Recombinant Human CXCL16

2-1-1-green-tea-extract-1

Recombinant Human CXCL16

Cat. No.: PRODRP00030
Size:
Quantity:
Pricey: Inquiry

Product Details

Source: Escherichia coli
Molecular Weight: Approximately 10 kDa, a single non-glycosylated polypeptide chain containing 89 amino acids.
AA Sequence: Asn49-Pro137; Accession # NP_071342
Purity: > 97% by SDS-PAGE analyses.
Biological Activity: Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with mouse CXCR6. The ED50 for this effect is 2.5-12 ng/mL.
Physical Appearance: Sterile filtered white lyophilized (freeze-dried) powder.
Formulation: Lyophilized from 0.2 µm filtered concentrated solution in PBS.
Endotoxin: Less than 1.0 EU/µg of rHuCXCL16 as determined by LAL method.
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile PBS to a concentration of 0.1 mg/mL. Further dilutions should be made in appropriately buffered solutions.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.
Background: CXC chemokine ligand 16 (CXCL16) is a type I membrane protein featuring a CXC chemokine domain without the ELR motif in its extracellular segment. Alongside Fractalkine (CX3CL1), CXCL16 comprises the sole two transmembrane chemokines in its superfamily. The human CXCL16 gene encodes a precursor protein of 273 amino acids (aa), including a presumed signal peptide, a CXC chemokine domain, a mucin-like spacer region, a transmembrane segment, and a cytoplasmic domain harboring potential tyrosine phosphorylation and SH2 protein-binding sites. Mouse and human CXCL16 share a 70% aa sequence similarity within their chemokine domains and a 49% overall aa sequence identity.

Get in Touch
Contact Info
Copyright © Alta Stomatology. All Rights Reserved.
Top