Growth Factors
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Recombinant Proteins
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Monoclonal Antibodies
Cytokines
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Enzymes
Product List
CEL Mouse
Carboxyl Ester Lipase Mouse Recombinant
CEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (21-599 aa) and having a molecular mass of 64.5kDa.
CEL is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT5131
Source
Sf9,
Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
CES2E Mouse
Carboxylesterase 2E Mouse Recombinant
CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.
CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5203
Source
Sf9,
Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
Lipase A
Lipase-A Recombinant
Recombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT5281
Source
Escherichia Coli.
Appearance
Sterile Filtered lyophilized powder.
LIPG Human
Lipase Endothelial Human Recombinant
LIPG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (21-340) and having a molecular mass of 38kDa.
LIPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
LIPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
LIPG Human, HEK
Lipase Endothelial Human Recombinant, HEK
LIPG Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Pro500) containing a total of 490 amino acids, having a calculated molecular mass of 55.8kDa. LIPG is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.
Shipped with Ice Packs
Cat. No.
BT5423
Source
HEK 293.
Appearance
Filtered White lyophilized (freeze-dried) powder.
LPL Human
Lipoprotein Lipase Human Recombinant
The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.
Shipped with Ice Packs
LPL Human, HEK
Lipoprotein Lipase Human Recombinant, HEK
The Recombinant Human LPL produced in HEK293 cell line has a molecular mass of 51.8kDa containing 461 amino acid residues of the human LPL (Ala28-Gly475, variant Asn > Ser318) and fused to a 13 a.a. Flag-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT5587
Source
HEK293 (Human Embryonic Kidney cell line).
Appearance
Filtered white lyophilized powder.
LYPLA1 Mouse
Lysophospholipase I Mouse Recombinant
LYPLA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 26.8kDa.
LYPLA1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
LYPLA1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
LYPLA2 Human
Lysophospholipase II Human Recombinant
LYPLA2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5696
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
LYPLAL1 Human
Lysophospholipase Like I Human Recombinant
LYPLAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.9kDa.
LYPLAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
LYPLAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Introduction
Definition and Classification
Lipases are a group of enzymes that catalyze the hydrolysis of fats (lipids) into glycerol and free fatty acids. They are classified based on their source and substrate specificity:
- Pancreatic Lipase: Found in the pancreas, it plays a crucial role in the digestion of dietary fats.
- Hepatic Lipase: Located in the liver, it is involved in the metabolism of lipoproteins.
- Hormone-Sensitive Lipase: Present in adipose tissue, it is regulated by hormonal signals and is essential for mobilizing stored fats.
- Lipoprotein Lipase: Found in the endothelial cells of capillaries, it hydrolyzes triglycerides in lipoproteins.
Biological Properties
Key Biological Properties:
- Catalytic Activity: Lipases exhibit high specificity for the ester bonds in triglycerides.
- Stability: They are stable under a wide range of pH and temperature conditions.
Expression Patterns:
- Pancreatic Lipase: Expressed predominantly in the pancreas.
- Hepatic Lipase: Expressed in the liver.
- Hormone-Sensitive Lipase: Expressed in adipose tissue.
- Lipoprotein Lipase: Expressed in endothelial cells of capillaries.
Tissue Distribution:
- Pancreatic Lipase: Found in the pancreas and small intestine.
- Hepatic Lipase: Found in the liver and blood plasma.
- Hormone-Sensitive Lipase: Found in adipose tissue.
- Lipoprotein Lipase: Found in capillary endothelial cells.
Biological Functions
Primary Biological Functions:
- Fat Digestion: Pancreatic lipase breaks down dietary fats into absorbable units.
- Lipoprotein Metabolism: Hepatic and lipoprotein lipases are involved in the metabolism of lipoproteins, which transport fats in the blood.
- Fat Mobilization: Hormone-sensitive lipase mobilizes stored fats for energy production.
Role in Immune Responses:
- Pathogen Recognition: Lipases can recognize and hydrolyze lipid components of pathogen membranes, aiding in immune defense.
Modes of Action
Mechanisms with Other Molecules and Cells:
- Binding to Substrates: Lipases bind to triglycerides and hydrolyze the ester bonds.
- Interaction with Co-factors: Some lipases require co-factors such as bile salts for optimal activity.
Binding Partners:
- Colipase: Pancreatic lipase requires colipase for binding to lipid-water interfaces.
- Apolipoproteins: Lipoprotein lipase interacts with apolipoproteins on lipoprotein particles.
Downstream Signaling Cascades:
- Hormone-Sensitive Lipase: Activated by cyclic AMP (cAMP) signaling in response to hormonal signals like adrenaline.
Regulatory Mechanisms
Regulatory Mechanisms:
- Transcriptional Regulation: Gene expression of lipases is regulated by transcription factors such as PPARs (Peroxisome Proliferator-Activated Receptors).
- Post-Translational Modifications: Lipases can be activated or inhibited by phosphorylation, glycosylation, and other modifications.
Applications
Biomedical Research:
- Metabolic Studies: Lipases are used to study lipid metabolism and related disorders.
Diagnostic Tools:
- Enzyme Assays: Lipase activity assays are used to diagnose pancreatic diseases.
Therapeutic Strategies:
- Enzyme Replacement Therapy: Lipase supplements are used to treat conditions like exocrine pancreatic insufficiency.
Role in the Life Cycle
Role Throughout the Life Cycle:
- Development: Lipases are essential for the digestion and absorption of dietary fats, crucial for growth and development.
- Aging: Changes in lipase activity can affect lipid metabolism and contribute to age-related diseases.
- Disease: Dysregulation of lipase activity is associated with metabolic disorders such as obesity, diabetes, and cardiovascular diseases.
