Category: Proteins & Peptides

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  • Brand: Boster
  • Brand: Cell Guidance Systems
  • Brand: KACTUS
Reference: M16S

OptiCol™ Human Collagen Type I is isolated from human neo-natal fibroblast cells. These cells are cultured in optimal conditions allowing these cells to naturally and efficiently secrete extracellular matrix which is processed and purified to produce human collagen. Manufactured under stringent quality standards with high lot-to-lot consistency. Made up of 97% Type I human collagen and 3% Type III collagen. OptiCol™ Human Collagen Type I exhibits high monomer content (as measured by gel permeation chromatography).

Reference: M11L

OptiCol™ Human Collagen Type I is isolated from human neo-natal fibroblast cells. These cells are cultured in optimal conditions allowing these cells to naturally and efficiently secrete extracellular matrix which is processed and purified to produce human collagen. Manufactured under stringent quality standards with high lot-to-lot consistency. Made up of 97% Type I human collagen and 3% Type III collagen. OptiCol™ Human Collagen Type I exhibits high monomer content (as measured by gel permeation chromatography).

Reference: M18S

OptiCol™ Rat Type I Acid Soluble Collagen contains 100 mg at a concentration of approximately 4 mg/ml in a 0.02 M acetic acid solution (pH 2 to 3). Rat Tail collagen is soluble telo-collagen. Each product includes a bottle containing 100 mg of collagen solution accompanied with a bottle of pre-formulated neutralizing solution for the formation of a collagen gel.

Reference: M20S

OptiCol™ Human Collagen Type III is initially produced as procollagen, a protein consisting of three pro-α1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the procollagen molecule is modified by the cell.

Reference: M21L

OptiCol™ Human Collagen Type III is initially produced as procollagen, a protein consisting of three pro-α1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the procollagen molecule is modified by the cell. Enzymes modify the amino acids lysine and proline in the protein strands by adding chemical groups that are necessary for the strands to form a stable molecule and then later to crosslink to other molecules outside the cell.

Reference: M23L

OptiCol™ Human Collagen Type IV is the primary collagen found in the extracellular basement membranes separating a variety of epithelial and endothelial cells. It is a major component of the dermal-epidermal junction where it is mostly found in the lamina densa. It is a heterotrimeric molecule containing two α1-like and one α2-like chains. This Type IV collagen is isolated from human placenta and is purified using a multi-step process.

Reference: M24L

OptiCol™ Human Collagen Type IV is isolated from human placenta and is purified using a multi-step process. The product is supplied as a non-sterile powder containing 5 mg of Type IV collagen per vial. It is a heterotrimeric molecule containing two α1-like and one α2-like chains.

Reference: AP16

RGD peptide is a synthetic peptide containing the RGD cell attachment sequence found in fibronectin, vitronectin and many other matrix and serum proteins. This binding is mediated via a hydroscopic C-terminal sequence. The RGD motif is present at the N-terminal end of the peptide, allowing for optimal cell attachment via integrin receptors.

Reference: AP17

Poly-D-Lysine is a synthetic amino acid chain that is positively charged. The molecular weight of Poly-D-Lysine can vary significantly with lower molecular weight (30,000 Da) being less viscous and higher molecular weight (>300,000 Da) having more binding sites per molecule. This product’s molecular weight ranges from 70,000 to 150,000 Da yielding a solution viscosity for easy handling while providing sufficient binding sites for cell attachment.

Reference: AP18

Poly-L-Lysine is a synthetic amino acid chain that is positively charged having one hydrobromide per unit of Lysine. The molecular weight of Poly-L-Lysine can vary significantly with lower molecular weight (30,000 Da) being less viscous and higher molecular weight (>300,000 Da) having more binding sites per molecule. This product’s molecular weight ranges from 70,000 to 150,000 Da yielding a solution viscosity for easy handling while providing sufficient binding sites for cell attachment.

Reference: AP19

Poly-L-Ornithine is a synthetic amino acid chain that is positively charged having one hydrobromide per unit of ornithine. The molecular weight of Poly-L-Ornithine can vary significantly with lower molecular weight (30,000 Da) being less viscous and higher molecular weight (>300,000 Da) having more binding sites per molecule. This product’s molecular weight ranges from 70,000 to 150,000 Da yielding a solution viscosity for easy handling while providing sufficient binding sites for cell attachment.