Technical Data
H7021-80
Hormone Sensitive Lipase (HSL)
Description:
Lipase, hormone-sensitive also known as LIPE is an enzyme that, in humans, is encoded by the LIPE gene. LIPE is an intracellular neutral lipase that is capable of hydrolyzing a variety of esters.[2] The enzyme has a long and a short form. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production. The short form is expressed in adipose tissue, among others, where it hydrolyzes stored triglycerides to free fatty acids.

LIPE functions to hydrolyze the first fatty acid from a triacylglycerol molecule, freeing a fatty acid and diglyceride. It is also known as triglyceride lipase, while the enzyme that cleaves the second fatty acid in the triglyceride is known as diglyceride lipase, and the third enzyme that cleaves the final fatty acid is called monoglyceride lipase. Only the initial enzyme is affected by hormones, hence its hormone-sensitive lipase name. The diglyceride and monoglyceride enzymes are tens to hundreds of times faster, hence HSL is the rate-limiting step in cleaving fatty acids from the triglyceride molecule.

LIPE is activated when the body needs to mobilize energy stores, and so responds positively to catecholamines, ACTH, and negatively to insulin. Previously, glucagon was thought to activate LIPE, however the removal of insulin's inhibitory effects ("cutting the brakes") is the source of activation. The lipolytic effect of glucagon in adipose tissue is minimal in humans. LIPE may be activated by two mechanisms. In the first, phosphorylated perilipin A causes it to move to the surface of the lipid droplet, where it may begin hydrolyzing the lipid droplet. Also, it may be activated by a cAMP-dependent protein kinase (PKA). This pathway is significantly less effective than the first, which is necessary to lipid mobilization in response to cyclic AMP, which itself is provided by beta adrenergic stimulation of the glucagon receptor.

Applications:
Suitable for use in Western Blot and ELISA. Other applications have not been tested.

Recommended Dilution:
ELISA: 1:1000-1:5000
Western Blot: 1:1000-1:5000
Optimal dilutions to be determined by the researcher.

Recommended Secondary Antibodies:
I1906 IgY, Chicken Pab Rb x Ch
I1906-10 IgY, Chicken (HRP) Rb x Ch
I1906-12 IgY, Chicken (FITC) Rb x Ch
I1906-14 IgY, Chicken (AP) Rb x Ch

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabIgYPurified
SizeStorageShippingSourceHost
500ug4C (-20C Glycerol)Blue IceHumanChicken
Concentration:
~1mg/ml
Immunogen:
HSL mixed peptides (NSQEEAEAKDEV, SGRKPQKTTSPT and FGEHYKRNETGL)
Purity:
Purified immunoglobulin
Form
Supplied as a liquid in PBS, pH 7.4, 0.02% sodium azide.
Specificity:
Binds to a band at about 83kD (HSL) in various fat cell lysates from mouse and rat, and an additional band at about 40kD (unknown). Species Crossreactivity: human, rat and mouse.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
General References:
1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C (June 1993). "Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium". Proc. Natl. Acad. Sci. U.S.A. 90 (11): 4897901. doi:10.1073/pnas.90.11.4897. PMID 8506334.
2. Kraemer FB, Shen WJ (October 2002). "Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis". J. Lipid Res. 43 (10): 158594. doi:10.1194/jlr.R200009-JLR200. PMID 12364542.
3. "Entrez Gene: LIPE lipase, hormone-sensitive".
4. Crabtree B, Newsholme EA (December 1972). "The activities of lipases and carnitine palmitoyltransferase in muscles from vertebrates and invertebrates". Biochem. J. 130 (3): 697705. PMID 4664927.
5. de Meijer J., (1998-05-01). Hormone sensitive lipase: structure, function and regulation. demeijer.com. Retrieved 2009-02-04.
6. Cox, Michael; Nelson, David R.; Lehninger, Albert L (2005). Lehninger principles of biochemistry. San Francisco: W.H. Freeman. ISBN 0-7167-4339-6.