prospec

RGS17 Human

  • Name
  • Description
  • Pricings
  • Quantity
  • RGS17 Human
  • Regulator of G-Protein Signaling 17 Human Recombinant
  • Shipped with Ice Packs

Catalogue number

PRO-924

Synonyms

Regulator of G-protein signaling 17, RGS-17, RGSZ2, hRGS17.

Introduction

RGS17 weakens the signaling activity of G-proteins by binding to activated GTP-bound G alpha subunits and performing as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, creating inactive G-protein heterotrimers, which terminates the signal. RGS17 has a vital part in ending the signaling by mu opioid receptors and development of tolerance to opioid analgesic drugs.

Description

RGS17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-210) and having a molecular mass of 26.5 kDa.
The RGS17 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The RGS17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,1mM DTT and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

Avoid multiple freeze-thaw cycles.

Purity

Greater than 90% as determined by SDS-PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MRKRQQSQNE GTPAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGE NAGRPTHTTK MESIQVLEEC QNPTAEEVLS WSQNFDKMMK APAGRNLFRE FLRTEYSEEN LLFWLACEDL KKEQNKKVIE EKARMIYEDY ISILSPKEVS LDSRVREVIN RNLLDPNPHM YEDAQLQIYT LMHRDSFPRF LNSQIYKSFV ESTAGSSSES.

Safety Data Sheet

Usage

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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