Recombinant Proteins

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GIPC1 Human

GIPC PDZ Domain Member 1 Human Recombinant

Recombinant Human GIPC1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 353 amino acids (1-333 a.a). It has a molecular weight of 38.2 kDa. The GIPC1 protein is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11204
Source
Escherichia Coli.
Appearance
A sterile, colorless solution that has been filtered.

GIPC2 Human

GIPC PDZ Domain Member 2 Human Recombinant

Recombinant GIPC2, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 339 amino acids (residues 1-315) with a molecular weight of 36.9 kDa. The protein includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11284
Source
E.coli.
Appearance
The product is a sterile, colorless, and clear solution.
Definition and Classification

The GIPC (GAIP-interacting protein, C-terminus) family consists of adaptor proteins that contain a single PDZ (PSD95, DLG1, ZO1) domain. These proteins are involved in various cellular processes, including vesicular trafficking and signal transduction. The PDZ domain is a compact protein module that mediates specific protein-protein interactions, typically recognizing short amino acid motifs at the C-termini of target proteins .

Biological Properties

Key Biological Properties: GIPC proteins, including GIPC1, GIPC2, and GIPC3, are characterized by a central PDZ domain flanked by an N-terminal GIPC-homology 1 (GH1) domain and a C-terminal GH2 domain .

Expression Patterns and Tissue Distribution: GIPC proteins are widely expressed in various tissues. For instance, GIPC3 is localized in sensory hair cells and spiral ganglion neurons, playing a crucial role in auditory function . GIPC1 is found in neurons, where it is distributed throughout the cell, including both presynaptic and postsynaptic locations .

Biological Functions

Primary Biological Functions: GIPC proteins are involved in the trafficking and signaling of several membrane proteins. They interact with key transmembrane proteins such as receptor tyrosine kinases, G-protein-coupled receptors, and integrins .

Role in Immune Responses and Pathogen Recognition: GIPC proteins modulate phagocytosis, a critical process in the immune response. For example, CD93, a myeloid cell-surface marker, interacts with GIPC to enhance phagocytosis .

Modes of Action

Mechanisms with Other Molecules and Cells: GIPC proteins bind to PDZ-binding motifs (PBMs) of interacting proteins. For instance, GIPC3 binds directly to MYO6, and this interaction is crucial for shaping the cuticular plate in hair cells .

Binding Partners and Downstream Signaling Cascades: GIPC1 interacts with various proteins, including IGF1R, NTRK1, ADRB1, and TGFbR3, to mediate endosomal trafficking and signal transduction . GIPC also regulates NMDA receptor trafficking, influencing synaptic plasticity and development .

Regulatory Mechanisms

Transcriptional Regulation and Post-Translational Modifications: GIPC proteins are regulated through various mechanisms, including phosphorylation and autoinhibition. For example, GIPC1 can exist in an autoinhibited configuration, where binding sites are masked until interaction with PBMs releases this inhibition .

Applications

Biomedical Research: GIPC proteins are studied for their roles in cancer biology, as their dysregulation is associated with tumor proliferation and invasion .

Diagnostic Tools and Therapeutic Strategies: Understanding GIPC interactions can lead to the development of diagnostic markers and therapeutic targets for diseases such as cancer and hereditary deafness .

Role in the Life Cycle

Development to Aging and Disease: GIPC proteins play roles throughout the life cycle. For instance, GIPC3 is essential for auditory function from early postnatal development to adulthood . Dysregulation of GIPC proteins can lead to various pathologies, including cancer and neurodegenerative diseases .

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