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Recombinant Proteins
Product List
S100A6 Human
S100 Calcium Binding Protein A6 Human Recombinant
S100A6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT126
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
S100A6 Mouse
S100 Calcium Binding Protein A6 Mouse Recombinant
S100A6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89 a.a) and having a molecular mass of 12.2kDa.
S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
S100A6 Murine
S100 Calcium Binding Protein A6 Mouse
S100A6 also called Calcyclin has been purified by HPLC (see Kuznicki et al. (1989) Biochem. J. 263: 951-956).
Shipped with Ice Packs
Cat. No.
BT278
Source
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
S100A7 Human
S100 Calcium Binding Protein A7 Human Recombinant
S100A7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.6 kDa.
The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
S100A7A Human
S100 Calcium Binding Protein A7A Human Recombinant
The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).
Shipped with Ice Packs
S100A8 Human
S100 Calcium Binding Protein A8 Human Recombinant
S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT488
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.
S100A8 Human, His
S100 Calcium Binding Protein A8 Human Recombinant, His Tag
The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.
Shipped with Ice Packs
S100A8 Human, His-Myc
S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant
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.
Shipped with Ice Packs
Cat. No.
BT672
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
S100A8 Mouse
S100 Calcium Binding Protein A8 Mouse Recombinant
S100A8 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.4kDa.
S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
S100A9 Human
S100 Calcium Binding Protein A9 Human Recombinant
S100A9 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-114 a.a.) and having a molecular mass of 14.3kDa. S100A9 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Shipped with Ice Packs
Cat. No.
BT831
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
Introduction
Definition and Classification
Calcium binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca²⁺) through specific domains known as EF-hand motifs. These proteins play crucial roles in various cellular processes by regulating calcium signaling pathways. CaBPs can be classified into several families based on their structure and function, including calmodulins, troponins, S100 proteins, and annexins.
Biological Properties
Key Biological Properties:
- Calcium Binding: CaBPs have high affinity for calcium ions, which allows them to act as calcium sensors and buffers.
- Conformational Changes: Binding of calcium induces conformational changes in CaBPs, enabling them to interact with target proteins.
- Versatility: CaBPs are involved in a wide range of cellular functions due to their ability to bind calcium and interact with various proteins.
Expression Patterns:
- CaBPs are ubiquitously expressed in many tissues, but their expression levels can vary significantly depending on the tissue type and physiological conditions.
Tissue Distribution:
- Calmodulins: Found in almost all eukaryotic cells.
- Troponins: Predominantly present in cardiac and skeletal muscles.
- S100 Proteins: Expressed in the brain, heart, and other tissues.
- Annexins: Widely distributed in various tissues, including the lungs, liver, and kidneys.
Biological Functions
Primary Biological Functions:
- Signal Transduction: CaBPs play a key role in translating calcium signals into cellular responses.
- Muscle Contraction: Troponins regulate muscle contraction by controlling the interaction between actin and myosin.
- Cell Cycle Regulation: Calmodulins are involved in cell cycle progression and division.
- Neurotransmitter Release: S100 proteins modulate neurotransmitter release in the nervous system.
Role in Immune Responses:
- CaBPs are involved in the activation and regulation of immune cells, such as T cells and macrophages, by modulating calcium-dependent signaling pathways.
Pathogen Recognition:
- Certain CaBPs, like S100 proteins, can recognize and bind to pathogen-associated molecular patterns (PAMPs), playing a role in the innate immune response.
Modes of Action
Mechanisms with Other Molecules and Cells:
- CaBPs interact with a variety of target proteins, including enzymes, ion channels, and structural proteins, to modulate their activity.
Binding Partners:
- Calmodulins: Bind to and regulate kinases, phosphatases, and other signaling proteins.
- Troponins: Interact with actin and myosin in muscle fibers.
- S100 Proteins: Bind to receptors on immune cells and other target proteins.
- Annexins: Interact with phospholipids and membrane proteins.
Downstream Signaling Cascades:
- CaBPs initiate and regulate various signaling pathways, such as the calcium/calmodulin-dependent protein kinase (CaMK) pathway, which is involved in processes like memory formation and muscle contraction.
Regulatory Mechanisms
Regulatory Mechanisms that Control Expression and Activity:
- Transcriptional Regulation: The expression of CaBPs is regulated by transcription factors that respond to cellular signals and environmental cues.
- Post-Translational Modifications: CaBPs can undergo modifications such as phosphorylation, acetylation, and ubiquitination, which can alter their activity, stability, and interactions with other proteins.
Applications
Biomedical Research:
- CaBPs are used as markers to study calcium signaling pathways and their role in various diseases, including cancer and neurodegenerative disorders.
Diagnostic Tools:
- Elevated levels of certain CaBPs, such as troponins, are used as biomarkers for diagnosing myocardial infarction and other cardiac conditions.
Therapeutic Strategies:
- Targeting CaBPs and their interactions with other proteins is being explored as a potential therapeutic approach for treating diseases like cancer, heart disease, and inflammatory disorders.
Role in the Life Cycle
Role Throughout the Life Cycle:
- Development: CaBPs are essential for proper embryonic development, particularly in the formation of the nervous system and muscles.
- Aging: Changes in the expression and function of CaBPs are associated with aging and age-related diseases, such as Alzheimer’s disease and sarcopenia.
- Disease: Dysregulation of CaBPs is implicated in various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.
