SPA, His

Staphylococcal Protein-A Recombinant, His Tag
Cat. No.
BT10225
Source
Escherichia Coli.
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by 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

SPA Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with 6×His tag at C-terminus. SPA is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 306 amino acids and having a molecular mass of 34.7kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.

Product Specs

Introduction
Protein A, a cell wall component found in certain Staphylococcus aureus strains, is crucial for antibody purification. Our recombinant Protein A, engineered with five IgG-binding regions, mimics native Protein A's functionality. It efficiently purifies polyclonal and monoclonal IgG antibodies, binding specifically to human IgG1, IgG2, IgG4; mouse IgG2a, IgG2b, IgG3; and rat IgG2c. Additionally, it binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
Description
Our SPA Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain. Featuring a 6xHis tag at the C-terminus, it encompasses five IgG-binding domains (E-D-A-B-C) in series. With 306 amino acids and a molecular weight of 34.7 kDa, it contains minimal to no carbohydrates. The cell wall, cell membrane, and albumin binding regions have been removed to maximize specific IgG binding.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The lyophilized SPA protein is supplied without any additional additives.
Solubility
For reconstitution, dissolve the lyophilized SPA in sterile 18 MΩ-cm H2O to a concentration of at least 0.1 mg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized SPA remains stable at room temperature for up to 3 weeks. However, for long-term storage, it should be stored desiccated at temperatures below -18°C. After reconstitution, store SPA at 4°C for 2-7 days. For extended storage, add a carrier protein (0.1% HSA or BSA) and store below -18°C. Avoid repeated freeze-thaw cycles.
Purity
The purity is greater than 97.0% as determined by: - High-Performance Liquid Chromatography (HPLC) analysis - Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Source
Escherichia Coli.
Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHH.

Product Science Overview

Introduction

Staphylococcal Protein-A (SpA) is a cell wall component produced by several strains of Staphylococcus aureus. It is widely used in biochemical research and biotechnology due to its ability to bind immunoglobulins, particularly IgG. The recombinant form of Protein-A, often tagged with a His (histidine) tag, is engineered for enhanced purification and detection.

Structure and Function

Protein-A consists of five immunoglobulin-binding domains (E, D, A, B, and C) aligned in series. These domains enable Protein-A to bind to the Fc region of IgG antibodies, as well as the Fab region, which is responsible for antigen recognition . This binding capability makes Protein-A a valuable tool for purifying antibodies from complex mixtures.

The recombinant form of Protein-A is produced in Escherichia coli and is designed to retain the functional properties of the native protein. The His tag, typically a sequence of six histidine residues, is added to the N- or C-terminus of the protein. This tag facilitates affinity purification using nickel or cobalt-based resins and allows for easy detection using anti-His tag antibodies .

Applications

Recombinant Protein-A with a His tag is used in various applications, including:

  • Antibody Purification: Due to its strong affinity for IgG, Protein-A is commonly used to purify polyclonal and monoclonal antibodies from serum, cell culture supernatants, and other sources .
  • Immunoprecipitation: Protein-A can be used to isolate antigen-antibody complexes, aiding in the study of protein-protein interactions and other immunological assays.
  • Diagnostic Assays: Protein-A is employed in diagnostic assays to capture and detect antibodies, enhancing the sensitivity and specificity of these tests .
Advantages of Recombinant Protein-A

The recombinant form of Protein-A offers several advantages over the native protein:

  • High Purity: Recombinant Protein-A is produced with high purity, often exceeding 99%, and has low endotoxin levels, making it suitable for sensitive applications .
  • Consistency: The recombinant production process ensures batch-to-batch consistency, which is crucial for reproducible results in research and industrial applications.
  • Versatility: The addition of the His tag allows for versatile purification and detection methods, streamlining experimental workflows .

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