Human Hormone-sensitive Lipase/HSL Alexa Fluor® 750-conjugated Antibody
R&D Systems, part of Bio-Techne | Catalog # AF7104S
Conjugate
Catalog #
Key Product Details
Species Reactivity
Human
Applications
Western Blot
Label
Alexa Fluor 750 (Excitation = 749 nm, Emission = 775 nm)
Antibody Source
Polyclonal Sheep IgG
Product Specifications
Immunogen
E. coli-derived recombinant human Hormone-sensitive Lipase/HSL
Met302-Leu425
Accession # Q05469
Met302-Leu425
Accession # Q05469
Specificity
Detects human Hormone-sensitive Lipase/HSL in direct ELISAs and Western blots.
Clonality
Polyclonal
Host
Sheep
Isotype
IgG
Applications
Application
Recommended Usage
Western Blot
Optimal dilution of this antibody should be experimentally determined.
Formulation, Preparation, and Storage
Purification
Antigen Affinity-purified
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
Background: Hormone-sensitive Lipase/HSL
LIPE (also known as hormone sensitive lipase/HSL) is a 88-90 kDa member of the GDXG lipolytic enzyme family of molecules. It is expressed in multiple cell types, including skeletal muscle, adrenal gland and adipocytes, and is regulated by a series of phosphorylations. Catecholamines activate the enzyme via PKA through the phosphorylation of Ser853, Ser855, and Ser951, while insulin depresses its activity via PDE3B. LIPE acts on triglycerides to release free fatty acids, and serves as a retinyl ester hydrolase. Human LIPE is 1076 amino acids (aa) in length, and contains one HSL domain (aa 302-616). This restricted 116 kDa isoform is found in testis (spermatids). There are additional isoform variants. One is 88-90 kDa in size in SDS-Page and possesses an alternative start site to the long form at Met302. This is considered the standard and most common LIPE isoform. A second is approximately 93 kDa in size and contains a 39 aa substitution for aa 1-294. A third isoform is 80 kDa in size and shows a 76 aa deletion in the center of the molecule, reducing its enzymatic activity. It is suggested that LIPE may act as both a monomer and homodimer. Over aa 302-425, human HSL shares 92-93% aa identity with both mouse and rat LIPE.
Alternate Names
Hormonesensitive Lipase, HSL, LHS, LIPE
Gene Symbol
LIPE
UniProt
Additional Hormone-sensitive Lipase/HSL Products
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
For research use only
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