Human Thrombospondin-1 Antibody Summary
Asn19-Pro1170
Accession # CAA32889
Applications
Human Thrombospondin-1 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human Thrombospondin-1 by Immunocytochemistry/Immunofluorescence ARPC1B-null and Wiskott–Aldrich syndrome platelets are similar.(a) Transmission electron microscopy (TEM) imaging of sections from normal donor, ARPC1B-null (Patient 1) and WASP-null patient platelets show typical structures including alpha -granules (white arrows), mitochondria (black arrows) and internal membrane systems (bars=500 nm; see Fig. 4 for further comparisons). (b) Immunofluorescence microscopy of cells stained for circumferential ring tubulin (green) and alpha -granule membrane P-selectin (red) shows that ARPC1B-null and WASP-null platelets appear small and dysmorphic compared to normal (bars=5 μm). (c) A comparison of circumferential ring diameter distributions confirmed that both ARPC1B-null and WASP-null platelets are significantly smaller than normal (P<0.0001, unpaired t-test; n=57 cells; 95% confidence intervals shown) and do not differ significantly from each other. Equivalent comparisons of all patients with WASP-null and normal control platelets is shown in Fig. 5a. (d) The morphology of a normal platelet showing the typical subcellular locations of tubulin (magenta), P-selectin (red) and alpha -granule cargo thrombospondin-1 (TSP1, green; bars=1 μm). (e) Collections of representative cells illustrate the range of abnormal features observed in ARPC1B-null and WASP-null platelets, including small size and the variable absence of internal contents (bars=1 μm). Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28368018), licensed under a CC-BY license. Not internally tested by R&D Systems.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Thrombospondin-1
Thrombospondin-1 (TSP-1) is a 150‑180 kDa charter member of the thrombospondin family of extracellular matrix proteins. Human TSP‑1 is synthesized as an 1170 amino acid (aa) precursor that contains an 18 aa signal sequence and 1152 aa mature molecule. The mature molecule has been described as containing three distinct regions that create the shape of a dumbbell. There is an intital, 140 aa N-terminal laminin G-like globular region that binds heparin (aa 19‑258). This is followed by an extended, central collagen-binding region that contains one type C von Willebrand factor domain, plus three TSP type I and three TSP type II (or EGF-like) domains (aa 259‑712). The C‑terminus (aa 713‑1170) appears as a large globule with two halves; one calcium‑binding region (aa 713‑950) with seven Asp‑rich TSP type III domains, and one terminal region (aa 951‑1170) with TSP‑unique motifs (1). This C-terminal region is believed to mediate CD47 and cell binding (2‑5). The TSP type I repeats have multiple functions. They bind to type V collagen, laminin, fibronectin and CD36. They also contain a recognition site for C‑mannosylation on Trp. Finally, a type I KRFK motif induces the release of mature TGF-b from LAP. This is an effect not found in TSP-2. The function of the type II repeats in unclear. TSP‑1 is secreted as a disulfide-linked 450 kDa homotrimer. The cysteines responsible lie just N‑terminal to the first type I TSP repeat. Mature human TSP-1 is 61% aa identical to human TSP-2. It is also 95%, 97% and 95% aa identical to mouse, dog and rat TSP-1, respectively.
- Lawler, J. and R.O. Hynes (1986) J. Cell Biol. 103:1635.
- Frazier, W.A. (1987) J. Cell Biol. 105:625.
- Sid, B. et al. (2004) Crit. Rev. Oncol. Hematol. 49:245.
- Floquet, N. et al. (2008) Anch. Biochem. Biophys. 478:103.
Product Datasheets
Citations for Human Thrombospondin-1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 6
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Development of an enzyme-linked immunosorbent assay for thrombospondin-1 and comparison of human plasma and serum concentrations
Authors: Johanna L Barclay, Sahar Keshvari, Jonathan P Whitehead, Warrick J Inder
Annals of Clinical Biochemistry: International Journal of Laboratory Medicine
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BMP-1 disrupts cell adhesion and enhances TGF-beta activation through cleavage of the matricellular protein thrombospondin-1
Authors: Cyril Anastasi, Patricia Rousselle, Maya Talantikite, Agnès Tessier, Caroline Cluzel, Alice Bachmann et al.
Science Signaling
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Development and clinical testing of individual immunoassays for the quantification of serum glycoproteins to diagnose prostate cancer
Authors: K Endt, J Goepfert, A Omlin, A Athanasiou, P Tennstedt, A Guenther, M Rainisio, DS Engeler, T Steuber, S Gillessen, T Joos, R Schiess
PLoS ONE, 2017-08-02;12(8):e0181557.
Species: Human
Sample Types: Tissue Homogenates
Applications: ELISA Development (Capture) -
Loss of the Arp2/3 complex component ARPC1B causes platelet abnormalities and predisposes to inflammatory disease
Authors: WH Kahr, FG Pluthero, A Elkadri, N Warner, M Drobac, CH Chen, RW Lo, L Li, R Li, Q Li, C Thoeni, J Pan, G Leung, I Lara-Corra, R Murchie, E Cutz, RM Laxer, J Upton, CM Roifman, RS Yeung, JH Brumell, AM Muise
Nat Commun, 2017-04-03;8(0):14816.
Species: Human
Sample Types: Whole Cells
Applications: ICC -
Normal ranges of angiogenesis regulatory proteins in human platelets.
Authors: Peterson JE, Zurakowski D, Italiano JE
Am. J. Hematol., 2010-07-01;85(7):487-93.
Species: Human
Sample Types: Cell Lysates
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Thrombospondin-1 is a glucocorticoid responsive protein in humans
Authors: Johanna L Barclay, Carolyn J Petersons, Sahar Keshvari, Jane Sorbello, Brenda L Mangelsdorf, Campbell H Thompson et al.
European Journal of Endocrinology
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