The adhesive glycoprotein thrombospondin-1 (THBS1, TSP1) localizes to the extracellular matrix (ECM) and mediates interactions between cells and the ECM and among cells. Thrombospondin-1 is a multi-domain, glycosylated protein that interacts with a wide variety of extracellular targets, including matrix metalloproteinases (MMPs), collagens, cell receptors, growth factors, and cytokines. The protein structure of THBS1 includes an amino-terminal laminin G-like domain, a von Willebrand factor-binding domain, and multiple thrombospondin (TSP) repeated sequences designated as type I, type II, or type III repeats. Each thrombospondin domain interacts with a distinct type of cell surface ligands or protein targets. The amino-terminal domain interacts with aggrecan, heparin, and integrin proteins. Type I TSP repeats interact with MMPs and CD36, while carboxy-terminal repeats bind the thrombospondin receptor CD47 . Through these interactions, THBS1 exerts diverse effects on different signaling pathways, such as VEGF receptor/NO signaling, TGFβ signaling, and the NF-κB pathway . Thrombospondin-1 is an important regulator of many biological processes, including cell adhesion/migration, apoptosis, angiogenesis, inflammation, vascular function, and cancer development . The activity of thrombospondin-1 is mainly regulated by extracellular proteases. The metalloproteinase ADAMTS1 cleaves thrombospondin, resulting in the release of peptides with anti-angiogenic properties. Elastase and plasmin proteases degrade the THBS1 protein and down regulate its activity

Thrombospondin-1
Glycoprotein G
THBS1
TSP, TSP1

p07996

WB,IHC,IF,ICC,FC

WB 1:1000-1:2000
IHC 1:2000-1:8000
IF 1:500
ICC 1:100
FC 1:1000

Human,Mouse,Rat

Predicted size: 129 kDa

Rabbit

Endoplasmic reticulum. Sarcoplasmic reticulum.

Protein A affinity purified.

Recombinant Rabbit monoclonal

IgG

Liquid

PBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.