Recombinant Proteins

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CLEC10A Human

C-Type Lectin Domain Family 10, Member A Human Recombinant

Recombinant human CLEC10A protein was expressed in Sf9 insect cells. It is a single, glycosylated polypeptide chain containing 241 amino acids (corresponding to amino acid residues 61-292 of the full-length protein). The recombinant protein has a molecular mass of 27.3 kDa, determined by its amino acid sequence. On SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 28-40 kDa. The CLEC10A protein contains a 9 amino acid His-tag at the C-terminus to facilitate purification. The protein was purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21486
Source
Sf9, Insect cells.
Appearance
Clear, colorless, and sterile-filtered solution.

CLEC1B Human

C-type Lectin Domain Family 1, Member B Human Recombinant

Recombinant human CLEC1B, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 23.1 kDa. It consists of 198 amino acids (residues 55-229) and includes a 23 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22094
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.

CLEC1B Human, Sf9

C-type Lectin Domain Family 1, Member B, Human Recombinant, Sf9

This product is a recombinant CLEC1B protein produced in Sf9 insect cells. It's a single, non-glycosylated polypeptide chain containing 184 amino acids (residues 55-229) with a molecular weight of 21.8 kDa. However, it appears larger (28-57 kDa) on SDS-PAGE due to its structure. The protein has a 6-amino acid His-tag at its C-terminus to facilitate purification, which is done through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22187
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.

CLEC2B Human

C-type Lectin Domain Family 2, Member B Human Recombinant

Recombinant human CLEC2B protein was produced in E. coli and purified to a single, non-glycosylated polypeptide chain. This protein consists of 147 amino acids (residues 26-149) and has a molecular weight of 16.9 kDa. For purification and detection purposes, a 23 amino acid His-tag is fused to the N-terminus.
Shipped with Ice Packs
Cat. No.
BT22257
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

CLEC2B Human, Sf9

C-type Lectin Domain Family 2, Member B Human Recombinant, Sf9

CLEC2B, a glycosylated polypeptide chain, is produced in Sf9 Baculovirus cells. This recombinant protein consists of 366 amino acids (26-149a.a.) with a molecular mass of 41.7kDa. However, the molecular size on SDS-PAGE may appear between 40-57kDa. The protein is expressed with a 242 amino acid hIgG-His tag at the C-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22327
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

CLEC2D Human

C-type Lectin Domain Family 2, Member D Human Recombinant

Recombinant human CLEC2D, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 155 amino acids (60-191 a.a.). It has a molecular weight of 17.7 kDa. The CLEC2D protein is fused to a 23 amino acid His tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22416
Source

Escherichia Coli.

Appearance
A clear, colorless solution that has been sterilized by filtration.

CLEC7A Human

C-Type Lectin Domain Family 7, Member A Human Recombinant

Recombinant human CLEC7A, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It consists of 183 amino acids (spanning from residues 71 to 244), resulting in a molecular weight of 21 kDa. This CLEC7A protein has a 9 amino acid His-tag fused at its C-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22853
Source

Sf9, Baculovirus cells.

Appearance
A clear solution that has been sterilized by filtration.

CLEC4E Human

C-type Lectin Domain Family 4, Member E Human Recombinant

Recombinant human CLEC4E protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 200 amino acids (41-219) and has a molecular mass of 22.9 kDa. The protein is fused to a 21 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22488
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.

CLEC4M Human

C-type Lectin Domain Family 4, Member M Human Recombinant

This product consists of the extracellular domain of human CLEC4M, spanning amino acids 72 to 399, fused to a C-terminal 239 amino acid hIgG-His-Tag. This recombinant protein is expressed in Sf9 insect cells using a baculovirus expression system. The result is a glycosylated polypeptide with a molecular weight of 64.8 kDa. Following expression, the protein undergoes purification using proprietary chromatographic methods to ensure high purity.

Shipped with Ice Packs
Cat. No.
BT22559
Source

Sf9, Baculovirus cells.

Appearance

The purified CLEC4M protein solution appears colorless and is sterile-filtered.

CLEC5A Human

C-Type Lectin Domain Family 5, Member A Human Recombinant

Recombinant human CLEC5A, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 184 amino acids (residues 28-188), resulting in a molecular weight of 20.8 kDa. The protein is purified using proprietary chromatographic techniques and is fused to a 23 amino acid His-tag at its N-terminus.
Shipped with Ice Packs
Cat. No.
BT22673
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
Definition and Classification

A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. The “C-type” designation is derived from their requirement for calcium for binding. Proteins that contain C-type lectin domains have a diverse range of functions, including cell-cell adhesion, immune response to pathogens, and apoptosis . C-type lectins are classified into several subgroups based on the order of the various protein domains in each protein. Drickamer et al. initially classified C-type lectins into seven subgroups, which was later expanded to include additional groups .

Biological Properties

C-type lectins are expressed by numerous cells in the body, including hepatocytes, activated macrophages, dendritic cells, bone marrow, and epithelial cells in the intestines and lungs . They are often complex, multidomain proteins with a single protein module for sugar binding, termed the carbohydrate recognition domain (CRD). The expression of C-type lectins can be induced by factors such as interferon-γ, interleukin-4, and interleukin-6 during infection . Additionally, several types of cancer cells express elevated levels of lectin mRNA .

Biological Functions

C-type lectins play crucial roles in the immune system, including pathogen recognition and the activation of immune responses. They are involved in cell-cell adhesion, immune response to pathogens, and apoptosis . In the innate immune system, interactions between lectins and carbohydrates are essential for activating the complement cascade and phagocytosis of potential pathogens . C-type lectins also play roles in cell development, cell signaling, and glycoprotein quality control .

Modes of Action

C-type lectins interact with other molecules and cells through their carbohydrate recognition domains (CRDs). These domains bind to specific sugar ligands in a calcium-dependent manner . The binding of C-type lectins to their ligands can trigger downstream signaling cascades that lead to various cellular responses, including the activation of immune cells and the production of cytokines . Some C-type lectins can also act as pattern recognition receptors (PRRs), binding to ligands derived from fungi, bacteria, or viruses .

Regulatory Mechanisms

The expression and activity of C-type lectins are regulated by various mechanisms, including transcriptional regulation and post-translational modifications. Cytokines such as interleukin-10, interleukin-4, interleukin-13, and interferon-γ can differentially regulate the expression of C-type lectins . Post-translational modifications, such as oligomerization, can enhance the binding affinity of lectins for multivalent or clustered ligands on pathogenic organisms .

Applications

C-type lectins have various applications in biomedical research, diagnostic tools, and therapeutic strategies. They are involved in extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions . In diagnostic tools, C-type lectins can be used to detect specific carbohydrate structures on pathogens or cancer cells. Therapeutically, targeting C-type lectins may help modulate immune responses or deliver drugs to specific cells .

Role in the Life Cycle

C-type lectins play roles throughout the life cycle, from development to aging and disease. They are involved in essential processes such as development, respiration, coagulation, angiogenesis, and inflammation . During infection and inflammatory responses, the expression of C-type lectins is upregulated to enhance the immune response . Additionally, C-type lectins contribute to immune homeostasis by recognizing and clearing apoptotic cells .

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