Human CXCL5 Recombinant Protein (RPES1386)
- SKU:
- RPES1386
- Product Type:
- Recombinant Protein
- Species:
- Human
- Research Area:
- Chemokines
Frequently bought together:
Description
system_update_altDatasheet
Human CXCL5 Recombinant Protein
C-X-C Motif Chemokine 5 (CXCL5) is a member of the Intercrine Alpha (Chemokine CXC) family. CXCL5 is cleaved into two chains: ENA-78 (8-78) and ENA-78 (9-78). In vitro, ENA-78(8-78) and ENA-78 (9-78) show a threefold higher chemotactic activity for neutrophil granulocytes. CXCL5 is a secreted protein that acts primarily through CXCR2 interactions. CXCL5 upregulation is responsible for the development of increased blood flow, tumour growth, and metastasis in a variety of cancers. Human CXCL5 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
Product Name: | Human CXCL5 Recombinant Protein (RPES1386) |
Product Code: | RPES1386 |
Size: | 10µg |
Species: | Human |
Expressed Host: | E.coli |
Synonyms: | C-X-C Motif Chemokine 5, ENA-78 (1-78), Epithelial-Derived Neutrophil-Activating Protein 78, Neutrophil-Activating Peptide ENA-78, Small-Inducible Cytokine B5, ENA-78 (8-78), ENA-78 (9-78), CXCL5, ENA78, SCYB5 |
Accession: | P42830 |
Sequence: | Leu44-Asn114 |
Fusion tag: | |
Endotoxin: | <1.0 EU per µg as determined by the LAL method. |
Protein Construction: | Recombinant Human C-X-C Motif Chemokine 5 is produced by our E.coli expression system and the target gene encoding Leu44-Asn114 is expressed. |
Purity: | > 95 % as determined by reducing SDS-PAGE. |
Mol Mass: | 8.0 kDa |
AP Mol Mass: | 12 kDa |
Formulation: | Lyophilized from a 0.2 µm filtered solution of 20mM PB, pH 6.0. |
Shipping: | This product is provided as lyophilized powder which is shipped with ice packs. |
Stability and Storage: | Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months. |