X-linked retinitis pigmentosa GTPase regulator (RPGR), Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

>85% (SDS-PAGE) (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of RPGR recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

This gene encodes a protein with a series of six RCC1-like domains (RLDs), characteristic of the highly conserved guanine nucleotide exchange factors. The encoded protein is found in the Golgi body and interacts with RPGRIP1. This protein localizes to the outer segment of rod photoreceptors and is essential for their viability. Mutations in this gene have been associated with X-linked retinitis pigmentosa (XLRP). Multiple alternatively spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length natures of only some have been determined.

44,827 Da

X-linked retinitis pigmentosa GTPase regulator

X-linked retinitis pigmentosa GTPase regulator

Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. May be involved in microtubule organization and regulation of transport in primary cilia. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes.

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