MGLL Human

Monoglyceride Lipase Human Recombinant

Recombinant human MGLL, with a 20 amino acid His tag attached to its N-terminus, is produced in E. coli. It exists as a single, non-glycosylated polypeptide chain comprising 333 amino acids (including the 20 amino acid His tag; the MGLL sequence spans amino acids 1-313) and has a molecular weight of 36.4 kDa. Purification of MGLL is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5869
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MGLL Human, Active

Monoglyceride Lipase Human Recombinant, Active

This product is a recombinant human MGLL protein expressed in E. coli. It is a single, non-glycosylated polypeptide chain with a His-tag on the N-terminus. The protein consists of 333 amino acids, including the 20-amino acid His-tag (amino acids 1-313 of the MGLL sequence), and has a molecular weight of 36.4 kDa. The protein is purified using proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT5946
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PLA1A Human

Phospholipase A1 Member A Human Recombinant

Recombinant human PLA1A, produced in E. coli, is a single polypeptide chain with no glycosylation. It consists of 454 amino acids (residues 26-456), resulting in a molecular weight of 49.5 kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus and is purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6010
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

LYPLA1 Mouse

Lysophospholipase I Mouse Recombinant

Produced in E. coli, LYPLA1 is a non-glycosylated polypeptide chain with a single chain. It consists of 250 amino acids (specifically, amino acids 1 to 230) and has a molecular weight of 26.8 kDa. For purification, LYPLA1 is tagged with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5643
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

LYPLA2 Human

Lysophospholipase II Human Recombinant

Recombinant human LYPLA2, fused with a 20 amino acid His tag at the N-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 251 amino acids (residues 1-231) and has a molecular weight of 26.9 kDa. LYPLA2 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5696
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

LYPLAL1 Human

Lysophospholipase Like I Human Recombinant

Recombinant human LYPLAL1, expressed in E. coli, is a single polypeptide chain with a molecular weight of 28.9 kDa. It comprises 261 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-237). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5770
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

LIPG Human, HEK

Lipase Endothelial Human Recombinant, HEK

Recombinant human LIPG, produced in HEK cells, is a single, glycosylated polypeptide chain consisting of amino acids Ser21 to Pro500 (total 490 amino acids). It has a calculated molecular mass of 55.8 kDa. This LIPG protein includes a 2 amino acid N-terminal linker, a 2 amino acid C-terminal linker, and a 6 amino acid His tag located at the C-terminus.
Shipped with Ice Packs
Cat. No.
BT5423
Source
HEK 293.
Appearance
White powder, lyophilized (freeze-dried), and filtered.

LPL Human

Lipoprotein Lipase Human Recombinant

This recombinant human LPL protein, expressed in E. coli, has a molecular weight of 51.61 kDa. It consists of 458 amino acids corresponding to the human LPL sequence, with a 10-amino acid His tag attached to the N-terminus.
Shipped with Ice Packs
Cat. No.
BT5501
Source
Escherichia Coli.

LPL Human, HEK

Lipoprotein Lipase Human Recombinant, HEK

This recombinant human LPL protein, expressed in HEK293 cells, is a 51.8 kDa protein comprising a 461 amino acid sequence of human LPL (Ala28-Gly475, with Asn substituted by Ser at position 318) fused to a 13 amino acid Flag-tag at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT5587
Source
HEK293 (Human Embryonic Kidney cell line).
Appearance
White, lyophilized powder after filtration.

CEL Mouse

Carboxyl Ester Lipase Mouse Recombinant

Recombinant Mouse CEL was expressed in Sf9 insect cells using a Baculovirus expression system. It is a single, glycosylated polypeptide chain containing 585 amino acids (21-599 aa), resulting in a molecular mass of 64.5 kDa. A 6-amino acid His-tag is fused to the C-terminus for purification purposes. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT5131
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
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.
© Copyright 2024 Thebiotek. All Rights Reserved.