Recombinant Proteins

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S100A4 Human

S100 Calcium-Binding Protein A4 Human Recombinant

Recombinant human S100A4, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 121 amino acids (residues 1-101) with a molecular weight of 13.8 kDa. This protein is engineered with a 20 amino acid His-Tag fused to its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT30025
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

S100A4 Mouse

S100 Calcium Binding Protein A4 Mouse Recombinant

Recombinant S100A4 Mouse protein, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 13.9kDa. It consists of 121 amino acids, including a 20 amino acid His-tag at the N-terminus, covering amino acids 1-101 of the S100A4 sequence. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30095
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

S100A5 Human

S100 Calcium Binding Protein A5 Human Recombinant

Recombinant human S100A5, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a 20 amino acid His tag attached to its N-terminus. It consists of 112 amino acids, including the 92 amino acids of S100A5 (residues 1-92), resulting in a molecular weight of 12.9 kDa. The purification process for S100A5 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30140
Source
Escherichia Coli.
Appearance
The product is a clear and colorless solution that has been sterilized by filtration.

S100A5 Mouse

S100 Calcium Binding Protein A5 Mouse Recombinant

Recombinant S100A5 Mouse protein, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 13.4 kDa. It consists of 117 amino acids (residues 1-93) and includes a 24 amino acid His-Tag at the N-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT30189
Source
Escherichia Coli.
Appearance
S100A9 is provided as a clear, sterile-filtered solution.

CAB39 Human

Calcium Binding Protein 39 Human Recombinant

CAB39 Recombinant Human protein is produced in E. coli. It is a single polypeptide chain that does not contain glycosylation. It contains 361 amino acids (specifically amino acids 1 through 341) and has a molecular mass of 42 kDa. The CAB39 is fused to a 20 amino acid His-Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28693
Source
Escherichia Coli.
Appearance
A clear and colorless solution that is sterile and has been filtered.

CAB39L Human

Calcium Binding Protein 39 Like Human Recombinant

This version of CAB39L is made in bacteria and is a single chain of protein building blocks. It is not modified with sugars and contains 360 building blocks, including a tag for purification. It has a size of 41.5 kDa.
Shipped with Ice Packs
Cat. No.
BT28754
Source
Escherichia Coli.
Appearance
A clear and colorless liquid free from bacteria.

CABP7 Human

Calcium Binding Protein 7 Human Recombinant

Recombinantly produced in E. coli, CABP7 is a single, non-glycosylated polypeptide chain consisting of 208 amino acids (specifically, amino acids 1 to 188). This protein has a molecular weight of 23.7 kDa. For purification and detection purposes, it has been engineered with a 20 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28811
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

S100A2 Human

S100 Calcium Binding Protein A2 Human Recombinant

Recombinant Human S100A2 is produced in E. coli. It is a single, non-glycosylated polypeptide chain fused with a 20 amino acid His tag at its N-terminus. This protein contains 117 amino acids (including the His tag, residues 1-97 represent the S100A2 sequence) and has a molecular weight of 13.1 kDa. Purification is achieved using proprietary chromatographic techniques, resulting in a highly pure protein.
Shipped with Ice Packs
Cat. No.
BT29840
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

S100A3 Human

S100 Calcium Binding Protein A3 Human Recombinant

Recombinantly produced in E. coli, S100A3 Human is a non-glycosylated polypeptide chain consisting of 121 amino acids (1-101), with a molecular weight of 13.9 kDa. The protein is purified using proprietary chromatographic techniques and features a 20 amino acid His-Tag fused at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT29893
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

S100A3 Mouse

S100 Calcium Binding Protein A3 Mouse Recombinant

Recombinant S100A3 Mouse is produced in E. coli and is a single, non-glycosylated polypeptide chain composed of 125 amino acids (specifically, amino acids 1-101). The protein has a molecular mass of 14.3 kDa. It is engineered with a 24 amino acid His-tag at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29964
Source
Escherichia Coli.
Appearance
S100A3 is provided as 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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