Recombinant Human ATP citrate lyase / ATPCL Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0287
Recombinant Human ATP citrate lyase / ATPCL Protein (His Tag)

Recombinant Human ATP citrate lyase / ATPCL Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0287
Catalog No.: BLPSN-0287

Product Overview

Tag His
Host Species Human
Accession P53396
Synonym ACL, ATPCL, CLATP
Background ATP citrate lyase, also known as Acly or Acl, is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is composed of two polymer chains which are polypeptides in human. ATP citrate lyase is responsible for catalyzing the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, along with the hydrolysis of ATP. A definitive role for ATP citrate lyase in tumorigenesis has emerged from ATP citrate lyase RNAi and chemical inhibitor studies, showing that ATP citrate lyase inhibition limits tumor cell proliferation and survival and induces differentiation in vitro. In vivo, it reduces tumor growth leading to a cytostatic effect and induces differentiation.
Description A DNA sequence encoding the human ACLY (P53396) (Met 1-Met 1101) was expressed, with a His tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Met 1-Met 1101
Molecular Weight The recombinant human ACLY consists of 1120 a.a. and has a calculated molecular mass of 123 kDa. It migrates as an approximately 110 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% gly.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Recently viewed