articular cartilage

OGT-IN-2 is a potent O-GlcNAc transferase (OGT) inhibitor. OGT-IN-2 inhibits sOGT and ncOGT with IC50 values of 30 μM and 53 μM, respectively[1]. OGT-IN-2 can be used for the research of articular diseases[1].

Type IX collagen (from bovine articular cartilage) is a highly purified protein that can stimulate the immune system in animals to produce specific antibodies against this collagen. Additionally, collagen acts as a substrate for matrix metalloproteinases (MMP).

Type XI collagen (from bovine articular cartilage) is an immunization-grade collagen protein that induces the animal immune system to produce specific antibodies against it. Additionally, this collagen serves as a hydrolytic substrate for matrix metalloproteinases (MMP).

Type IX collagen (from chick articular cartilage) is a collagen protein capable of stimulating the immune system of animals to produce specific antibodies against it. Additionally, this collagen serves as a hydrolytic substrate for MMP.

Type XI collagen (from chick articular cartilage) is a collagen protein capable of stimulating the immune system in animals to produce specific antibodies against it. Additionally, this collagen acts as a hydrolysis substrate for MMP.

Type II collagen (from porcine articular cartilage) is a collagen protein that can stimulate an animal's immune system to produce specific antibodies against this collagen. Additionally, collagen serves as a hydrolysis substrate for MMP.

Type IX collagen (from porcine articular cartilage) is a collagen protein sourced from pig cartilage that can stimulate the immune system in animals to produce specific antibodies against this collagen. Additionally, the protein serves as a hydrolytic substrate for MMP.

Type XI collagen (from porcine articular cartilage) serves as a collagen protein that can stimulate the animal immune system to produce specific antibodies against this collagen. Additionally, the collagen protein acts as a hydrolytic substrate for MMP.

Type II collagen ( from sheep articular cartilage) can stimulate the immune system in animals to produce specific antibodies against the collagen. Additionally, collagen serves as a hydrolytic substrate for MMP.

Type II collagen (from goat articular cartilage) is a collagen protein capable of stimulating the immune system in animals to produce specific antibodies against it. This collagen also serves as a hydrolytic substrate for matrix metalloproteinases (MMPs).

Type II collagen (from bovine articular cartilage)serves as the primary matrix protein in cartilage and is suitable for arthritis research.

Heneicosanoic acid (C21:0) (HEA) is a fatty acid found in human milk fat. HEA is also a part of the phospholipids of the articular cartilage boundary lubricant. HEA is a constituent of red blood cell fatty acids.

RCGD423, a small molecule gp130 modulator, prevents articular cartilage degeneration and promotes repair.

RO314724 is a HDAC inhibitor. RO314724 is also a a reversible, tightly binding, MMP inhibitor with a Ki of 26 nm. Matrix metalloproteinases (MMPs) belong to the key enzymes of the proteolytic destruction of cartilage matrix during chronic rheumatic diseases. Ro314724 displayed MMP-proteoglycanase inhibitory activity both in vitro and ex vivo and proved to be not harmful to the morphology, viability and proteoglycan biosynthesis of bovine articular cartilage explants.

Sodium iodoacetate, a specific inhibitor of GAPDH, can induce articular cartilage damage (OA) [1] [2].

Heneicosanoic acid (Standard) is the standard substance of Heneicosanoic acid, and it is applicable for quantitative analysis, quality control, and related research in biochemical experiments. Heneicosanoic acid (C21:0) (HEA) is a fatty acid found in human milk fat. HEA is also a part of the phospholipids of the articular cartilage boundary lubricant. HEA is a constituent of red blood cell fatty acids.