SKU(재고 관리 코드):PDMH100109
Recombinant Human MMP8/CLG1 protein (His tag)
Recombinant Human MMP8/CLG1 protein (His tag)
A DNA sequence encoding the Human MMP8 protein (P22894) (Met1-Gly467) was expressed with a C-His.
The Recombinant Human MMP8/CLG1 Protein (HIS TAG) is a highly purified and bioactive protein that has been produced using advanced recombinant DNA technology. This protein is a member of the matrix metalloproteinase (MMP) family and is also known as collagenase 1 (CLG1). It is expressed in a proenzyme form and can be activated by proteolytic cleavage.
The Recombinant Human MMP8/CLG1 Protein (HIS TAG) is provided in a lyophilized form, ensuring its stability and long shelf life. It is produced in a mammalian expression system, resulting in a protein that closely resembles the native human MMP8/CLG1. The protein is tagged with a histidine (HIS) tag, which allows for easy purification using affinity chromatography techniques.
This protein is widely used in various research applications, including studies on extracellular matrix remodeling, tissue repair, and wound healing. It plays a crucial role in the degradation of collagen, a major component of the extracellular matrix, and is involved in tissue remodeling processes. The Recombinant Human MMP8/CLG1 Protein (HIS TAG) can be used to investigate the mechanisms underlying these processes and to study the effects of MMP8/CLG1 on cell behavior and tissue homeostasis.
The Recombinant Human MMP8/CLG1 Protein (HIS TAG) is provided with high purity, ensuring reliable and reproducible results in experiments. It is recommended to reconstitute the lyophilized protein in sterile water or an aqueous buffer before use. The protein can be stored at -20°C for long-term storage or at 4°C for short-term storage.
In summary, the Recombinant Human MMP8/CLG1 Protein (HIS TAG) is a valuable tool for researchers studying extracellular matrix remodeling, tissue repair, and wound healing. Its high purity, stability, and bioactivity make it an ideal choice for various experimental applications.