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The antibody against ILVBL was raised in rabbit using the Human ILVBL as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
The antibody against ILVBL was raised in rabbit using the Human ILVBL as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
$600.00
| Cat.No | ADC-53022A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | ILVBL |
| Target Synonyms | ILVBL; AHAS; HACL2; 2-hydroxyacyl-CoA lyase 2; Acetolactate synthase-like protein; IlvB-like protein | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.1% Sodium Azide | Purification Method | Antigen affinity purified |
| Conjugate | Non-conjugated | Application | ELISA, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Human ILVBL | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | A1L0T0 |
Uniprot Id
A1L0T0
Target Species
Human
Target Name
ILVBL
Target Full Name
2-hydroxyacyl-CoA lyase 2
Target Function
Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
Target Subcellular Location
Endoplasmic reticulum membrane; Single-pass membrane protein.
Target Protein Families
TPP enzyme family
Target Tissue Specificity
Expressed in all tissues tested, with highest expression in heart, pancreas and placenta.
Target Synonyms
ILVBL; AHAS; HACL2; 2-hydroxyacyl-CoA lyase 2; Acetolactate synthase-like protein; IlvB-like protein
Target Background
The protein encoded by this gene shares similarity with several thiamine pyrophosphate-binding proteins identified in bacteria, yeast, and plants. The highest degree of similarity is found with bacterial acetolactate synthases (AHAS), which are enzymes that catalyze the first step in branched-chain amino acid biosynthesis.
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