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XCL1-2 inquiry  | Purity Not Available

Protheragen

Mouse lymphotactin (Lptn) and its human homologue (also named human SCM-1 and ATAC) belong to the C or gamma subfamily of chemokines. The C chemokines lack two (the 1st and 3rd) of the four invariant cysteine residues normally found in the CC and CXC chemokines and have an extended carboxy terminus. Mouse lymphotactin encodes a […]

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CXCL17-2 inquiry  | Purity Not Available

Protheragen

Dendritic cell and monocyte chemokine-like protein (DMC), also known as VEGF-correlated chemokine-1 (VCC-1), is a secreted molecule with a size and predicted three-dimensional folding pattern similar to that of chemokines CXCL8/IL-8 and CXCL14/BRAK. It has no predicted N-glycosylation sites, so cleavage of a 22 amino acid (aa) signal sequence likely results in a mature mouse […]

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CXCL17-1 inquiry  | Purity Not Available

Protheragen

CXCL17 also named dendritic cell and monocyte chemokine-like protein (DMC) and VEGF co-regulated chemokine 1 (VCC-1), is a small cytokine belonging to the CXC chemokine family. CXCL17 was the last chemokine ligand to be described and is the 17th member of the CXC chemokine family. Its strategic expression in mucosal tissues suggests that it is […]

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CXCL16 inquiry  | Purity Not Available

Protheragen

CXCL16 is a member of the CXC chemokine family. Mouse CXCL16 has 246 a.a. and consists of a 26 a.a. residue putative signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucin-like spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail. Mouse and human CXCL16 share […]

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CXCL15 inquiry  | Purity Not Available

Protheragen

Mouse Lungkine/CXCL15, also named WECHE, is a member of the ELR motif-containing CXC chemokines. Mouse Lungkine shares 35% aa sequence identity with human ENA-78 and 31% identity with human IL-8. CXCL15 is a novel CXC chemokine that is highly expressed in the adult mouse lung. CXCL15 has suppressive activity on proliferation and expansion of multi-potential, […]

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CXCL14-1 inquiry  | Purity Not Available

Protheragen

Chemokine (C-X-C motif) ligand 14 (CXCL14), also named BRAK, is a small cytokine belonging to the CXC chemokine family. Recombinant mouse CXCL14 contains 77 amino acid residues and it shares 97 % and 99 % a.a. sequence identity with human and rat CXCL14. CXCL14 serves as a chemoattractant for activated macrophages, immature dendritic cells and […]

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CXCL14-2 inquiry  | Purity Not Available

Protheragen

Chemokine (C-X-C motif) ligand 14 (CXCL14), also named BRAK, is a small cytokine belonging to the CXC chemokine family. Recombinant mouse CXCL14 contains 77 amino acid residues and it shares 97 % and 99 % a.a. sequence identity with human and rat CXCL14. CXCL14 serves as a chemoattractant for activated macrophages, immature dendritic cells and […]

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CXCL13-2 inquiry  | Purity Not Available

Protheragen

The homeostatic chemokine CXCL13 (also called B cell-attracting chemokine 1 [BCA-1] or B-lymphocyte chemoattractant [BLC]) is constitutively expressed in secondary lymphoid tissue and initiates lymphoid neogenesis when expressed aberrantly. Recombinant human CXCL13 is a single non-glycosylated polypeptide chain containing 87 amino acids and mature human BCA-1 shares 64% amino acid sequence similarity with the mouse […]

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CXCL13-1 inquiry  | Purity Not Available

Protheragen

The homeostatic chemokine CXCL13 (also called B cell-attracting chemokine 1 [BCA-1] or B-lymphocyte chemoattractant [BLC]) is constitutively expressed in secondary lymphoid tissue and initiates lymphoid neogenesis when expressed aberrantly. Recombinant human CXCL13 is a single non-glycosylated polypeptide chain containing 87 amino acids and mature human BCA-1 shares 64% amino acid sequence similarity with the mouse […]

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CXCL12γ inquiry  | Purity Not Available

Protheragen

Human CXCL12 is expressed as five isoforms that differ only in the C-terminal tail. The gamma isoform of CXCL12, also known as SDF-1 gamma, is a 12 kDa, heparin-binding member of the CXC (or alpha) family of chemokines ,Mature SDF-1 molecules are not glycosylated and exhibit a typical three antiparallel beta -strand chemokine-like fold. N-terminal […]

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