Datasheet

Biological Description

Specificity	SCD1 Antibody [H13N22] detects endogenous levels of total SCD1 protein.
Background	Stearoyl-CoA desaturase-1 (SCD1) is a membrane-bound enzyme predominantly localized in the endoplasmic reticulum. SCD1 is a key member of the lipid metabolism enzyme family, catalyzing the biosynthesis of monounsaturated fatty acids (MUFAs) from saturated fatty acyl-CoAs by introducing a cis double bond at the Δ9 position between the ninth and tenth carbon atoms. It is composed of four transmembrane domains that form a characteristic “mushroom-shaped” fold, with eight histidine residues at the catalytic site coordinating a diiron center crucial for enzymatic function. SCD1 converts stearoyl-CoA and palmitoyl-CoA into oleoyl-CoA and palmitoleoyl-CoA, respectively. These MUFAs are major constituents of membrane phospholipids, triglycerides, and cholesterol esters, thus regulating membrane fluidity and lipid signaling. SCD1 is central to fatty acid metabolism, energy homeostasis, and lipid biosynthesis, interacting with enzymes such as acetyl-CoA carboxylase and fatty acid synthase to maintain lipid balance. SCD1 modulates insulin sensitivity, as knockout models exhibit improved insulin signaling and resistance to obesity and hepatic steatosis, emphasizing its importance in metabolic syndrome and related diseases. SCD1 is also implicated in cancer progression by supporting the lipid metabolism required for tumor growth, making it a promising therapeutic target. Its activity depends on an electron transfer chain from NAD(P)H through cytochrome b5 reductase and cytochrome b5 to the diiron center, ensuring accurate double bond formation and substrate specificity.

Specificity

SCD1 Antibody [H13N22] detects endogenous levels of total SCD1 protein.

Background

Stearoyl-CoA desaturase-1 (SCD1) is a membrane-bound enzyme predominantly localized in the endoplasmic reticulum. SCD1 is a key member of the lipid metabolism enzyme family, catalyzing the biosynthesis of monounsaturated fatty acids (MUFAs) from saturated fatty acyl-CoAs by introducing a cis double bond at the Δ9 position between the ninth and tenth carbon atoms. It is composed of four transmembrane domains that form a characteristic “mushroom-shaped” fold, with eight histidine residues at the catalytic site coordinating a diiron center crucial for enzymatic function. SCD1 converts stearoyl-CoA and palmitoyl-CoA into oleoyl-CoA and palmitoleoyl-CoA, respectively. These MUFAs are major constituents of membrane phospholipids, triglycerides, and cholesterol esters, thus regulating membrane fluidity and lipid signaling. SCD1 is central to fatty acid metabolism, energy homeostasis, and lipid biosynthesis, interacting with enzymes such as acetyl-CoA carboxylase and fatty acid synthase to maintain lipid balance. SCD1 modulates insulin sensitivity, as knockout models exhibit improved insulin signaling and resistance to obesity and hepatic steatosis, emphasizing its importance in metabolic syndrome and related diseases. SCD1 is also implicated in cancer progression by supporting the lipid metabolism required for tumor growth, making it a promising therapeutic target. Its activity depends on an electron transfer chain from NAD(P)H through cytochrome b5 reductase and cytochrome b5 to the diiron center, ensuring accurate double bond formation and substrate specificity.

Usage Information

Application

WB, IP, IHC, IF, FCM

Dilution

WB	IP	IHC	IF	FCM
1:1000	1:30	1:2000	1:100	1:500

Reactivity

Mouse, Rat, Human

Source

Rabbit Monoclonal Antibody

MW

42 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/19066317/
https://pubmed.ncbi.nlm.nih.gov/32470559/

SCD1 Antibody [H13N22]

Biological Description

Usage Information

References

Application Data