CYR61 Human

Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

This description details the characteristics of the CYR61 Human Recombinant product, specifying it as a single, non-glycosylated polypeptide chain produced in E.Coli. It outlines its molecular weight and purification method.
Shipped with Ice Packs
Cat. No.
BT16195
Source
Escherichia Coli.
Appearance
This describes the visual appearance of the lyophilized CYR61 Human Recombinant product, stating it as a sterile, filtered, white powder.

IGFBP 1 Human

Insulin-Like Growth Factor Binding Protein-1 Human Recombinant

Recombinant Human IGFBP-1 (amino acids 26-259) is produced in NS0 cells. It is a single, glycosylated polypeptide chain with 234 amino acids and a molecular weight of 25 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16250
Source
Mouse myeloma cell line, NS0.
Appearance
White, sterile, lyophilized powder.

IGFBP 4 Human

Insulin-Like Growth Factor Binding Protein-4 Human

This product is recombinant human IGFBP-4, encompassing amino acids Asp22 to Glu258. Produced in HEK293 cells, it features a C-terminal polyhistidine tag. The predicted molecular weight (Mw) of IGFBP4 is 27 kDa. However, under denaturing conditions on SDS-PAGE, it appears as a 32 kDa band. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16328
Source
HEK293 cells.
Appearance
The product is a sterile, filtered, white lyophilized (freeze-dried) powder.

IGFBP 5 Human

Insulin-Like Growth Factor Binding Protein-5 Human Recombinant

Recombinant Human IGFBP5, produced in E. coli, is a non-glycosylated homodimer with a molecular weight of 28.6 kDa. Each homodimer consists of two polypeptide chains, each containing 252 amino acids. The purification of IGFBP5 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16415
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder that has been sterile filtered.

IGFBP1 Human, HEK

Insulin-Like Growth Factor Binding Protein-1 Human Recombinant, HEK

Recombinant human IGFBP1 is a single polypeptide chain with glycosylation. It consists of 234 amino acids (26-259 a.a) and has a molecular weight of 25.2 kDa. The purification of IGFBP1 is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT16512
Source

HEK293 Cells.

Appearance

A clear, colorless solution that has been sterile filtered.

IGFBP7 Human, His

Insulin Like Growth Factor Binding Protein-7Human Recombinant, His Tag

Recombinant human IGFBP7, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 279 amino acids (residues 27-282) and has a molecular weight of 28.8 kDa. The protein includes a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17208
Source
Escherichia Coli.
Appearance
The product appears as a clear, sterile-filtered solution.

IGFBP6 Human

IGFBP-6 Human Recombinant

Recombinant human IGFBP6 is a 20 kDa protein that is produced in E. coli. It is a single, non-glycosylated polypeptide chain that contains amino acids 148-240 of the human IGFBP6 protein. The recombinant protein also contains a 4 kDa His tag to facilitate purification.
Shipped with Ice Packs
Cat. No.
BT16971
Source
Escherichia Coli.
Appearance
White powder, freeze-dried.

IGFBP6 Mouse

Insulin Like Growth Factor Binding Protein-6 Mouse Recombinant

Recombinant Mouse IGFBP6, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 221 amino acids (26-238 a.a.), with a molecular weight of 23.7kDa (observed as 28-40kDa on SDS-PAGE under reducing conditions). This IGFBP6 protein is expressed with an 8 amino acid His tag at its C-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17059
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

IGFBP7 Human

Insulin-Like Growth Factor Binding Protein-7 Human Recombinant

Recombinant Human IGFBP7, produced in E.coli cells, is a non-glycosylated protein with a homodimeric structure. It consists of two polypeptide chains, each containing 256 amino acids, resulting in a molecular mass of 26.4kDa. The purification of IGFBP-7 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17129
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

IGFBP2 Mouse

Insulin Like Growth Factor Binding Protein-2 Mouse Recombinant

Recombinant Mouse IGFBP2, produced in HEK293 cells, is a single glycosylated polypeptide chain encompassing amino acids 35-305. This protein, with a molecular mass of 30.3 kDa, comprises 277 amino acids. It features a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16593
Source

HEK293 cells.

Appearance
Sterile Filtered colorless solution.
Definition and Classification

Insulin-like growth factor binding proteins (IGFBPs) are a family of proteins that bind to insulin-like growth factors (IGFs) with high affinity. There are six distinct types of IGFBPs in vertebrates: IGFBP-1, IGFBP-2, IGFBP-3, IGFBP-4, IGFBP-5, and IGFBP-6 . These proteins play a crucial role in regulating the availability and activity of IGFs by extending their half-life and modulating their interaction with IGF receptors .

Biological Properties

Key Biological Properties: IGFBPs are present in all biological fluids and have a molecular weight ranging from 24 to 45 kDa . They share significant sequence homology and have binding affinities for IGF-I and IGF-II .

Expression Patterns: The expression of IGFBPs varies across different tissues and developmental stages. For example, IGFBP-3 is the most abundant and accounts for 80% of all IGF binding .

Tissue Distribution: IGFBPs are widely distributed in various tissues, including the liver, prostate, and other organs . Their expression can be influenced by physiological conditions and disease states .

Biological Functions

Primary Biological Functions: IGFBPs regulate the bioavailability of IGFs, thereby influencing cell growth, proliferation, differentiation, and survival . They can either enhance or inhibit IGF signaling depending on the context .

Role in Immune Responses and Pathogen Recognition: IGFBPs have been shown to modulate immune responses and may play a role in pathogen recognition . They can influence the activity of immune cells and the production of cytokines .

Modes of Action

Mechanisms with Other Molecules and Cells: IGFBPs interact with IGFs to regulate their access to IGF receptors . They can also bind to other cell surface receptors, such as integrins and transforming growth factor β (TGF-β) family receptors .

Binding Partners and Downstream Signaling Cascades: IGFBPs can modulate signaling cascades by interacting with various binding partners, including intracellular ligands and nuclear hormone receptors . These interactions can influence gene transcription and cellular functions .

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of IGFBPs are controlled by various regulatory mechanisms, including transcriptional regulation and post-translational modifications . Phosphorylation, glycosylation, and proteolysis are some of the post-translational modifications that can affect IGFBP function .

Applications

Biomedical Research: IGFBPs are used as biomarkers in cancer research and other diseases . They can provide insights into disease progression and prognosis .

Diagnostic Tools: IGFBPs are being explored as diagnostic tools for various conditions, including cancer and metabolic disorders .

Therapeutic Strategies: IGFBPs have potential therapeutic applications, such as targeting IGFBP-3 for cancer treatment . Their ability to modulate IGF signaling makes them attractive candidates for drug development .

Role in the Life Cycle

Role Throughout the Life Cycle: IGFBPs play a critical role throughout the life cycle, from development to aging . They are involved in various physiological processes, including growth, metabolism, and tissue repair . Dysregulation of IGFBP expression and function can contribute to aging and age-related diseases .

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