Key Product Details
Leu29-Lys1114 (Gln1113Arg), with an N-terminal 9-His tag
N-terminal Sequence Analysis
Predicted Molecular Mass
When 4 x 104 cells/well are added to rhNidogen-1 coated plates (30 µg/mL with 100 µL/well), approximately 40-75% will adhere after one hour at 37 °C.
Optimal dilutions should be determined by each laboratory for each application.
Formulation, Preparation and Storage
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
Reconstitute at 100 μg/mL in sterile 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.
Nidogen-1 (also entactin) is a 150 kDa, secreted, monomeric glycoprotein that serves as a major linking component of basement membranes (1 - 4). It is synthesized as a 1247 amino acid (aa) precursor with a 28 aa signal sequence and a 1219 aa mature protein. The molecule is modular in structure with five distinct regions. There are three globular domains (G1-3) separated by a mucin region and an extended rod-shaped segment (5 - 7). The N-terminal globular domain (G1) is 200 aa in length and seemingly unrelated to any known motif (8). The mucin region is nearly 160 aa in length and presumably O-glycosylated (2, 8). G2 and G3 are both approximately 300 aa in length. G2 is described as a Nidogen ( beta-barrel) domain, while C-terminal G3 assumes a beta-propeller configuration (1). The 250 aa rod-shaped segment has multiple EGF-like motifs and two thyroglobulin type 1 domains. Functionally, G1 is reported to bind type IV collagen (2, 7). The mucin region contains a short peptide that ligates alpha3 beta1 integrins (9, 10). G2 interacts with perlecan, and an RGD motif in the rod-shaped segment serves as a binding site for alphav beta3 integrins (9, 10). Finally, G3 is associated with laminin binding (2, 7). As a full-length molecule, the multiple extracellular matrix-binding sites of Nidogen-1 are well positioned to serve as anchor sites for basement membrane molecules. Nidogen-1 also undergoes proteolytic processing by at least two MMPs, MMP7 and MMP19 (10, 11). While this destroys the integrity of Nidogen-associated matrices, it also generates peptide fragments that are capable of inducing neutrophil chemotaxis and phagocytosis (10). Nidogen-2 is related to Nidogen-1 (≈ 50% aa identity) and shares many of the same adhesive properties as Nidogen-1 (12). Both bind perlecan plus collagens I and IV. Nidogen-2, however, does not bind fibulin-1 or 2, and shows only modest interaction with laminin. Thus, although coexpressed, Nidogen-2 serves as only a partial substitute for Nidogen-1 (2, 12). Human Nidogen-1 is 85% aa identical to both mouse and rat Nidogen-1, and 88% aa identical to canine Nidogen-1.
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- Miosge, N. et al. (2001) Histochem. J. 33:523.
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- Gresham, H.D. et al. (1996) J. Biol. Chem. 271:30587.
- Dong, L-J. et al. (1995) J. Biol. Chem. 270:15383.
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- Kohfeldt, K. et al. (1998) J. Mol. Biol. 282:99.
Entrez Gene IDs
Product Specific Notices for Recombinant Human Nidogen-1/Entactin Protein, CF
For research use only