TIMP1 Human

Tissue Inhibitor of Metalloprotease 1 Human Recombinant

TIMP1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 184 amino acids fragment (24-207) having a total molecular mass of 25.21kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TIMP1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9976
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

TIMP1 Human, HEK

Tissue Inhibitor of Metalloprotease 1 Human Recombinant, HEK

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

TIMP1 Human, Sf9

Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9

TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (24-207a.a.) and having a molecular mass of 21.5kDa. TIMP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10247
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

TIMP1 Mouse

Tissue Inhibitor of Metalloprotease 1 Mouse Recombinant

TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (25-205 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 187 amino acids and having a molecular mass of 21kDa.
TIMP1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10328
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

TIMP1 Rat

Tissue Inhibitor of Metalloprotease 1 Rat Recombinant

TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-217 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 200 amino acids and having a molecular mass of 22.3kDa.
TIMP1 Ligand shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10412
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

TIMP2 Human

Tissue Inhibitor of Metalloprotease 2 Human Recombinant

TIMP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 194 amino acids and having a molecular mass of 21.8kDa. 
Shipped with Ice Packs
Cat. No.
BT10502
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TIMP2 Human HEK

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, HEK

TIMP2 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-2 (amino acids Cys27-Pro220) and is fused to 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.

TIMP2 Human, His

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag

TIMP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 232 amino acids (27-220) and having a molecular mass of 26.1 kDa.
TIMP2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10646
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TIMP2 Human, Sf9

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, Sf9

TIMP2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (27-220a.a.) and having a molecular mass of 22.5kDa. 
(Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
TIMP2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10723
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear 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.) and having a molecular mass of 23.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). 
TIMP4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10843
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
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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