MLEC Human

Malectin Human Recombinant
Cat. No.
BT24629
Source
Escherichia Coli.
Synonyms
Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% 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.

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Description

MLEC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (29-269) and having a molecular mass of 29.1kDa.
MLEC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
MLEC, a member of the malectin family, resides on the endoplasmic reticulum membrane. This carbohydrate-binding protein exhibits a strong affinity for Glc2-N-glycan and plays a crucial role in the early stages of protein N-glycosylation.
Description
Recombinant human MLEC, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 264 amino acids (residues 29-269) with a molecular weight of 29.1 kDa. This protein is fused to a 23-amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The MLEC solution is formulated in 20 mM Tris-HCl buffer (pH 8.0), 0.15 M NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing cycles should be avoided.
Purity
The purity of this protein is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSPGLGVAG VAGAAGAGLP ESVIWAVNAG GEAHVDVHGI HFRKDPLEGR VGRASDYGMK LPILRSNPED QILYQTERYN EETFGYEVPI KEEGDYVLVL KFAEVYFAQS QQKVFDVRLN GHVVVKDLDI FDRVGHSTAH DEIIPMSIRK GKLSVQGEVS TFTGKLYIEF VKGYYDNPKV CALYIMAGTV DDVPKLQPHP GLEKKEEEEE EEEYDEGSNL KKQTNKNRVQ SGPRTPNPYA SDNS

Product Science Overview

Structure and Expression

Recombinant Human Malectin is a fragment protein that ranges from amino acids 29 to 269. It is expressed in Escherichia coli and has a purity greater than 95%, making it suitable for applications such as SDS-PAGE and mass spectrometry (MS) . The protein is tagged with a His tag at the N-terminus to facilitate purification and detection.

Biological Function

Malectin is involved in the quality control of glycoproteins. It binds to specific glycan structures and plays a role in the early steps of protein N-glycosylation. This process is essential for the proper folding and function of glycoproteins, which are critical for various cellular functions .

Role in Viral Infections

Recent studies have highlighted the role of Malectin in viral infections, particularly in the replication and biogenesis of viral proteins. For instance, Malectin has been shown to promote the replication of coronaviruses by interacting with viral nonstructural proteins and host factors. This interaction helps stabilize the association with the Oligosaccharyltransferase (OST) complex, which is crucial for viral glycoprotein production . This makes Malectin a potential target for antiviral therapies, especially for coronaviruses like SARS-CoV-2 .

Applications

Recombinant Human Malectin is widely used in research to study glycoprotein quality control and protein N-glycosylation. It is also used in high-throughput screening assays and other biochemical applications . The protein’s high purity and specific binding properties make it a valuable tool for researchers studying glycoprotein interactions and functions.

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