SUCLA2 Antibody
Product Specifications
Background
Succinyl-CoA synthetase (SCS) is a mitochondrial matrix enzyme that acts as a heterodimer, being composed of an invariant alpha subunit and a substrate-specific beta subunit. The protein encoded by this gene is an ATP-specific SCS beta subunit that dimerizes with the SCS alpha subunit to form SCS-A, an essential component of the tricarboxylic acid cycle. SCS-A hydrolyzes ATP to convert succinate to succinyl-CoA. Defects in this gene are a cause of myopathic mitochondrial DNA depletion syndrome. A pseudogene of this gene has been found on chromosome 6.
NCBI Gene ID
8803
Swiss Prot
Q9P2R7
Host
Rabbit
Reactivity
Human, Mouse, Rat
Immunogen
Recombinant fusion protein containing a sequence corresponding to amino acids 1-180 of human SUCLA2 (NP_003841.1) .
Clonality
Polyclonal
Conjugation
Unconjugated
Type
Primary Antibodies
Field of Research
Neuroscience, Signal Transduction
Purification
Affinity purification
Positive Control
293T
Concentration
Batch dependent
Buffer
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Modification
None
Shipping Conditions
Blue Ice
Storage Conditions
Store at -20˚ C. Avoid freeze / thaw cycles.
Calculated Molecular Weight
Observed: 50kDa
Fragment
IgG
Applications Notes
WB: 1:500 - 1:1000
Symbol
SUCLA2
Positive Control 2
SW480
Positive Control 3
HeLa
Positive Control 4
Mouse heart
Positive Control 5
Mouse liver
Positive Control 6
Mouse brain
NCBI Official Name
Succinate-CoA ligase ADP-forming beta subunit
NCBI Organism
Homo sapiens
Other Product Names
A-BETA, A-SCS, MTDPS5, SCS-betaA, succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial, ATP-specific succinyl-CoA synthetase subunit beta, ATP-specific succinyl-CoA synthetase, beta subunit, mitochondrial succinyl-CoA ligase [ADP-forming] subunit beta, renal carcinoma antigen NY-REN-39, succinate-CoA ligase beta subunit, succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial, succinyl-CoA synthetase beta-A chain
Tested Applications
WB
Physical Properties
Liquid
Curated Selection
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