VTN Human
Vitronectin Human Recombinant
Cat. No.
BT30136
Source
Escherichia Coli.
Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa.
VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
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. VTN exhibits inhibitory effects on the membrane-damaging activity of the terminal cytolytic complement pathway and demonstrates binding affinity to numerous serpin serine protease inhibitors. Notably, researchers have observed elevated levels of VTN, integrins, and plasminogen in migrating cells during the wound healing process.
Description
Recombinant Human VTN, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 482 amino acids (specifically, residues 20-478). It possesses a molecular weight of 54.7 kDa. This VTN variant is fused to a 23-amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic methods.
Physical Appearance
A sterile, filtered solution that is colorless.
Formulation
The VTN protein solution is provided at a concentration of 0.5 mg/ml. It is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure long-term stability during storage, the addition of a carrier protein (either 0.1% HSA or BSA) is advised. It's important to avoid subjecting the product to repeated cycles of freezing and thawing.
Purity
The purity of the protein is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDQESCKG 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 HL.
Product Science Overview
Introduction
Vitronectin is a large glycoprotein found in blood and the extracellular matrix (ECM). It plays a crucial role in various physiological processes, including cell adhesion, migration, and tissue repair. The recombinant form of vitronectin, known as Vitronectin (Human Recombinant), is produced using advanced biotechnological methods to ensure high purity and functionality.
Structure and Function
Vitronectin is composed of 459 amino acids and includes several functional domains:
- Somatomedin B domain: Involved in binding to the urokinase receptor and integrins.
- Hemopexin domain: Facilitates binding to heparin and collagen.
- Heparin-binding domain: Enhances interactions with glycosaminoglycans in the ECM.
These domains enable vitronectin to interact with a variety of cell surface receptors and ECM components, thereby influencing cell behavior and tissue organization .
Production of Human Recombinant Vitronectin
Recombinant human vitronectin is typically produced in mammalian cell lines, such as Chinese Hamster Ovary (CHO) cells or human embryonic kidney (HEK) cells. The gene encoding vitronectin is inserted into these cells, which then express and secrete the protein. The recombinant protein is subsequently purified using techniques like affinity chromatography to achieve high purity levels .
Applications
Recombinant human vitronectin is widely used in biomedical research and clinical applications:
- Cell Culture: It provides a defined surface for the feeder-free culture of human pluripotent stem cells (PSCs). When used with specific culture media, vitronectin supports the attachment, survival, and proliferation of PSCs, maintaining their pluripotency and normal growth characteristics .
- Tissue Engineering: Vitronectin-coated surfaces are used to enhance cell adhesion and proliferation in tissue engineering applications.
- Wound Healing: Due to its role in cell migration and tissue repair, vitronectin is explored for its potential in promoting wound healing and tissue regeneration.
Advantages of Recombinant Vitronectin
- Consistency: Recombinant production ensures batch-to-batch consistency, reducing variability in experimental results.
- Purity: High purity levels minimize the risk of contamination and unwanted immune responses.
- Defined Composition: The use of recombinant vitronectin provides a defined and controlled environment for cell culture and other applications, enhancing reproducibility and reliability .
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