Recombinant Proteins

p53
LBP
CEA
HLA
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TTC
NPM
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Bax
BID

CST3 Human, Pichia

Cystatin C Human Recombinant, Pichia

Recombinant Human Cystatin C has a molecular mass of approximately 13kDa.
Shipped with Ice Packs
Cat. No.
BT23568
Source

Pichia pastoris.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

CST3 k9

Cystatin-C Canine Recombinant

Cystatin-C Protein from Canis lupus familiaris (dog) is a 14.85 kDa protein comprising 133 amino acids, including an 8 amino acid N-terminal His-tag.
Shipped with Ice Packs
Cat. No.
BT23641
Source
E. coli

CST3 Mouse

Cystatin-C Mouse Recombinant

Recombinant Murine Cystatin-C, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 15 kDa, comprising 134 amino acids. This protein is engineered with an N-terminal His tag to facilitate purification. The purification process involves proprietary chromatographic techniques to obtain highly pure Mouse Cystatin-C.
Shipped with Ice Packs
Cat. No.
BT23715
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered for purity.

CST3 Mouse, Active

Cystatin-C Mouse Recombinant, Active

CST3 Mouse, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain comprising 126 amino acids (specifically, amino acids 21 to 140). It has a molecular mass of 14.2 kDa, though on SDS-PAGE, it appears between 13.5 and 18 kDa. This protein is engineered with a 6-amino-acid His tag at its C-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23833
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CST3 Rat, sf9

Cystatin C Rat Recombinant, sf9

Recombinant Rat CST3, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein consists of 128 amino acids (spanning from amino acid positions 21 to 140a.a.) and has a molecular mass of 14.3 kDa. On SDS-PAGE, the apparent molecular size will appear between 13.5 kDa and 18 kDa. The CST3 protein is engineered with an 8 amino acid His tag at the C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24318
Source
Sf9, Baculovirus cells.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

CST4 Human

Cystatin 4 Human Recombinant

Recombinant human CST4, produced in E. coli, is a single polypeptide chain consisting of 145 amino acids (21-141). With a molecular weight of 16.8 kDa, it features a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24404
Source
E.coli.
Appearance
Sterile, filtered solution, colorless in appearance.

CST5 Human

Cystatin 5 Human Recombinant

Recombinant human CST5, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular mass of 14.36 kDa. It contains 123 amino acids (26-142 a.a), including a 6 amino acid His-tag fused at the C-terminus. CST5 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24991
Source

Sf9, Baculovirus cells.

Appearance
Clear, sterile-filtered solution.

CST6 Human

Cystatin E/M Human Recombinant

Recombinant CST6 Human, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 142 amino acids (29-149). It has a molecular weight of 15.9 kDa. A 21 amino acid His-Tag is fused to the N-terminus of CST6, and purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25138
Source
E.coli.
Appearance
A sterile, colorless solution.

CST6 Human, Active

Cystatin E/M, BioActive Human Recombinant

Recombinant Human CST6, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 142 amino acids (residues 29-149). With a molecular weight of 15.9 kDa, it includes a 21 amino acid His tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25211
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CST7 Human

Cystatin 7 Human Recombinant

Recombinant human CST7, produced in E. coli, is a single polypeptide chain comprising 132 amino acids (residues 20-145) with a molecular weight of 15.3 kDa. A 7-amino acid His-tag is fused to the C-terminus of CST7. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25265
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
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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