Recombinant Proteins

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S100A15 Mouse

S100 Calcium Binding Protein A15 Mouse Recombinant

Recombinant Mouse S100A15 is produced in E. coli. It is a single polypeptide chain containing 132 amino acids (amino acids 1-108) with a molecular mass of 15.0 kDa. It is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29689
Source
E.coli.
Appearance
A sterile, colorless, and filtered solution.

S100A16 Human

S100 Calcium Binding Protein A16 Human Recombinant

Produced in E. coli, S100A16 is a single, non-glycosylated polypeptide chain comprising 123 amino acids (specifically, amino acids 1 through 103). It has a molecular weight of 13.9 kDa. The protein includes a 20 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29778
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

S100A10 Human

S100 Calcium Binding Protein A10 Human Recombinant

S100A10 Human Recombinant, also known as Calpactin light chain, is expressed in E. coli and has a molecular weight of 15.3kDa. It is fused to an amino-terminal hexahistidine tag.
Shipped with Ice Packs
Cat. No.
BT29257
Source
Escherichia Coli.

S100A10 Mouse

Recombinant Mouse S100 Calcium Binding Protein A10

S100A10 Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97a.a) and having a molecular mass of 13.6kDa. S100A10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29335
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

S100A11 Human

S100 Calcium Binding Protein A11 Human Recombinant

S100A11 Human Recombinant, with a molecular weight of 17kDa, is expressed in E. coli and fused to an amino-terminal hexahistidine tag.
Shipped with Ice Packs
Cat. No.
BT29382
Source
Escherichia Coli.

S100A12 Human

S100 Calcium Binding Protein A12 Human Recombinant

Recombinant Human S100A12, expressed in E. coli, is a 11.63 kDa protein comprising 101 amino acid residues of the human S100A12 protein with an N-terminal 10-amino acid His tag.
Shipped with Ice Packs
Cat. No.
BT29464
Source
Escherichia Coli.

S100A13 Human

S100 Calcium Binding Protein A13 Human Recombinant

Recombinant human S100A13, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 118 amino acids (residues 1-98). It has a molecular weight of 13.6 kDa. The S100A13 protein includes a 20 amino acid His-Tag fused at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29537
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
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.
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