Matrix Protein, Recombinant, Rabies Virus, aa1-202, His-Tag (M)

Referencia 374157-20ug

embalaje : 20ug

Marca : US Biological

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374157 Matrix Protein, Recombinant, Rabies Virus, aa1-202, His-Tag (M)

Swiss Prot
P15200
Grade
Purified
Shipping Temp
Blue Ice
Storage Temp
-20°C

Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons.

Source:
Recombinant protein corresponding to aa1-202 from rabies virus M, fused to His-Tag at N-terminal, expressed in Yeast.

Molecular Weight:
~25.2kD

Amino Acid Sequence:
MNVLRKIVKKCRDEDTQKPSPVSAPPDDDDLWLPPPEYVPLKELTSKKNMRNFCVNGDVKACSPNGYSFRILRHILRSFNEIYSGNHRMIGLVKVVVGLALSGAPVPEGMNWVYKLRRTLIFQWADSRGPLEGEELEYSQEITWDDDTEFVGLQIRVSARQCHIQGRIWCINTNSRACQLWSDMSLQTQRSEEDKDSSLLLE

Storage and Stability:
Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Applications
Source: Recombinant, Yeast|Purity: ≥90% (SDS-PAGE)|Form: Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
Purity
≥90% (SDS-PAGE)
References
1. Sequence of the 3386 3' nucleotides of the genome of the AVO1 strain rabies virus structural similarities in the protein regions involved in transcription. Poch O., Tordo N., Keith G.Biochimie 70:1019-1029(1988).