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Recombinant Proteins
Product List
S100A8 Mouse
S100 Calcium Binding Protein A8 Mouse Recombinant
Recombinant S100A8 from mouse has been produced in an E. coli expression system. This non-glycosylated polypeptide chain consists of 109 amino acids, including a 20 amino acid His-tag at the N-terminus, resulting in a molecular weight of 12.4 kDa. Purification is achieved through proprietary chromatographic techniques, ensuring high purity of the recombinant protein.
Shipped with Ice Packs 
Cat. No.
BT743
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized by filtration.
S100A9 Human
S100 Calcium Binding Protein A9 Human Recombinant
Recombinant Human S100A9, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 122 amino acids (1-114 a.a.) with a molecular weight of 14.3 kDa. This protein is fused to an 8 amino acid His-Tag at its C-terminus and purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT831
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
S100A9 Mouse
S100 Calcium Binding Protein A9 Mouse Recombinant
Recombinant S100A9 Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 133 amino acids (1-113) with a molecular weight of 15.2 kDa. This protein is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT929
Source
Escherichia Coli.
Appearance
S100A9 is supplied as a sterile filtered solution with a yellowish tint.
S100b Human
S100 Calcium Binding Protein B Human Recombinant
S100b Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 92 amino acids (1-92 a.a.) with a molecular mass of 10.7 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1044
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution without any particulate matter.
CACYBP Human
Calcyclin Binding Protein Human Recombinant
Recombinant CACYBP Human, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 205 amino acids (1-185a.a.) with a molecular weight of 23.4 kDa. The protein includes a 20 amino acid His tag at the N-terminus and undergoes purification through standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28907
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
CALN1 Human
Calnueron-1 Human Recombinant
CALN1 Human Recombinant, incorporating a 20 amino acid His tag at the N-terminus and produced in E.Coli, is characterized as a single, non-glycosylated polypeptide chain. This chain comprises 212 amino acids (1-192 a.a.) and exhibits a molecular mass of 24kDa. The purification process of CALN1 involves the utilization of proprietary chromatographic techniques.
Shipped with Ice Packs
CAMLG Human
Calcium Modulating Ligand Human Recombinant
Recombinant human CAMLG, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 212 amino acids (1-189) with a molecular mass of 23.2kDa. It's fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29081
Source
Escherichia Coli.
Appearance
Sterile, colorless solution that has been filtered.
S100A1 Human
S100 Calcium Binding Protein A1 Human Recombinant
Recombinant human S100A1, expressed in E. coli, is a non-glycosylated polypeptide chain with a single chain. It consists of 103 amino acids, including a 10 amino acid His tag at the N-terminus, resulting in a molecular weight of 11.66 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29140
Source
Escherichia Coli.
Appearance
Lyophilized powder, white in color.
S100A1 Mouse
S100 Calcium Binding Protein A1 Mouse Recombinant
Produced in E. coli, our S100A1 is a single, non-glycosylated polypeptide chain comprising 114 amino acids (specifically, residues 1-94). It has a molecular mass of 12.6 kDa. However, the molecular weight observed on SDS-PAGE will appear higher due to the presence of a 20 amino acid His-tag fused at the N-terminus. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
S100A14 Human
S100 Calcium Binding Protein A14 Human Recombinant
Recombinant human S100A14 protein is expressed in E. coli with an N-terminal 20 amino acid His-tag. This non-glycosylated polypeptide consists of 124 amino acids (residues 1-104 of the S100A14 sequence) and has a molecular weight of 13.8 kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29614
Source
Escherichia Coli.
Appearance
Clear, colorless and sterile-filtered 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.
