Anti-Glucose 6 phosphate isomerase Rabbit Monoclonal Antibody

Overview

This product is an anti-GPI antibody for target detection and characterization. Key identifiers include host species: Rabbit; Monoclonal; clone 18G57; isotype IgG; reactivity: Human. Reported application contexts include WB, IHC, ICC, IF, Flow (as provided in the source record). Boster Bio Anti-Glucose 6 phosphate isomerase Rabbit Monoclonal Antibody catalog # M00108-1. Tested in WB, IHC, ICC/IF, Flow Cytometry applications. This antibody reacts with Human.

Key elements and design rationale

• Target: GPI (Proto-oncogene tyrosine-protein kinase Src).
• Antibody format: Monoclonal; clone 18G57; isotype IgG.
• Host: Rabbit.
• Species reactivity: Human (confirm in your model system with appropriate controls).

This description is intended to help interpret the antibody design and the biological context of the target using the fields provided in the catalog record, alongside general experimental considerations.

Biological background

GPI (protein: P2X purinoceptor 1) is a commonly studied target in molecular and cellular biology. Functional context (as provided): Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein- coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin- 43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr- 1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta- arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr- 128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. . Reported cellular localization context: Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. Tissue expression notes (as provided): Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.

Research relevance and current trends

• Research context keywords from the source record include: Protein Phosphorylation,Signal Transduction,Tyrosine Kinases.
• Current studies often focus on connecting target abundance/localization to pathway perturbations across models, tissues, and cell states.
• Quantitative and multiplexed assays (e.g., imaging + immunoblot panels) are commonly used to compare phenotypes across conditions and time-courses.

Common research applications

• Western blotting (WB): assess relative target abundance across samples, treatments, or time-points.
• Immunohistochemistry (IHC): evaluate spatial distribution of target-positive staining in tissue architecture.
• Immunofluorescence/ICC (IF/ICC): visualize subcellular localization patterns and cell-to-cell heterogeneity.
• Flow cytometry: quantify target-positive populations and compare shifts in marker distributions.

Workflow ideas (metafield): Validate GPI antibody specificity using KO/KD control samples (WB/IF/IHC as appropriate), Detect GPI expression by Western blot in cell or tissue lysates, Detect GPI in FFPE tissue sections by immunohistochemistry, Localize GPI by immunofluorescence/immunocytochemistry in cultured cells, Quantify GPI-positive cells by flow cytometry in single-cell suspensions

Notes for experimental interpretation

• Consider isoforms and post-translational modifications (PTMs) that may shift apparent molecular weight or epitope accessibility.
• Apparent molecular weight may vary by sample type and processing (observed MW: 63 kDa; calculated MW: 59835 MW).
• Control concepts: include appropriate negative controls (e.g., isotype, KO/KD samples) and orthogonal validation when feasible.

Additional product details (from the source record)

• Molecular weight (observed): 63 kDa
• Cellular localization (provided): Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.
• Tissue details (provided): Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.

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