Thrombospondin 1 Antibody [N18C17]

Application: Reactivity: Human, Mouse, Rat

Lane 1: ACHN, Lane 2: LN18, Lane 3: MEF

Usage Information

Dilution
WB1:1000 IP1:100

Application
WB, IP

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
170 kDa

Positive Control	ACHN cells; ScaBER cells; LN18 cells; mIMCD-3 cells; MEF cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Thrombospondin 1 Antibody [N18C17] detects endogenous levels of total Thrombospondin 1 protein.

Clone
N18C17

Synonym(s)
THBS1; Thrombospondin-1; Glycoprotein G; TSP; TSP1

Background
Thrombospondin-1 (TSP-1 or THBS1) is a homotrimeric matricellular glycoprotein secreted by platelets, endothelial cells, and fibroblasts, and integrates into the extracellular matrix to regulate tissue remodeling through a wide array of ligand interactions. TSP-1 consists of an N-terminal globular TSPN domain that forms a β-sandwich of 13 antiparallel strands with a distinctive irregular β4′ segment and a disulfide bond at Cys248, enabling binding to heparin, aggrecan, and integrin αvβ3. This is followed by a von Willebrand factor C domain, three type I repeats (TSRs) characterized by stacked tryptophan/arginine ladders and conserved WXXWCSXG motifs that mediate engagement with CD36 and CD47 and inhibit MMP2/9, EGF-like type II repeats, and 15 calponin homology repeats with an RGD motif in the last repeat conferring affinity for integrins αvβ3 and αIIbβ3. The protein terminates with a C-terminal lectin-like globular domain that binds proteoglycans and stabilizes oligomers through interchain disulfide bonds at Cys252 and Cys256. TSP-1 potently inhibits angiogenesis by clustering CD47, thereby disrupting VEGF-R2 and nitric oxide (NO) signaling via SHP-2 phosphatase recruitment and blockade of eNOS S-nitrosylation. TSP-1 also activates latent TGF-β1 through integrin αvβ3/β8-mediated, shear-dependent unfolding of the latency-associated peptide, leading to Smad2/3 phosphorylation and fibrosis. It induces anoikis and CD36-mediated apoptosis in endothelial and smooth muscle cells via caspase-8/3 cascades and inhibition of Fyn/FAK, while also paradoxically promoting leukocyte transmigration and phagocytosis through calreticulin/LRP1/CD91-mediated engulfment of apoptotic bodies or pathogens. TSP-1 deficiency exacerbates tumorigenesis by permitting pathological angiogenesis and immune evasion in models of breast and prostate cancer, while its 3TSR fragment possesses strong anti-angiogenic activity when released by ADAMTS1 cleavage.

Background

Thrombospondin-1 (TSP-1 or THBS1) is a homotrimeric matricellular glycoprotein secreted by platelets, endothelial cells, and fibroblasts, and integrates into the extracellular matrix to regulate tissue remodeling through a wide array of ligand interactions. TSP-1 consists of an N-terminal globular TSPN domain that forms a β-sandwich of 13 antiparallel strands with a distinctive irregular β4′ segment and a disulfide bond at Cys248, enabling binding to heparin, aggrecan, and integrin αvβ3. This is followed by a von Willebrand factor C domain, three type I repeats (TSRs) characterized by stacked tryptophan/arginine ladders and conserved WXXWCSXG motifs that mediate engagement with CD36 and CD47 and inhibit MMP2/9, EGF-like type II repeats, and 15 calponin homology repeats with an RGD motif in the last repeat conferring affinity for integrins αvβ3 and αIIbβ3. The protein terminates with a C-terminal lectin-like globular domain that binds proteoglycans and stabilizes oligomers through interchain disulfide bonds at Cys252 and Cys256. TSP-1 potently inhibits angiogenesis by clustering CD47, thereby disrupting VEGF-R2 and nitric oxide (NO) signaling via SHP-2 phosphatase recruitment and blockade of eNOS S-nitrosylation. TSP-1 also activates latent TGF-β1 through integrin αvβ3/β8-mediated, shear-dependent unfolding of the latency-associated peptide, leading to Smad2/3 phosphorylation and fibrosis. It induces anoikis and CD36-mediated apoptosis in endothelial and smooth muscle cells via caspase-8/3 cascades and inhibition of Fyn/FAK, while also paradoxically promoting leukocyte transmigration and phagocytosis through calreticulin/LRP1/CD91-mediated engulfment of apoptotic bodies or pathogens. TSP-1 deficiency exacerbates tumorigenesis by permitting pathological angiogenesis and immune evasion in models of breast and prostate cancer, while its 3TSR fragment possesses strong anti-angiogenic activity when released by ADAMTS1 cleavage.

References
https://pubmed.ncbi.nlm.nih.gov/16407063/ https://pubmed.ncbi.nlm.nih.gov/29137447/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%