Anti-Human CD2 [Clone G11] — Purified in vivo GOLD™ Functional Grade

The clone G11 in mice is primarily associated with two distinct applications:

1. Anti-Human CD2 Antibody: Clone G11 is used to recognize an epitope of human CD2, a type I transmembrane glycoprotein belonging to the Ig superfamily. In vivo applications of this antibody in mice are typically related to immunological studies, where CD2 plays a role in immune cell interactions. However, since CD2 is a human antigen, its direct application in mice would be limited to xenograft models or studies involving human cells.

2. Gq/G11 G Proteins: The term "G11" also relates to G11 G proteins, which are part of the Gq/G11 family involved in neuronal signaling. Studies using mice with specific inactivation of Gq/G11 family G proteins have focused on understanding their role in neuronal excitability and endocannabinoid synthesis. These studies, however, do not involve the clone G11 but rather the G11 subunit of G proteins.

There is no direct indication that the clone G11 is commonly used in mice for applications related to the Gq/G11 family of G proteins. Instead, the clone G11 is specifically linked to the anti-human CD2 antibody. Therefore, common in vivo applications of clone G11 in research involving mice would likely be limited to studies that involve human cells or xenograft models where CD2 is a relevant target.

The most commonly used antibodies or proteins with G11 in the literature depend on the specific context—primarily, whether G11 refers to the anti-tenascin-C antibody (often in cancer research) or the GNG11 protein (G-protein gamma subunit 11 in signal transduction). In oncological applications, G11 is frequently paired or compared with other antibodies targeting tumor-associated antigens, antibody formats, or immune modulators.

Key examples in published literature include:

• G11 Antibody Formats: G11 (anti-tenascin-C) has been expressed as:

  • scFv (single-chain variable fragment)
  • SIP (small immunoprotein, fused to human IgE domain)
  • Fusion proteins such as scFv(G11)-IL2, pairing the G11 targeting specificity with the immune-activating cytokine interleukin-2.

• Other Tumor-Associated Antibodies:

  • scFv(L19): Used for comparison due to its targeting of a different domain of tenascin-C or its fusion with IL2.
  • Herceptin (trastuzumab): Frequently referenced as a standard monoclonal antibody against HER2 in comparative oncology, showing the broader context of antibody therapeutics.

• Antibodies for Combined or Comparative Use:

  • In some immunotherapy or experimental designs, G11 is studied alongside tumor-targeting antibodies of different isotypes (e.g., IgG1, IgG2, IgG3).
  • Logic-gated or bispecific antibody strategies sometimes involve pairs of monoclonal antibodies for synergistic cell targeting or depletion—for example, combinations akin to Rituximab and Obinutuzumab in B cell depletion experiments, though not explicitly with G11.

• Antibodies/Proteins Related to GNG11 Context:

  • When studying GNG11, typical pairings involve antibodies against other G-protein subunits (beta, gamma) or signaling pathway proteins for pathway mapping (e.g., GNG11 with GNG4, GNB1, etc.), but specific literature pairings are less frequently named.

• Experimental Antibody Protein Partners:

  • G11 has also been tested in formats fused to proteins such as human cytokines (IL2), and in the context of antibody engineering, different Fc backbones and antibody scaffolds (e.g., IgG1, IgG3) are sometimes explored.

• Comparative/Control Antibodies:

  • Standard immunoassay controls and comparative reagents (anti-IgG, anti-mouse/human IgE, anti-STK19 in the context of G11 being an alternate name for STK19, depending on the manufacturer/antibody).

The most consistent pattern in published studies is the use of G11 in fusion formats (with cytokines like IL-2), comparisons with L19 or Herceptin for benchmarking, and exploration of different antibody isotypes or scaffolds for optimizing pharmacokinetics and tumor targeting.

If you are referring specifically to a commercial reference or signaling context for GNG11, common protein partners include other G-protein subunits, with various recombinant forms produced for rat, mouse, and human species for ELISA and immunohistochemistry.

If your context is immunotherapy, the pairing pattern is with antibodies targeting different tumor markers or with immunomodulatory fusion partners. If you specify your application—e.g., cancer targeting vs. G-protein research—I can provide more tailored protein and antibody pairings.

Key Findings from Clone G11 in Scientific Literature

Multiple studies have investigated the properties and therapeutic potential of clone G11, primarily as a single-chain variable fragment (scFv) antibody targeting the C domain of tenascin-C (TNC-C), but also in other contexts.

