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Recombinant Proteins
Product List
S100A6 Murine
S100 Calcium Binding Protein A6 Mouse
Calcyclin, also known as S100A6, has been purified using HPLC, as described in Kuznicki et al. (1989) Biochem. J. 263: 951-956.
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S100A7 Human
S100 Calcium Binding Protein A7 Human Recombinant
Recombinant human S100A7, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 121 amino acids (1-101) with a molecular weight of 13.6 kDa. This protein features a 20 amino acid His-Tag fused at the N-terminus and undergoes purification using proprietary chromatographic methods.
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S100A7A Human
S100 Calcium Binding Protein A7A Human Recombinant
Recombinant Human S100A7A is produced with an N-terminal 9-amino acid His Tag fusion. This His-Tagged S100A7A Fusion Protein has a molecular weight of 12.3kDa, comprising 109 amino acid residues of the protein and an additional 9-amino acid His Tag (underlined).
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S100A8 Human
S100 Calcium Binding Protein A8 Human Recombinant
Recombinantly produced in E. coli, S100A8 Human is a non-glycosylated polypeptide chain comprising 93 amino acids (1-93 a.a.) with a molecular weight of 10.8 kDa. The protein is purified using proprietary chromatographic methods.
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Cat. No.
BT488
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterile filtered.
s100bb Bovine
s100bb Bovine homodimer
s100bb Bovine is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
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Cat. No.
BT1526
Source
Bovine brain tissue.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
s100bb Human
s100bb Human homodimer
s100bb Human produced in Human brain tissue is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
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Cat. No.
BT1587
Source
Human brain tissue.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
S100G Human
S100 Calcium Binding Protein G Human Recombinant
Recombinant Human S100G, expressed in E. coli, has a molecular weight of 10.04 kDa. It comprises 87 amino acid residues of the human S100G protein and incorporates a 9 amino acid Histidine tag at the N-terminus.
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S100G Rat
S100 Calcium Binding Protein G Rat Recombinant
S100G, also known as Calbindin-D9k or CaBP9K, is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1752
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
S100P Human
S100 Calcium Binding Protein P Human Recombinant
Recombinant Human S100P is a protein with a molecular weight of 10.4 kDa, composed of 95 amino acid residues of the human S100P protein.
Shipped with Ice Packs
Cat. No.
BT1814
Source
Escherichia Coli.
Appearance
White powder, lyophilized and filtered.
S100A6 Human
S100 Calcium Binding Protein A6 Human Recombinant
Recombinant Human S100A6, expressed in E. coli, is a non-glycosylated polypeptide chain with a 20 amino acid His tag at its N-terminus. This single-chain protein comprises 110 amino acids (including amino acids 1-90) and has a molecular weight of 12.3 kDa. Purification of S100A6 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT126
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
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.
