Protein-L, His

Protein L Recombinant, His Tag
Cat. No.
BT9961
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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

Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

Product Specs

Introduction
Recombinant Protein L, composed of 5 kappa-binding domains, exhibits exceptional binding affinity to immunoglobulin kappa light chains without interfering with the antibody's antigen-binding site. This unique characteristic allows Protein L to bind a wider variety of Ig classes and subclasses compared to other antibody-binding proteins. Its exceptional binding properties make it ideal for purifying both polyclonal and monoclonal IgG antibodies. Notably, Protein L demonstrates binding affinity to IgG from various species, including humans, mice, rats, and pigs.
Description
Recombinant Protein-L, expressed in E.Coli, is a single, non-glycosylated polypeptide chain with a 6×His tag fused at its N-terminus. This protein comprises 5 IgG-binding regions (B1-B2-B3-B4-B5) of the native Protein L, encompassing a total of 372 amino acids. While its molecular mass is 41.5kDa, it appears as a 46kDa band on SDS-PAGE. To ensure maximum specific IgG binding, the cell wall binding region, cell membrane binding region, and albumin binding region have been removed from the recombinant Protein-L.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
Protein-L is lyophilized without the addition of any other substances.
Solubility
To reconstitute the lyophilized Protein-L, it is recommended to dissolve it in sterile 18M-cm H2O at a concentration of at least 0.1mg/ml. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized Protein-L remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, Protein-L should be stored at 4°C for a period of 2-7 days. For extended storage, it is advisable to add a carrier protein such as HSA or BSA at a concentration of 0.1%. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of Protein-L is determined to be greater than 97.0% through the following analyses:
(a) Size-Exclusion High-Performance Liquid Chromatography (SEC-HPLC)
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
Source
Escherichia Coli.
Amino Acid Sequence
MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.

Product Science Overview

Structure and Expression

Recombinant Protein L, His Tag, is a genetically engineered version of the native Protein L. It is typically expressed in Escherichia coli (E. coli) and includes a polyhistidine (His) tag at the N-terminus and a single cysteine at the C-terminus . The His tag facilitates purification through immobilized metal affinity chromatography (IMAC), a common technique for isolating recombinant proteins.

The recombinant Protein L retains the immunoglobulin-binding domains of the native protein, allowing it to bind to a wide range of antibody fragments, including Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs) .

Binding Properties

Unlike other immunoglobulin-binding proteins such as Protein A and Protein G, which bind to the Fc region of antibodies, Protein L binds through the variable light (VL) domain of kappa light chains . This binding does not interfere with the antigen-binding site of the antibody, making Protein L suitable for capturing a broader range of Ig classes and subclasses, including IgG, IgM, IgA, IgE, and IgD .

Applications

Recombinant Protein L, His Tag, is widely used in various applications, including:

  • Antibody Purification: Due to its ability to bind kappa light chains, Protein L is used to purify polyclonal and monoclonal antibodies from different species, including human, mouse, rat, and pig .
  • Immunoprecipitation: Protein L can be used to isolate specific antibodies from complex mixtures, facilitating downstream analyses such as Western blotting and mass spectrometry.
  • Flow Cytometry: Protein L is employed in flow cytometry to detect and quantify antibodies and antibody fragments in various samples .
Production and Purity

Recombinant Protein L, His Tag, is produced in E. coli and purified to a high degree of purity, typically greater than 95% as determined by SDS-PAGE . The protein is lyophilized from a filtered solution and can be reconstituted in distilled water or saline for use in experiments .

Storage and Stability

For long-term storage, the lyophilized product should be kept at -20°C or lower to maintain stability. After reconstitution, the protein can be stored at -70°C under sterile conditions for up to three months .

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