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Description
GFP His Tag protein, Aequorea victoriaProduct Specification Species Aequorea victoria Antigen GFP Synonyms GFP Protein Accession AAB65663 Amino Acid Sequence Ser2 Lys238, with N terminal 8*His HHHHHHHHSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK Expression System E. coli Molecular Weight 27. 8kDa
Product Specification
| Species | Aequorea victoria |
| Antigen | GFP |
| Synonyms | GFP Protein |
| Accession | AAB65663 |
| Amino Acid Sequence | Ser2-Lys238, with N-terminal 8*His HHHHHHHHSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK |
| Expression System | E.coli |
| Molecular Weight | 27.8kDa |
| Purity | ＞95% by SDS-PAGE&RP-HPLC |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4 |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied; 6 months, -20 to -70 °C under sterile conditions after reconstitution; 1 week, 2 to 8 °C under sterile conditions after reconstitution; Please avoid repeated freeze-thaw cycles. |
| Reference | 1.Trends Biochem Sci 1995 Nov;20(11):448-55. |
Background
The green fluorescent protein (GFP) is a protein that exhibit bright green fluorescence when exposed to blue light. It is a widely used reporter in gene expression and protein localization studies. the green fluorescent protein (GFP) from the jellyfish Aequorea victoria is a widely used reporter in studies of gene expression and protein localization. GFP is a single chain polypeptide of 238 amino acids .Most of these amino acids form β sheets that are compacted through an antiparallel structure to form the barrel. So far, they have been used as reporters of gene expression, tracers of cell lineage, and as fusion tags to monitor protein localization within living cells.
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