Abhydrolase Domain Containing 12B (ABHD12B) Antibody

52€ (10 µg)
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935106861
info@markelab.com
name
Abhydrolase Domain Containing 12B (ABHD12B) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx119588
tested applications
IHC
Description
ABHD12B Antibody is a Rabbit Polyclonal antibody against ABHD12B.
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | Abhydrolase Domain Containing 12B (ABHD12B) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified from rabbit antiserum by affinity chromatography using epitope-specific immunogen. |
Size 1 | 10 µg |
Size 2 | 100 µg |
Size 3 | 200 µg |
Size 4 | 300 µg |
Size 5 | 1 mg |
Form | Liquid |
Tested Applications | IHC |
Buffer | PBS (without Mg<sup>2+</sup> and Ca<sup>2+</sup>), pH 7.4, 150 mM NaCl, 0.02% sodium azide, 50% glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q7Z5M8 |
Alias | BEM46L3,C14orf29,c14_5314 |
Background | Antibody anti-ABHD12B |
Status | RUO |
Note | Concentration: 1 mg/ml - |
Descripción
ABHD12B (Abhydrolase Domain Containing 12B) is a member of the ABHD family, which consists of proteins with an alpha/beta hydrolase fold, typically involved in lipid metabolism. ABHD12B is thought to function as a lipase or hydrolase, potentially playing a role in the regulation of lipid signaling pathways. It is expressed in various tissues, with notable expression in the brain and immune-related cells, suggesting roles in neurological and immunological processes. Although its precise enzymatic activity and substrates remain to be fully elucidated, ABHD12B is structurally similar to ABHD12, which is implicated in phospholipid metabolism. Mutations or dysregulation may influence lipid homeostasis.
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