Binding and Affinity Characteristics

• High Affinity for Tenascin-C (TNC-C): The scFv(G11) clone exhibits a high affinity for the human TNC-C antigen, with a monomeric dissociation constant ((K_D)) of 4.2 nM, representing a 22-fold improvement over the previous scFv(E10) and a 160-fold improvement over the parental scFv(A12).
• Target Specificity: Immunohistochemical analysis showed that scFv(G11) binds strongly and specifically to various human lung tumor tissues (including squamous cell carcinoma, adenocarcinoma, and others), while showing no detectable staining in normal tissues, indicating a highly restricted expression pattern of the targeted TNC-C isoform in tumors.

Engineering and Applications

• Format Optimization: The G11 antibody has been reformatted into several constructs, including bivalent miniantibodies (small immunoprotein, SIP) and cytokine fusions (e.g., with interleukin-2), which may offer advantages for in vivo tumor targeting and delivery of therapeutic payloads.
• Tumor-Penetrating Peptide Fusion: Genetic fusion of the iRGD tumor-penetrating peptide to scFv(G11) markedly enhanced the antibody’s ability to bind αVβ3 integrins and improved its tumor homing, extravasation, and penetration into glioblastoma (U87-MG) xenografts in mice. This modification did not affect the antibody’s binding to TNC-C and could facilitate more efficient delivery of imaging or therapeutic agents to solid tumors.
• Relevance for Solid Tumors: The C domain of TNC-C is upregulated in solid tumors, and scFv(G11)-based vehicles have been explored for both therapeutic and diagnostic applications due to their specificity and restricted expression in the tumor microenvironment.

Broader Impact

• Tool for Tumor Targeting: Clone G11, as an affinity ligand for TNC-C, is part of a broader effort to develop targeting vehicles for solid tumors, alongside other ligands like aptamers and the FH peptide.
• Other Contexts: The identifier “G11” is used in other research areas (e.g., in the context of monoclonal antibodies against Echinococcus multilocularis antigens), but the most extensively characterized “clone G11” in the provided literature refers to the anti-TNC-C scFv.

Summary Table: Key Features of scFv(G11) Anti-TNC-C

Conclusion

The clone G11 scFv antibody is a high-affinity, tumor-specific ligand for TNC-C, with demonstrated utility in cancer imaging and targeted therapy. Its fusion with tumor-penetrating peptides further enhances its delivery capabilities, making it a promising candidate for improving the specificity and efficacy of cancer therapeutics and diagnostics.

Dosing regimens for clone G11 vary depending on both the specific antibody format and the mouse model employed, particularly in the context of cancer, immunotherapy, and glioblastoma experiments. However, direct, detailed regimen data for clone G11 across multiple mouse models is not comprehensively available in the provided results.

Key insights from the available data:

• Tumor models (e.g., U87-MG glioblastoma xenografts):

  • When fused to iRGD (a tumor-penetrating peptide), a G11 single-chain variable fragment (scFv G11) antibody was used in an intravascular/intravenous administration regimen in mice.
  • The regimen improved antibody homing and penetration into tumor tissue, but the exact dose/concentration was not specified in the summary.
  • Dosing frequency or adjustment for different mouse strains or immunodeficient (e.g., nude, SCID) mice was not explicitly stated.

• General principles from related antibody dosing guides:

  • Standard in vivo antibody doses in mice typically range from 100–250 μg per mouse per injection, commonly administered via intraperitoneal (i.p.) injection every 3–5 days, with adjustments based on antibody isotype, target, and goal (blockade vs. depletion vs. immunostimulation).
  • Dosing regimens may be further tailored according to mouse strain, immune status, tumor burden, and experimental endpoints.

Examples from related antibodies (for reference):

Important context and limitations:

• Direct dosing data for clone G11 in multiple mouse models is sparse. The main published example found refers to its use as part of a fusion construct in human glioblastoma xenografts (U87-MG), without explicit dose/frequency details.
• For standard antibody regimens in mice, the dose is often in the range of 100-250 μg per injection, given i.p. or i.v., adjusting for mouse size, tumor type, and experimental objective.

If planning experiments with clone G11:

• Start with the 100–250 μg/mouse/dose range, adjusting based on pilot results and literature precedent for similar antibody formats and targets.
• Carefully review the specific goals (e.g., tumor targeting, immune cell depletion, imaging) and any available preclinical studies for this clone to match dosing, route, and schedule to your mouse model.

Summary:
The exact dosing regimen for clone G11 in different mouse models is not fully characterized in the current literature, but based on antibody dosing norms in mice, it is likely to fall within the standard 100–250 μg per mouse per dose range, given by i.p. or i.v. injection every 3–5 days, with further adjustment depending on mouse strain and tumor model.