
Aplicação
Anti-DPP4 antibody produced in rabbit is suitable for western blotting at a working dilution of 1:500-1:2000. Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.
Ações bioquímicas/fisiológicas
DPP4 is a cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. It regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. It removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini with proline as the penultimate residue. It is ubiquitously expressed in epithelial and endothelial cells and plays a role in the migration and invasion of human endothelial cells in collagenous matrices. ADA-DPP4 interaction on the cell surface regulates lymphocyte-epithelial cell adhesion. Dipeptidyl peptidase activity of this protein is inhibited by the binding of Simpson-Golabi-Behmel syndrome causative glypican-3.
forma física
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
Exoneração de responsabilidade
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 2
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Certificados de análise (COA)
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Giulio Ghersi et al.
Cancer research, 66(9), 4652-4661 (2006-05-03)
Dipeptidyl peptidase IV (DPP4/CD26) and seprase/fibroblast activation protein alpha are homologous type II transmembrane, homodimeric glycoproteins that exhibit unique prolyl peptidase activities. Human DPP4 is ubiquitously expressed in epithelial and endothelial cells and serves multiple functions in cleaving the penultimate
Kei Ohnuma et al.
The Journal of biological chemistry, 282(13), 10117-10131 (2007-02-09)
CD26 is a widely distributed 110-kDa cell surface glycoprotein with an important role in T-cell costimulation. We demonstrated previously that CD26 binds to caveolin-1 in antigen-presenting cells, and following exogenous CD26 stimulation, Tollip and IRAK-1 disengage from caveolin-1 in antigen-presenting
Silvia Ginés et al.
The Biochemical journal, 361(Pt 2), 203-209 (2002-01-05)
The extra-enzymic function of cell-surface adenosine deaminase (ADA), an enzyme mainly localized in the cytosol but also found on the cell surface of monocytes, B cells and T cells, has lately been the subject of numerous studies. Cell-surface ADA is
Jamshid Davoodi et al.
Proteomics, 7(13), 2300-2310 (2007-06-06)
Simpson-Golabi-Behmel syndrome (SGBS) is an X-linked condition shown to be the result of deletions of the glypican-3 (GPC3) gene. GPC3 is a proteoglycan localized to the cell membrane via a glycosylphosphatidyl-inositol (GPI) anchor. To further elucidate the GPC3 function(s), we
Cuiqing Ma et al.
Vaccine, 32(46), 6170-6176 (2014-09-23)
The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) is currently spreading among humans, making development of effective MERS vaccines a high priority. A defined receptor-binding domain (RBD) in MERS-CoV spike protein can potentially serve as a subunit vaccine candidate
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