TIMP1 Human

Tissue Inhibitor of Metalloprotease 1 Human Recombinant

Recombinant human TIMP1, produced in E. coli, is a non-glycosylated polypeptide chain encompassing amino acids 24-207 (184 amino acids total). This protein, with a molecular weight of 25.21 kDa, includes a 4.5 kDa N-terminal hexahistidine tag. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9976
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

TIMP1 Human, HEK

Tissue Inhibitor of Metalloprotease 1 Human Recombinant, HEK

Recombinant Human TIMP1, produced in HEK-293 cells, is a secreted protein encompassing the amino acid sequence of Human TIMP-1 (Cys24-Ala207) and fused to a C-terminal polyhistidine tag.
Shipped with Ice Packs
Cat. No.
BT10067
Source
HEK293 Cells.
Appearance
Sterile Filtered White lyophilized powder.

TIMP2 Human, His

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag

Recombinant Human TIMP2, expressed in E. coli, is a single polypeptide chain with a molecular weight of 26.1 kDa. It consists of 232 amino acids (residues 27-220) and includes a 38 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10646
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

TIMP2 Human, Sf9

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, Sf9

Recombinant TIMP2, expressed in Sf9 insect cells using baculovirus, is a single, glycosylated polypeptide chain. It encompasses amino acids 27 to 220, resulting in a molecular weight of 22.5 kDa. Note: The apparent molecular size on SDS-PAGE may vary between 18-28 kDa. This TIMP2 variant is engineered with a 6-amino acid His tag at the C-terminus to facilitate purification via proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10723
Source
Sf9, Baculovirus cells.
Appearance
The product is a clear, sterile-filtered solution.

TIMP4 Human

Tissue Inhibitor of Metalloprotease 4 Human Recombinant

TIMP4, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 204 amino acids (30-224 a.a.) with a molecular mass of 23.5 kDa. The molecular size on SDS-PAGE will appear at approximately 18-28 kDa. TIMP4 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.
BT10843
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered, colorless solution.

TIMP1 Human, Sf9

Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, TIMP1 is a single, glycosylated polypeptide chain with a molecular weight of 21.5kDa. It comprises 190 amino acids (24-207a.a.) and includes a 6-amino acid His tag at the C-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10247
Source
Sf9, Baculovirus cells.
Appearance
The product appears as a clear, sterile-filtered solution.

TIMP1 Mouse

Tissue Inhibitor of Metalloprotease 1 Mouse Recombinant

TIMP1, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain encompassing amino acids 25-205. A 6 amino acid His Tag is fused to the C-terminus, resulting in a protein with a total of 187 amino acids and a molecular mass of 21 kDa. TIMP1 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10328
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

TIMP1 Rat

Tissue Inhibitor of Metalloprotease 1 Rat Recombinant

TIMP1, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain encompassing amino acids 24-217. It is fused to a 6-amino acid His Tag at the C-terminus, resulting in a total of 200 amino acids and a molecular mass of 22.3 kDa. On SDS-PAGE under reducing conditions, TIMP1 Ligand exhibits multiple bands between 18-28 kDa. It is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10412
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

TIMP2 Human

Tissue Inhibitor of Metalloprotease 2 Human Recombinant

Recombinant human TIMP2, produced in E. coli, is a single, non-glycosylated polypeptide chain with 194 amino acids and a molecular weight of 21.8 kDa.
Shipped with Ice Packs
Cat. No.
BT10502
Source
Escherichia Coli.
Appearance
White, sterile-filtered, lyophilized (freeze-dried) powder.

TIMP2 Human HEK

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, HEK

Recombinant Human TIMP2, produced in HEK-293 cells, is a secreted protein. It encompasses the amino acid sequence of Human TIMP-2 (Cys27-Pro220) and carries a polyhistidine tag at the C-terminus.
Shipped with Ice Packs
Cat. No.
BT10567
Source
HEK293 Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Tissue Inhibitors of Metalloproteinases (TIMPs) are a family of proteins that inhibit the activity of matrix metalloproteinases (MMPs), which are enzymes involved in the degradation of the extracellular matrix (ECM). There are four known TIMPs: TIMP-1, TIMP-2, TIMP-3, and TIMP-4 . Each TIMP has a unique structure and function, but they all share the ability to inhibit MMP activity.

Biological Properties

Key Biological Properties: TIMPs are known for their ability to regulate ECM turnover by inhibiting MMPs. They also have roles in cell growth, apoptosis, differentiation, and angiogenesis .

Expression Patterns and Tissue Distribution: TIMPs are expressed in various tissues throughout the body. For example, TIMP-1 is found in high levels in the liver, spleen, and lung, while TIMP-2 is more ubiquitously expressed . TIMP-3 is primarily found in the ECM, and TIMP-4 is expressed in the heart and other tissues .

Biological Functions

Primary Biological Functions: TIMPs play a crucial role in maintaining tissue homeostasis by regulating ECM turnover. They also have cytokine-like activities, influencing processes such as cell proliferation, apoptosis, and differentiation .

Role in Immune Responses and Pathogen Recognition: TIMPs are involved in immune responses by modulating the activity of MMPs, which can influence the migration and activation of immune cells . They also play a role in pathogen recognition by regulating the ECM, which can act as a barrier to infection .

Modes of Action

Mechanisms with Other Molecules and Cells: TIMPs interact with MMPs to form non-covalent 1:1 stoichiometric complexes, inhibiting their proteolytic activity . They also interact with other proteins, such as integrins and growth factors, to modulate cellular responses .

Binding Partners and Downstream Signaling Cascades: TIMPs can bind to specific surface receptors, initiating signaling cascades that influence cell behavior. For example, TIMP-1 can bind to the CD63 receptor, activating downstream signaling pathways that promote cell survival and proliferation .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: TIMP expression is regulated at both the transcriptional and post-transcriptional levels. Various cytokines and growth factors, such as TGF-β and EGF, can upregulate TIMP expression . Post-translational modifications, such as glycosylation, can also influence TIMP activity .

Applications

Biomedical Research: TIMPs are used as biomarkers for various diseases, including cancer and cardiovascular diseases . They are also studied for their potential therapeutic applications, such as in the treatment of fibrosis and cancer .

Diagnostic Tools: TIMP levels can be measured in biological samples to diagnose and monitor disease progression .

Therapeutic Strategies: TIMPs are being explored as therapeutic agents for diseases characterized by excessive ECM degradation, such as arthritis and cancer .

Role in the Life Cycle

Role Throughout the Life Cycle: TIMPs play a role in various stages of life, from development to aging. During development, they regulate ECM remodeling, which is crucial for tissue formation and organogenesis . In adulthood, they maintain tissue homeostasis and repair . In aging and disease, dysregulation of TIMP activity can contribute to pathological conditions, such as fibrosis and cancer .

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