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ASNS rabbit pAb

CAT: 0855-ES18228-01Size: 50 µLDry Ice: NoHazardous: No
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CAT#:0855-ES18228-01Size:50 µL
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Background
The protein encoded by this gene is involved in the synthesis of asparagine. This gene complements a mutation in the temperature-sensitive hamster mutant ts11, which blocks progression through the G1 phase of the cell cycle at nonpermissive temperature. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, May 2010]
Description
The protein encoded by this gene is involved in the synthesis of asparagine. This gene complements a mutation in the temperature-sensitive hamster mutant ts11, which blocks progression through the G1 phase of the cell cycle at nonpermissive temperature. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, May 2010],
Product Name Alternative
Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Cell cycle control protein TS11) (Glutamine-dependent asparagine synthetase)
UniProt
P08243
Swiss Prot
P08243
Reactivity
Human; Mouse; Rat
Immunogen
Synthesized peptide derived from human ASNS AA range: 390-440
Target
ASNS
Clonality
Polyclonal
Source
Rabbit
Applications
WB
Concentration
1 mg/ml
Dilution
WB 1:500-2000
Buffer
-20°C/1 year
Molecular Weight
60kD
Storage Conditions
-20°C/1 year
Observed Molecular Weight
60kD
Fragment
IgG
Subcellular Location
Cytosol
Other Product Names
Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Cell cycle control protein TS11) (Glutamine-dependent asparagine synthetase)
Gene ID (Human)
440

UniProtKB · P08243

Asparagine synthetase [glutamine-hydrolyzing]

ASNS_HUMAN · Homo sapiens

View on UniProt ↗
Primary accession
P08243
Review status
UniProtKB reviewed (Swiss-Prot)
Gene
ASNS
Protein existence
1: Evidence at protein level
Organism
Homo sapiens (Human)
Taxonomy ID
9606
Alternative names
—
EC number
3.5.1.2, 6.3.5.4
Processing
—
Secondary accessions
A4D1I8, B4DXZ1, B7ZAA9, D6W5R3, E9PCI3, E9PCX6, P08184, Q15666, Q549T9, Q96HD0
Protein keywords

Technical term

3D-structureProteomics identificationReference proteome

PTM

AcetylationPhosphoprotein

Coding sequence diversity

Alternative splicing

Biological process

Amino-acid biosynthesisAsparagine biosynthesis

Ligand

ATP-bindingNucleotide-binding

Disease

Disease variantIntellectual disability

Domain

Glutamine amidotransferase

Molecular function

HydrolaseLigase

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