DPT Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q07507 |
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Clone Names | 81006100 |
Gene ID | 1805 |
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Other Names | Dermatopontin, Tyrosine-rich acidic matrix protein, TRAMP, DPT |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7485c was selected from the Center region of human DPT. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | DPT |
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Function | Seems to mediate adhesion by cell surface integrin binding. May serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. Enhances TGFB1 activity. Inhibits cell proliferation. Accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation (By similarity). |
Cellular Location | Secreted, extracellular space, extracellular matrix |
Tissue Location | Expressed in fibroblasts, heart, skeletal muscle, brain and pancreas. Expressed at an intermediate level in lung and kidney, and at a low level in liver and placenta. Expressed at a lower level in fibroblasts from hypertrophic scar lesional skin and in fibroblasts from patients with systemic sclerosis than in normal skin fibroblasts. |
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Provided below are standard protocols that you may find useful for product applications.
Background
DPT is an extracellular matrix protein with possible functions in cell-matrix interactions and matrix assembly. This protein is found in various tissues and many of its tyrosine residues are sulphated. The protein is postulated to modify the behavior of TGF-beta through interaction with decorin.
References
Cheung,C.L., Chan,B.Y. Hum. Mol. Genet. 18 (4), 679-687 (2009)Pochampally,R.R., Ylostalo,J. J. Bone Miner. Res. 22 (9), 1338-1349 (2007)Lunetta,K.L., D'Agostino,R.B. Sr. BMC Med. Genet. 8 SUPPL 1, S13 (2007)
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