Recombinant Human CD97 His-tag Protein, CF

Recombinant Human CD97 His-tag Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: CD97

CD97 is a member of the epidermal growth factor-seven transmembrane (EGF-TM7) subfamily of G-protein coupled receptors (1). Mature human CD-97 contains a large extracellular domain (ECD) followed by 7 transmembrane domains. Alternative splicing encodes 3 isoforms of the ECD with varying numbers of EGF-like repeats (4). Isoform 1, being the longest, contains 5 EGF-like domains, while isoform 2, which is described in this insert, is missing amino acids (aa) 116-208, corresponding to EGF-like domains 3 and 4. Mature isoform 2 of human CD97 shares 50% aa identity with the mouse protein. The EGF-like domains mediate binding to chondroitin sulfate and the complement regulatory protein CD55 (2, 3). CD97 may play a role inflammatory and immune responses as well as the progression of several types of cancer (3). Cells known to express CD97 include monocytes, macrophages, T cells, select B cells, dendritic cells and, potentially, vascular and visceral smooth muscle cells (5-7). CD97 is also differentially expressed on murine hematopoietic stem- and progenitor-cells (7). CD55 (decay accelerating factor), a GPI-linked cell surface molecule with short consensus repeats that regulates complement activation on cell surfaces, chondroiten sulfate and the integrin alpha 5 beta (also known as VLA-5) have been identified as cellular ligands for CD97 (7). The composition of the EGF domain region defines the ligand specificity of the different CD97 isoforms (7). The first and second EGF domains interact with CD55, whereas the fourth EGF domain binds chondroitin sulfate (7). The ligand affinity of the CD97 isoforms differs (7). While affinity for CD55 is significantly higher for the smaller isoforms, chondroitin sulfate interacts exclusively with the largest isoforms (7). Lymphocytes and erythrocytes (red blood cells) have been shown to specifically adhere to CD97-transfected COS cells. The adhesion of red blood cells to CD97 transfectants was blocked using a mAb which recognizes CD55 (8). It has also been demonstrated that CD97 is required for neutrophil migration and host defense (9).

Related Research Areas

• Acute Lymphoblastic Leukemia
• Adhesion G Protein-Coupled Receptors
• B Cell Activation
• Dendritic Cell Adhesion and Migration
• G Protein-Coupled Receptors in Immune Responses
• Monocyte Markers