LINGO1 Human
Leucine Rich Repeat And Ig Domain Containing 1 Human Recombinant
Cat. No.
BT20652
Source
Escherichia Coli.
Synonyms
Leucine Rich Repeat And Ig Domain Containing 1, LRRN6A, Leucine-Rich
Repeat And Immunoglobulin Domain-Containing Protein 1, Leucine-Rich Repeat
Neuronal Protein 1,
Leucine Rich Repeat Neuronal 6A, LERN1, Leucine-Rich
Repeat And Immunoglobulin-Like Domain-Containing Nogo Receptor-Interacting
Protein 1, Leucine-Rich Repeat Neuronal Protein 6A, UNQ201, LERN1, Leucine-rich
repeat and immunoglobulin-like domain-containing nogo receptor-interacting
protein 1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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 
Description
LINGO1 Human Recombinant produced in E.Coli is a single,
non-glycosylated polypeptide chain containing 133 amino acids (241-337 a.a) and
having a molecular mass of 15.1kDa.
LINGO1 is fused to a 36 amino acid His-tag at N-terminus
& purified by proprietary chromatographic techniques.
Product Specs
Introduction
Lingo1, short for Leucine Rich Repeat And Ig Domain Containing 1, is primarily found in neuronal tissue, particularly the cortex. It plays a role in suppressing axon regeneration by forming a three-part complex with NgR1 (responsible for binding) and p75 (responsible for signal transmission). This inhibitory effect is achieved by increasing RhoA-GTP activity in the presence of MOG, MAG, or Nogo-66 within the central nervous system. Additionally, LINGO-1 hinders both the maturation of oligodendrocyte precursor cells and the formation of myelin. This process also involves RhoA activation, but it seems to occur independently of p75 and NgR1.
Description
Recombinant human LINGO1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 133 amino acids (241-337 a.a). It has a molecular weight of 15.1 kDa. This protein includes a 36 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The LINGO1 protein solution is provided at a concentration of 1 mg/ml and contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer periods, store frozen at -20°C. To ensure maximum stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated cycles of freezing and thawing.
Purity
The purity of this product is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Leucine Rich Repeat And Ig Domain Containing 1, LRRN6A, Leucine-Rich
Repeat And Immunoglobulin Domain-Containing Protein 1, Leucine-Rich Repeat
Neuronal Protein 1,
Leucine Rich Repeat Neuronal 6A, LERN1, Leucine-Rich
Repeat And Immunoglobulin-Like Domain-Containing Nogo Receptor-Interacting
Protein 1, Leucine-Rich Repeat Neuronal Protein 6A, UNQ201, LERN1, Leucine-rich
repeat and immunoglobulin-like domain-containing nogo receptor-interacting
protein 1.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLKVL EISHWPYLDT MTPNCLYGLN LTSLSITHCN LTAVPYLAVR
HLVYLRFLNL SYNPISTIEG SMLHELLRLQ EIQLVGGQLA VVEPYAFRGL NYL.
Product Science Overview
Structure and Function
The LRIT1 gene encodes a protein that contains leucine-rich repeats (LRRs) and immunoglobulin (Ig)-like domains. These structural motifs are crucial for protein-protein interactions and are commonly found in proteins involved in cell adhesion, signaling, and immune responses . The LRRs are typically involved in forming a horseshoe-shaped structure that facilitates interactions with other proteins, while the Ig-like domains contribute to the protein’s stability and binding capabilities .
Biological Role
Associated Diseases
Research and Applications
Human recombinant LRIT1 is used in various research applications to study its function and role in disease. Recombinant proteins are produced through genetic engineering techniques, allowing scientists to investigate the protein’s properties and interactions in a controlled environment. This research is crucial for developing targeted therapies and understanding the molecular mechanisms underlying diseases associated with LRIT1 .
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