Recombinant Human CD157 protein (rFc Tag)

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• Recombinant Human CD157 protein (rFc Tag) (Eg2067)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg2067

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Validation Data Gallery

• 

  Purity of Recombinant Human CD157 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human CD157 protein Arg33-Ala293 (Accession# Q10588-1) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 683
• Accession: Q10588-1
• PredictedSize: 56.0 kDa
• SDS-PAGE: 58-70 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

CD157, also known as bone marrow stromal cell antigen 1 (BST-1), or ADP-ribosyl cyclase 2, is a glycosyl phosphotidylinositol-anchored protein that stimulates pre-B-cell growth and has adenosine diphosphate (ADP)-ribosyl cyclase and cyclic ADP-ribose (cADPR) hydrolase activity. The two enzymatic activities are responsible for the synthesis and hydrolysis of cADPR, a novel second messenger of calcium release from intracellular calcium stores .

References:

1. Sumie Yamamoto-Katayama, et al. (2002) J Mol Biol. Feb 22;316(3):711-23.
2. Y Okuyama, et al. (1996) Biochem Biophys Res Commun. Nov 21;228(3):838-45.
3. A Sato, et al. (1999) Eur J Biochem. Sep;264(2):439-45.