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D1445

Sigma-Aldrich

Anti-DPP4 (61-75) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-ADABP, Anti-ADCP2, Anti-CD26, Anti-DPPIV, Anti-Dipeptidyl peptidase 4, Anti-TP103

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~88 kDa

species reactivity

human

technique(s)

western blot: 1:500-1:2,000

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DPP4(1803)

Immunogen

synthetic peptide corresponding to amino acids 61-75 of human DPP4

Application

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.

Biochem/physiol Actions

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.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

Disclaimer

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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WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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

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