LOX Human

Lysyl Oxidase Human Recombinant
Cat. No.
BT18955
Source
E.coli.
Synonyms
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock
Quick Inquiry

Description

LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.
LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Lysyl Oxidase, also known as LOX, is an extracellular copper enzyme responsible for initiating the crosslinking of collagens and elastin. It catalyzes the oxidative deamination of specific lysine and hydroxylysine residues in collagens and lysine residues in elastin, leading to the formation of crosslinks in these extracellular matrix proteins. LOX plays a crucial role in tumor suppression and its deficiency can cause autosomal recessive cutis laxa type I (CL type I). There are two known transcript variants of LOX that encode distinct isoforms.
Description
Recombinant Human LOX, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 272 amino acids (169-417 a.a.). This protein, with a molecular weight of 31.4 kDa, is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
LOX protein is supplied in a solution at a concentration of 1mg/ml, formulated in 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store the protein at 4°C. For long-term storage, it is recommended to freeze the protein at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advised for extended storage. Avoid repeated freeze-thaw cycles to maintain protein stability.
Purity
The purity of LOX is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.

Product Science Overview

Introduction

Lysyl oxidase (LOX) is a copper-dependent amine oxidase that plays a crucial role in the biogenesis of connective tissue. It catalyzes the oxidative deamination of lysine residues in collagen and elastin precursors, leading to the formation of aldehydes. These aldehydes subsequently react with other lysine residues, resulting in the cross-linking of collagen and elastin, which is essential for the stabilization of collagen fibrils and the integrity and elasticity of mature elastin .

Structure and Function

Lysyl oxidase is synthesized as a precursor molecule, which undergoes proteolytic processing to become active. The enzyme contains a copper-binding site and a lysine tyrosylquinone (LTQ) cofactor, which are essential for its catalytic activity. The active enzyme is secreted into the extracellular matrix, where it performs its function of cross-linking collagen and elastin .

Biological Significance

The cross-linking of collagen and elastin by lysyl oxidase is vital for the tensile strength and structural integrity of various tissues, including skin, bones, and blood vessels. Defects in lysyl oxidase activity can lead to connective tissue disorders, such as cutis laxa and certain forms of Ehlers-Danlos syndrome .

Recombinant Lysyl Oxidase

Recombinant human lysyl oxidase is produced using various expression systems, including bacterial, yeast, and mammalian cells. The recombinant enzyme retains the biochemical properties of the native enzyme and is used in research to study its role in connective tissue biogenesis and its potential therapeutic applications .

Applications in Research and Medicine

Recombinant lysyl oxidase is used in various research applications, including:

  • Studying connective tissue disorders: Understanding the role of lysyl oxidase in diseases such as cutis laxa and Ehlers-Danlos syndrome.
  • Cancer research: Investigating the role of lysyl oxidase in tumor progression and metastasis, as it has been shown to contribute to the remodeling of the extracellular matrix in the tumor microenvironment .
  • Tissue engineering: Exploring the use of lysyl oxidase in the development of biomaterials for tissue repair and regeneration.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.