S100A8 Human, His-Myc

S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant
Cat. No.
BT672
Source
Escherichia Coli.
Synonyms
S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.
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

S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. 
S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.

Product Specs

Introduction
S100A8, a member of the S100 protein family, possesses two EF-hand calcium-binding motifs and plays a crucial role in various cellular processes. Primarily found in the cytoplasm and/or nucleus, S100A8 regulates cell cycle progression and differentiation. This protein exhibits cytokine-like activity and inhibits casein kinase. Notably, alterations in S100A8 expression are linked to cystic fibrosis. With its calcium-binding properties, S100A8 demonstrates antimicrobial activity against both bacteria and fungi, contributing significantly to host defense against pathogenic invasion. It upregulates the transcription of NF-κB-controlled genes and plays a critical role in the development of endotoxic shock following bacterial lipopolysaccharide exposure. Moreover, S100A8 promotes tubulin polymerization, facilitating phagocyte migration and granulocyte infiltration at wound sites, thus acting as a pro-inflammatory mediator in acute and chronic inflammation. Its role in upregulating IL-8 release and cell-surface ICAM1 expression further underscores its importance in inflammatory responses.
Description
Recombinantly produced in E. coli, the human S100A8 protein is a single, non-glycosylated polypeptide chain comprising 127 amino acids (residues 1-93), with a molecular weight of 14.5 kDa. The protein features a 24 amino acid His-tag at the N-terminus and a 10 amino acid Myc-tag at the C-terminus.
Physical Appearance
The appearance of this sterile filtered solution is colorless.
Formulation
The S100A8 solution is provided at a concentration of 1 mg/ml and contains 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.1 M NaCl.
Stability
For short-term storage (up to 4 weeks), the entire vial should be stored at 4°C. For extended storage, freeze the solution at -20°C. To ensure optimal stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
SDS-PAGE analysis indicates a purity greater than 90.0%.
Synonyms
S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.

Product Science Overview

Introduction

S100 Calcium Binding Protein A8 (S100A8), also known as calgranulin A, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium and zinc ions, which is crucial for their biological functions. S100A8 plays a significant role in the regulation of inflammatory processes and immune responses. It is predominantly found as part of the heterodimeric complex calprotectin (S100A8/A9), which has a wide range of intra- and extracellular functions .

Structure and Function

S100A8 is a small protein with a molecular mass of approximately 14.5 kDa. The recombinant form of this protein, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 127 amino acids. It includes a 24 amino acid His-tag at the N-terminus and a 10 amino acid Myc-tag at the C-terminus . These tags facilitate the purification and detection of the protein in various experimental setups.

The primary function of S100A8 is to regulate the inflammatory response. It can induce neutrophil chemotaxis and adhesion, which are critical steps in the immune response to infection and injury. Additionally, S100A8 is involved in the regulation of cell proliferation, differentiation, and apoptosis. It also plays a role in tumorigenesis and development .

Preparation Methods

The recombinant S100A8 protein is typically produced using bacterial expression systems, such as E. coli. The gene encoding S100A8 is cloned into an expression vector that includes sequences for the His and Myc tags. The vector is then introduced into E. coli cells, which are cultured under conditions that promote the expression of the recombinant protein. After expression, the protein is purified using affinity chromatography techniques that exploit the His-tag for selective binding to a nickel or cobalt resin .

Chemical Reactions and Analysis

S100A8 undergoes several post-translational modifications that are essential for its function. These modifications include phosphorylation, which can affect the protein’s ability to bind calcium and interact with other molecules. The protein’s interaction with calcium and zinc ions is critical for its role in the inflammatory response. Analytical techniques such as mass spectrometry and X-ray crystallography are used to study these interactions and the protein’s structure .

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