Recombinant Proteins

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S100A1 Human

S100 Calcium Binding Protein A1 Human Recombinant

S100A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 103 amino acids which include a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 11.66 kDa.
S100A1 Human Recombinant is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29140
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder.

S100A1 Mouse

S100 Calcium Binding Protein A1 Mouse Recombinant

S100A1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-94 a.a) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).
S100A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29203
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

S100A10 Human

S100 Calcium Binding Protein A10 Human Recombinant

S100A10 Human Recombinant also called Calpactin light chain is expressed in E. coli having a molecular weight of 15.3kDa fused to an amino terminal hexahistidine tag.
Shipped with Ice Packs
Cat. No.
BT29257
Source
Escherichia Coli.
Appearance

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 is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.
Shipped with Ice Packs
Cat. No.
BT29382
Source
Escherichia Coli.
Appearance

S100A12 Human

S100 Calcium Binding Protein A12 Human Recombinant

The Recombinant Human S100A12 produced in E.coli has a molecular mass of 11.63kDa containing 101 amino acid residues of the human S100A12 and fused to a 10 a.a. His tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT29464
Source
Escherichia Coli.
Appearance

S100A13 Human

S100 Calcium Binding Protein A13 Human Recombinant

S100A13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98) and having a molecular mass of 13.6 kDa.
The S100A13 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29537
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

S100A14 Human

S100 Calcium Binding Protein A14 Human Recombinant

S100A14 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 124 amino acids (1-104 a.a.) and having a molecular mass of 13.8kDa. The S100A14 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29614
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

S100A15 Mouse

S100 Calcium Binding Protein A15 Mouse Recombinant

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

S100A16 Human

S100 Calcium Binding Protein A16 Human Recombinant

S100A16 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-103 a.a.) and having a molecular mass of 13.9kDa.
S100A16 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29778
Source
Escherichia Coli.
Appearance
Sterile filtered colorless 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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