Recombinant Rat Agrin
| Code | Size | Price |
|---|
| LEI-A344-100ug | 100 ug | £694.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Rat
Regulatory Status: RUO
Shipping:
Ambient
Storage:
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Further Information
Format:
This recombinant protein was 0.2 um filtered and lyophilized from modified Dulbecco?s phosphate buffered saline (1X PBS) pH 7.2 ? 7.3 with no calcium, magnesium, or preservatives.
Formulation:
This recombinant protein was 0.2 um filtered and lyophilized from modified Dulbecco?s phosphate buffered saline (1X PBS) pH 7.2 ? 7.3 with no calcium, magnesium, or preservatives.
Long Description:
Agrin is a heparin sulfate proteoglycan secreted by the nerve, whose best characterized role is in the development of the neuromuscular junction during embryogenesis. Agrin is involved in the aggregation of acetylcholine receptors (AChR) during synaptogenesis (1). This activity has been shown to be mediated via a receptor complex that includes a receptor-like tyrosine kinase specific to the skeletal muscle termed muscle-specific kinase (MuSK) (2). Agrin also binds several other proteins on the surface of muscle, including dystroglycan and laminin, which are additional binding steps that are required to stabilize the neuromuscular junction. Agrin contains a number of structural domains, including regions of homology to laminin, Kazal protease inhibitors, and EGF repeats. In addition, there are several isoforms of Agrin which are produced by alternative splicing at sites in the C-terminal half. These isoforms have been shown to have significant differences in AChR clustering activities (3).
NCBI Gene:
25592
Purity:
>90% by SDS-PAGE and analyzed by silver stain.
Target:
Agrin
References
1. McMahan, UJ. et al. (1987) Prog. Brain Res. 71:391
2. Yancopoulos, GD. et al. (1996) Cell 85:513
3. McMahan, UJ. et al. (1992) Current Op. Cell Biol. 4:869
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