VTN Human, Sf9
Sf9, Insect cells.
VN, S-protein, Serum-spreading factor, V75, VTN.
Description
VTN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 468 amino acids (20-478a.a.) and having a molecular mass of 53.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
VTN is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Vitronectin (VTN), a member of the pexin family, is a cell adhesion and spreading factor present in serum and tissues. It interacts with glycosaminoglycans and proteoglycans, inhibiting the membrane-damaging effects of the terminal cytolytic complement pathway. VTN also binds to various serpin serine protease inhibitors. Notably, researchers have observed increased expression of VTN, integrins, and plasminogen in migrating cells during wound healing processes.
Produced in Sf9 insect cells, VTN is a single, glycosylated polypeptide chain comprising 468 amino acids (20-478a.a.). It has a molecular mass of 53.3 kDa. On SDS-PAGE, the molecular size appears approximately between 50-70 kDa.
This VTN protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
The VTN protein solution is provided at a concentration of 0.25 mg/ml and contains Phosphate Buffered Saline at a pH of 7.4, along with 10% glycerol.
To ensure long-term stability during storage, adding a carrier protein like HSA or BSA at a concentration of 0.1% is recommended.
Repeated freezing and thawing of the protein should be avoided.
The biological activity of VTN is evaluated by its ability to support the adhesion of B16-F10 mouse melanoma cells when the protein is immobilized. The ED50, which represents the effective concentration for 50% cell adhesion, is determined to be 5 µg/ml. This measurement is performed using plates coated with VTN, to which the cells are added.
VN, S-protein, Serum-spreading factor, V75, VTN.
Sf9, Insect cells.
ADPDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT
VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID
SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI
RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA
ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI
FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR
KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV
FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HLHHHHHH.
Product Science Overview
Vitronectin is composed of multiple domains that facilitate its interaction with various cell surface receptors, such as integrins and proteoglycans. These interactions are essential for mediating cell adhesion and signaling pathways that regulate cell survival, proliferation, and differentiation. The protein also binds to components of the complement system, inhibiting the formation of the membrane attack complex and thus protecting cells from lysis.
The production of human recombinant vitronectin in Sf9 cells involves the use of the baculovirus expression system. This system is advantageous due to its high yield and ability to produce complex proteins with post-translational modifications similar to those in mammalian cells. The recombinant vitronectin produced in Sf9 cells retains its functional properties, making it suitable for various biomedical applications.
One of the most significant applications of recombinant vitronectin is in the culture of human embryonic stem cells (hESCs) and induced pluripotent stem cells (iPSCs). Traditional culture methods often rely on undefined or animal-derived substrates, which can introduce variability and potential contaminants. Recombinant vitronectin provides a defined, xeno-free alternative that supports the self-renewal and pluripotency of stem cells .
Studies have shown that vitronectin interacts with integrins, particularly αVβ5, to mediate cell adhesion and promote the maintenance of stem cell characteristics . This interaction is crucial for the development of defined culture conditions that are essential for the clinical application of stem cell therapies.
The use of human recombinant vitronectin offers several advantages:
- Consistency: Being a defined substrate, it reduces variability in stem cell cultures.
- Safety: It eliminates the risk of animal-derived contaminants, making it suitable for clinical applications.
- Efficiency: It supports robust cell growth and differentiation, enhancing the scalability of stem cell production.
Future research is focused on optimizing the production and functional properties of recombinant vitronectin to further improve its efficacy in stem cell culture and other biomedical applications. The development of novel vitronectin variants with enhanced properties is also an area of active investigation .
In conclusion, human recombinant vitronectin produced in Sf9 cells represents a significant advancement in the field of regenerative medicine. Its ability to provide a consistent, safe, and efficient substrate for stem cell culture holds great promise for the future of cell-based therapies and tissue engineering.
