Recombinant Human ACYP1 Protein (GST Tag) | PKSH030812

Recombinant Human ACYP1 Protein (GST Tag) | PKSH030812 | Gentaur US, UK & Europe Disrtribition

Synonyms: Acylphosphatase-1;ACYP1;Acylphosphatase; erythrocyte isozyme;Acylphosphatase; organ-common type isozyme;Acylphosphate phosphohydrolase 1;ACYPE

Active Protein: N/A

Activity: A DNA sequence encoding the human ACYP1 (P07311) (Ala 2-Lys 99) was fused with the GST tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human ACYP1 (P07311) (Ala 2-Lys 99) was fused with the GST tag at the N-terminus.

Fusion Tag: N-GST

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 92 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 38 kDa

Formulation: Lyophilized from sterile 20mM Tris, 0.15M NaCl, 0.5mM GSH, pH 8.0

Reconstitution: Please refer to the printed manual for detailed information.

Background: ACYP1; also known as Acylphosphatase-1; Acylphosphatase; erythrocyte isozyme; Acylphosphatase; organ-common type isozyme; Acylphosphate phosphohydrolase 1 and ACYPE; is a small cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates.ACYP1 is a protein which belongs to the acylphosphatase family and contains 1 fibrinogen C-terminal domain. Two isoenzymes have been isolated; called muscle acylphosphatase and erythrocyte acylphosphatase; on the basis of their tissue localization. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis. Recombinant human ACYP1 protein was expressed in E. coli fused with HIS-tag at N-terminus.

Research Area: Signal Transduction, Cancer, metabolism,