Escherichia Coli.
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Sterile Filtered White lyophilized (freeze-dried) powder.
reater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.
Lymphotactin is purified by proprietary chromatographic techniques.
Lymphotactin, also known as XCL1, is a small cytokine classified as an XC chemokine. Highly expressed in the spleen, thymus, intestine, and peripheral blood leukocytes, it plays a crucial role in the immune response. XCL1 is produced by activated CD8+ T cells in the thymus and peripheral blood. Its primary function is to attract T cells to sites of inflammation. In humans, XCL1 shares a close relationship with XCL2, both genes residing at the same location on chromosome 1. The chemotactic activity of XCL1 is mediated through its binding to a specific chemokine receptor, XCR1.
Recombinant Mouse Lymphotactin (XCL1), produced in E. coli, is available as a non-glycosylated polypeptide chain composed of 93 amino acids. With a molecular weight of approximately 10.1 kDa, it is purified using proprietary chromatographic techniques.
Sterile Filtered White lyophilized (freeze-dried) powder.
The product is lyophilized from a 0.2 µm filtered concentrated solution prepared in phosphate-buffered saline (PBS) at pH 7.4.
To reconstitute the lyophilized Lymphotactin, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. Further dilutions can be prepared in other aqueous solutions as needed.
Lyophilized XCL1 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated at a temperature below -18°C for long-term preservation. Once reconstituted, Lymphotactin should be stored at 4°C and used within 2-7 days. For extended storage, it is advisable to keep it at -18°C. Avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of the protein is determined using the following methods, ensuring a purity greater than 97.0%:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
The biological activity of the protein, represented by ED50 (effective dose 50%), is determined through a chemotaxis bioassay employing human XCR1-transfected murine BaF3 cells. The ED50 value is less than 100 ng/ml, corresponding to a specific activity exceeding 1.0 × 104 IU/mg.
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Escherichia Coli.
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.
Lymphotactin, also known as XCL1, is a chemokine belonging to the C or gamma subfamily. This subfamily is characterized by the absence of two of the four invariant cysteine residues typically found in CC and CXC chemokines, and an extended carboxy terminus . Lymphotactin plays a crucial role in the immune system, particularly in the chemotaxis of lymphocytes and natural killer (NK) cells.
The gene encoding mouse lymphotactin is located on chromosome 1, similar to its human counterpart . The mouse lymphotactin protein is a precursor consisting of 114 amino acid residues, including a 21 amino acid signal peptide . This signal peptide is cleaved to produce the mature protein, which is involved in immune responses.
Lymphotactin is primarily expressed in activated mouse pro-T cells and class I MHC-restricted T cells . It has been shown to have chemotactic activity for lymphocytes, NK cells, and mouse splenocytes . The chemotactic properties of lymphotactin are mediated through its interaction with the XCR1 receptor, which is expressed on the surface of target cells .
Recombinant mouse lymphotactin is produced using E. coli expression systems. The recombinant protein is typically purified to a high degree of purity (>97%) and is free from endotoxins (<0.01 EU per 1 μg of protein) . The recombinant protein is used in various research applications, including studies on immune cell migration and function.
Recombinant mouse lymphotactin is widely used in immunological research to study the mechanisms of chemotaxis and the role of chemokines in immune responses. It is also used to investigate the interactions between lymphotactin and its receptor XCR1, as well as the downstream signaling pathways activated by this interaction .