Recombinant Human COL9A1 protein(Met1-Pro328), mFc-tagged

• Cat.No.: COL9A1-265H
• Product Overview: Recombinant Human COL9A1 (P20849-3) (Met1-Pro328) was expressed in HEK293, fused with Fc region of Mouse IgG1 at the C-terminus.

Specification

• Species: Human
• Source: HEK293
• Tag: mFc
• Protein Length: Met1-Pro328
• Form: Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human COL9A1/mFc is a disulfide-linked homodimer. The reduced monomer comprises 539 amino acids and has a predicted molecular mass of 59.2 kDa. The apparent molecular mass of the protein is approximately 62-72 in SDS-PAGE under reducing conditions.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Purity: > 95 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: COL9A1 collagen, type IX, alpha 1 [ Homo sapiens ]
• Official Symbol: COL9A1
• Synonyms: COL9A1; collagen, type IX, alpha 1; collagen alpha-1(IX) chain; alpha-1(IX) collagen chain; collagen IX, alpha-1 polypeptide; cartilage-specific short collagen; MED; EDM6; STL4; DJ149L1.1.2; FLJ40263
• Gene ID: 1297
• mRNA Refseq: NM_001851
• Protein Refseq: NP_001842
• MIM: 120210
• UniProt ID: P20849

Case Study

Case 1: Parsons P, et al. J Biol Chem. 2011

Type IX collagen is linked to type II collagen in cartilage, with its NC4 domain sticking out to interact with other molecules. To find these partners, we used the NC4 domain to search a chondrocyte cDNA library, discovering it mainly binds with fibronectin. This interaction was confirmed with lab tests showing it has a high affinity specifically for the NC4 domain, not involving the collagen strands. Both collagen and fibronectin are found together in cartilage, suggesting this bond plays a key role in maintaining cartilage structure.

Fig1. NC4 domain of type IX collagen interacts with human cellular FN in the yeast two-hybrid system.

Fig2. SPR sensogram. Analysis of a whole type IX collagen concentration series (0–200 nm) showing binding curves with curve fits for association events.

Case 2: Fresquet M, et al. J Biol Chem. 2007

Changes in matrilin-3 mess with bone growth, leading to early osteoarthritis. Most trouble spots are in the A-domain's structure, where they mess up how it folds and functions. When zinc is around, this domain stays snug and stable. Without zinc, it relaxes. Tests showed it clings to certain collagen types and cartilage proteins, but only when zinc is present. Some mutations can mess up this connection.

Fig1. Binding of type II collagen (10 μg/ml) to the matrilin-3 A-domain in the presence of 1 mM Zn2+, Ca2+, Mg2+ or Mn2+.

Fig2. Binding to collagen type II.

Application

Recombinant COL9A1 protein is drawing attention because of its potential benefits for joint health. Cartilage is super important for keeping our joints working well, acting like a cushion. COL9A1 helps maintain this structure and could be a game-changer for those dealing with osteoarthritis by repairing damaged cartilage, leading to less pain and more movement. Not stopping there, COL9A1 is also getting a nod in tissue engineering. Researchers are checking out its potential in creating artificial cartilage, which could be a breakthrough for surgeries that need new tissue. The focus here is on practical solutions to help folks live more comfortably and manage long-term joint issues better.

Fig1. Schematic diagram shows the involvement of ATRA in regulating the expression of COL9A1 in antler chondrocytes. (Hong-Liang Zhang, 2017)