Recombinant Proteins

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CST1 Human

Cystatin SN Human Recombinant

Recombinant human CST1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 145 amino acids (specifically, residues 21-141). With a molecular weight of 16.9 kDa, CST1 is fused to a 24 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23201
Source
E.coli.
Appearance
A sterile, filtered solution that is colorless.

CST11 Human

Cystatin 11 Human Recombinant

Recombinant human CST11, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 11.8 kDa. The protein consists of 101 amino acids (residues 26-103) and includes a 23 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23278
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CST3 Human

Cystatin-C Human

Shipped with Ice Packs
Cat. No.
BT23409
Source
Human urine.
Appearance
The product appears as a sterile, white powder that has been lyophilized (freeze-dried).

CST3 Human, His Active

Cystatin C, His BioActive Human Recombinant

Recombinant human CST3, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 141 amino acids (residues 27-146), has a molecular weight of 15.6 kDa, and includes a 21 amino acid His tag at the N-terminus. Purification is achieved using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT23486
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CST3 Mouse, sf9

Cystatin-C Mouse Recombinant, sf9

CST3, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 14.2 kDa, comprising 126 amino acids (21-140a.a.). Its apparent molecular size on SDS-PAGE is approximately 13.5-18 kDa. The protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23917
Source
Sf9, Insect cells.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

CST3 Protein, His

Cystatin-C Human Recombinant, His Tag

Recombinant Human Cystatin-C, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 129 amino acids, with a molecular weight of 14.5 kDa. This protein variant includes an additional His tag at its N-terminus. The amino acid sequence of this Cystatin-C is identical to amino acids 28-146 of the sequence corresponding to UniProtKB/Swiss-Prot entry Q6FGW9. The purification process of Cystatin-C involves proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24012
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder, filtered for purity.

CST3 Rat

Cystatin C Rat Recombinant

This recombinant Cystatin C protein consists of 134 amino acids, with a calculated molecular weight of 14.93 kDa. It includes a 14-amino acid His-tag located at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT24096
Source
Escherichia Coli.
Appearance
White powder, sterile-filtered and lyophilized.

CST4 Human, sf9

Cystatin 4 Human Recombinant, sf9

CST4, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 131 amino acids (21-141 a.a.). With a molecular mass of 15.4 kDa, it migrates at 13.5-18 kDa on SDS-PAGE under reducing conditions. This CST4 variant is expressed with a C-terminal 10 amino acid His tag and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24923
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless and sterile-filtered solution.

CSTB Human, Active

Cystatin-B, BioActive Human Recombinant

Recombinant Human CSTB, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 118 amino acids (specifically, amino acids 1 to 98). It has a molecular weight of 13 kDa. The CSTB protein is fused to a 20 amino acid His tag at its N-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT25751
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Cystatin-C Protein

Cystatin-C Human Recombinant

Recombinant Human Cystatin-C, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 120 amino acids. It has a molecular weight of 13.3 kDa. Cystatin-C undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25847
Source

Escherichia Coli. 

Appearance
Clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Cystatins are a family of cysteine protease inhibitors that play a crucial role in regulating proteolytic activity within cells. They are classified into three main types:

  • Type 1 Cystatins (Stefins): These are primarily intracellular proteins found in the cytosol of various cell types .
  • Type 2 Cystatins: These are mainly extracellular secreted polypeptides, found in most body fluids .
  • Type 3 Cystatins (Kininogens): These are multidomain proteins, with mammalian representatives including high-molecular-mass and low-molecular-mass kininogens .
Biological Properties

Cystatins exhibit several key biological properties:

  • Inhibitory Activity: They inhibit cysteine proteases such as cathepsins and legumain, which are involved in protein degradation .
  • Expression Patterns: Cystatins are expressed in a wide variety of tissues and body fluids .
  • Tissue Distribution: They are found in virtually all tissues, with specific types being more prevalent in certain tissues. For example, cystatin C is found in high concentrations in the brain and kidneys .
Biological Functions

Cystatins serve several primary biological functions:

  • Regulation of Protease Activity: They regulate the activity of cysteine proteases, preventing excessive proteolysis .
  • Immune Response: Cystatins modulate immune responses by influencing the activity of cathepsins involved in antigen presentation and cytokine production .
  • Pathogen Recognition: They play a role in recognizing and responding to pathogens by inhibiting proteases that pathogens use to invade host tissues .
Modes of Action

Cystatins interact with other molecules and cells through several mechanisms:

  • Binding Partners: They bind tightly and reversibly to their target proteases, forming enzyme-inhibitor complexes .
  • Downstream Signaling Cascades: By inhibiting proteases, cystatins can influence downstream signaling pathways involved in inflammation, apoptosis, and cell proliferation .
Regulatory Mechanisms

The expression and activity of cystatins are controlled by various regulatory mechanisms:

  • Transcriptional Regulation: Gene expression of cystatins is regulated at the transcriptional level by various factors .
  • Post-Translational Modifications: Cystatins undergo post-translational modifications such as glycosylation and phosphorylation, which can affect their stability and activity .
Applications

Cystatins have several applications in biomedical research and clinical practice:

  • Diagnostic Tools: Cystatin C is used as a biomarker for kidney function and cardiovascular diseases .
  • Therapeutic Strategies: Cystatins are being explored as potential therapeutic agents for diseases involving excessive protease activity, such as cancer and neurodegenerative disorders .
Role in the Life Cycle

Cystatins play a role throughout the life cycle, from development to aging and disease:

  • Development: They are involved in regulating protease activity during embryonic development and tissue remodeling .
  • Aging: Changes in cystatin levels and activity have been associated with aging and age-related diseases .
  • Disease: Dysregulation of cystatin activity is implicated in various diseases, including neurodegenerative disorders, cardiovascular diseases, and cancer .
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