Recombinant Human Kirrel1/NEPH1 His-tag Protein, CF Summary
Gln17-Leu493, with a C-terminal 6-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 µg/lane of Recombinant Human Kirrel 1/NEPH1 His-tag (Catalog # 10165-K1) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing major bands at 65-75 kDa and 50-60 kDa, respectively.
Kirrel1, also called NEPH1, is a 90-110 kDa type I transmembrane glycoprotein that belongs to the NEPH family of the immunoglobulin superfamily (1-4). The 757 amino acid (aa) human Kirrel1 contains a 16 aa signal sequence, a 483 aa extracellular domain (ECD) with five C2-type Ig-like domains, a 21 aa transmembrane sequence and a 237 aa cytoplasmic domain. The ECD also contains a site for FGF/FGF R interaction, and an RGD site that may allow integrin-mediated cell attachment. Five IgG-like repeats characterize the extracellular domain (5). The interaction of these five IgG-like motifs with the eight IgG-like motifs in Nephrin form a zipper-like meshwork around the glomerular capillaries in podocytes (5, 6). This interaction is what forms the structural basis of the slit diaphragm regulating macromolecule movement from the blood (5). Human Kirrel1 shares 98% aa identity with mouse and rat homologs, respectively, within the ECD. Kirrel1 expression has been mainly studied in the kidney glomerular slit diaphragm, but its expression with nephrin or other family members has also been reported in central nervous system neurons, pancreas and placenta (3, 4, 7-9). Kirrel1 forms cis hetero-oligomers with Nephrin, which brings together signaling molecules that direct actin polymerization (3, 4, 10). This interaction is essential for barrier function in the slit diaphragm, and mice deleted for Kirrel1 die perinatally due to proteinuria and failure to thrive (2, 3).
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