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Description
Fibronectin-CH296 Protein, HumanProduct Specification Species Human Synonyms Fibronectin Curated, FN, Cold insoluble globulin (CIG) Accession P02751 15 Amino Acid Sequence Pro1361 Ser1637&Ala1812 Thr2107 Expression System E. coli Molecular Weight 58 68 kDa (Reducing) Purity >95% by SDS PAGE & HPLC. Endotoxin <0. 1EU g Conjugation Unconjugated Tag No Tag Physical Appearance Liquid Storage Buffer 12. 5 mM sodium citrate, 1. 25% sucrose, pH 6. 2 Stability & Storage Stable for 12 months
Product Specification
| Species | Human |
| Synonyms | Fibronectin Curated, FN, Cold-insoluble globulin (CIG) |
| Accession | P02751-15 |
| Amino Acid Sequence | Pro1361-Ser1637&Ala1812-Thr2107 |
| Expression System | E.coli |
| Molecular Weight | 58-68 kDa (Reducing) |
| Purity | >95% by SDS-PAGE & HPLC. |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | No Tag |
| Physical Appearance | Liquid |
| Storage Buffer | 12.5 mM sodium citrate, 1.25% sucrose, pH 6.2 |
| Stability & Storage | Stable for 12 months upon stored at -80℃ from the date of receipt. And avoid repeated freeze-thaws cycles. |
| Reference | Nature. 1990 Jun 14;345(6276):642-6. |
Background
Fibronectin-CH296 is a recombinant human fibronectin fragment developed in 1995. The protein comprises 574 amino acids with a molecular weight of 58–63 kDa, produced in E. coli expression systems. CH296 contains three critical functional domains derived from the parent fibronectin molecule:
1. Central Cell-Binding Domain (type III repeats 8-10): Contains the Arg-Gly-Asp (RGD) sequence that binds integrin VLA-5 (α5β1) on target cells.
2. Heparin-Binding Domain II (type III repeats 12-14): Mediates binding to viral particles via heparan sulfate moieties on retroviral/lentiviral envelopes.
3. CS-1 Site (alternatively-spliced IIICS region): Binds integrin VLA-4 (α4β1) expressed on hematopoietic cells, T cells, and monocytes. This domain organization enables co-localization of viral particles and target cells on the CH296-coated surface, dramatically enhancing transduction efficiency by increasing effective viral concentration at the cell membrane.
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