Name :
Recombinant Human NAA10/ARD1 Protein (His & GST Tag)
Biological Activity :
Background :
ARD1 is a member of the 2-kDa ARF protein family. It is a multifunctional protein. ARD1 has an 18-kDa ADP-ribosylation factor (ARF) domain at the C-terminus (amino acids 43-574), and a 46-kDa N-terminal domain (amino acids 1-42). The C-terminal region of ARD1 may be involved in the formation of both ARD1-ARD1 and ARD1-NAT1 complexes. ARD1 and NAT1 genes are required for the expression of an N-terminal protein acetyltransferase. This activity is required for full repression of the silent mating-type locus HML, for sporulation, and for entry into G. Recombinant ARD1 (amino acids 1-574) or its RING finger domain (amino acids 1-11) produced polyubiquitylated proteins when incubated in vitro with a mammalian E1, an E2 enzyme, ATP, and ubiquitin.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
P41227
NCBI Gene ID :
Synonyms :
Synonyms :
N(alpha)-acetyltransferase 10, NatA catalytic subunit
Amino Acid Sequence :
Molecular Weight :
The recombinant human ARD1A/GST chimera consists of 472 amino acids and has a calculated molecular mass of 54 kDa. The recombinant protein migrates as an approximately 49 kDa band in SDS-PAGE under reducing conditions.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the human ARD1A (P41227) (Met1-Ser235) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Buffer Solution :
Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% glycerolPlease contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
ARD1 Protein, Human; ARD1A Protein, Human; ARD1P Protein, Human; DXS707 Protein, Human; MCOPS1 Protein, Human; NAA10 Protein, Human; NATD Protein, Human; OGDNS Protein, Human; TE2 Protein, Human NAA10/ARD1 背景信息 ARD1 is a member of the 2-kDa ARF protein family. It is a multifunctional protein. ARD1 has an 18-kDa ADP-ribosylation factor (ARF) domain at the C-terminus (amino acids 43-574), and a 46-kDa N-terminal domain (amino acids 1-42). The C-terminal region of ARD1 may be involved in the formation of both ARD1-ARD1 and ARD1-NAT1 complexes. ARD1 and NAT1 genes are required for the expression of an N-terminal protein acetyltransferase. This activity is required for full repression of the silent mating-type locus HML, for sporulation, and for entry into G. Recombinant ARD1 (amino acids 1-574) or its RING finger domain (amino acids 1-11) produced polyubiquitylated proteins when incubated in vitro with a mammalian E1, an E2 enzyme, ATP, and ubiquitin.
References & Citations :
Tribioli C., et al.,(1994), Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae. Hum. Mol. Genet. 3:1061-1068.Arnesen T., et al., (2005), Identification and characterization of the human ARD1-NATH protein acetyltransferase complex.Biochem. J. 386:433-443.Ross M.T., et al.,(2005), The DNA sequence of the human X chromosome.Nature 434:325-337.
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