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

Cat# C365-1

Size : 1.0mg

Brand : Leinco Technologies

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AntiHuman CD2 [Clone G11] — Purified in vivo GOLD™ Functional Grade

Product No.: C365

[product_table name="All Top" skus="C365"]

Clone
G11
Target
CD2
Formats AvailableView All
Product Type
Monoclonal Antibody
Isotype
Mouse IgG2a
Applications
Costim
,
FC
,
IHC
,
in vivo
,
WB

Antibody Details

Product Details

Reactive Species
Human
Host Species
Mouse
Recommended Isotype Controls
Recommended Dilution Buffer
Immunogen
Not available or unknown
Product Concentration
≥ 5.0 mg/ml
Endotoxin Level
< 1.0 EU/mg as determined by the LAL method
Purity
≥95% monomer by analytical SEC
>95% by SDS Page
Formulation
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Product Preparation
Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro cell culture techniques and are purified by a multistep process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
Storage and Handling
Functional grade preclinical antibodies may be stored sterile as received at 28°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≤ 70°C. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
USA
Shipping
Next Day 28°C
Applications and Recommended Usage?
Quality Tested by Leinco
FC The suggested concentration for this G11 antibody for staining cells in flow cytometry is ≤ 1.0 μg per 106 cells in a volume of 100 μl or 100μl of whole blood. Titration of the reagent is recommended for optimal performance for each application.
WB
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Description

Specificity
Clone G11 recognizes an epitope of human CD2.
Background
CD2 is a 4559 kD type I transmembrane glycoprotein belonging to the Ig superfamily. CD2 is the receptor for LFA3/CD58. CD2 serves as an adhesion receptor that binds to CD58; generating the activation of CD2positive T cells and NK cells and in the regulation of their cytolytic activities. CD2 is a specific marker for T cells and NK cells. Hence, it can be used in immunohistochemistry to identify the occurrence of these cells in tissue sections. The vast majority of T cell lymphomas and leukemias express CD2 which makes it possible to distinguish these conditions from Bcell lymphomas.
Antigen Distribution
CD2 is present on normal peripheral blood lymphocytes, thymocytes, mature circulating Tcells and a subset of NK cells.
Ligand/Receptor
CD58 (LFA3), CD48, CD59, CD15
PubMed
NCBI Gene Bank ID
Research Area
Costimulatory Molecules
.
Immunology

Leinco Antibody Advisor

Powered by AI: AI is experimental and still learning how to provide the best assistance. It may occasionally generate incorrect or incomplete responses. Please do not rely solely on its recommendations when making purchasing decisions or designing experiments.

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

  1. AntiHuman 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 antihuman 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 antitenascinC antibody (often in cancer research) or the GNG11 protein (Gprotein gamma subunit 11 in signal transduction). In oncological applications, G11 is frequently paired or compared with other antibodies targeting tumorassociated antigens, antibody formats, or immune modulators.

Key examples in published literature include:

  • G11 Antibody Formats: G11 (antitenascinC) has been expressed as:

    • scFv (singlechain variable fragment)
    • SIP (small immunoprotein, fused to human IgE domain)
    • Fusion proteins such as scFv(G11)IL2, pairing the G11 targeting specificity with the immuneactivating cytokine interleukin2.
  • Other TumorAssociated Antibodies:

    • scFv(L19): Used for comparison due to its targeting of a different domain of tenascinC 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 tumortargeting antibodies of different isotypes (e.g., IgG1, IgG2, IgG3).
    • Logicgated 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 Gprotein 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 (antiIgG, antimouse/human IgE, antiSTK19 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 IL2), 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 Gprotein 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. Gprotein 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 singlechain variable fragment (scFv) antibody targeting the C domain of tenascinC (TNCC), but also in other contexts.

Binding and Affinity Characteristics

  • High Affinity for TenascinC (TNCC): The scFv(G11) clone exhibits a high affinity for the human TNCC antigen, with a monomeric dissociation constant ((K_D)) of 4.2 nM, representing a 22fold improvement over the previous scFv(E10) and a 160fold 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 TNCC 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 interleukin2), which may offer advantages for in vivo tumor targeting and delivery of therapeutic payloads.
  • TumorPenetrating Peptide Fusion: Genetic fusion of the iRGD tumorpenetrating peptide to scFv(G11) markedly enhanced the antibody’s ability to bind αVβ3 integrins and improved its tumor homing, extravasation, and penetration into glioblastoma (U87MG) xenografts in mice. This modification did not affect the antibody’s binding to TNCC and could facilitate more efficient delivery of imaging or therapeutic agents to solid tumors.
  • Relevance for Solid Tumors: The C domain of TNCC 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 TNCC, 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 antiTNCC scFv.

Summary Table: Key Features of scFv(G11) AntiTNCC

FeatureDescription
TargetC domain of tenascinC (TNCC), specifically in solid tumors
Affinity ((K_D))4.2 nM (monomeric)
SpecificityBinds tumor tissues only, no staining in normal tissues
Engineering FormatsscFv, bivalent SIP, cytokine fusions (e.g., IL2)
Tumor Penetration EnhancementiRGD fusion improves homing, extravasation, and parenchymal penetration in glioblastoma models
ApplicationsTumor imaging, drug delivery, therapeutic targeting

Conclusion

The clone G11 scFv antibody is a highaffinity, tumorspecific ligand for TNCC, with demonstrated utility in cancer imaging and targeted therapy. Its fusion with tumorpenetrating 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., U87MG glioblastoma xenografts):

    • When fused to iRGD (a tumorpenetrating peptide), a G11 singlechain 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):

AntibodyTypical DoseRouteFrequencyApplication Example
9H10 (antiCTLA4)100–200 μg/mouseIntraperitonealEvery ~3 daysCheckpoint blockade in tumor models
9D9 (antiCTLA4)100–250 μg/mouseIntraperitonealEvery 3 daysTreg depletion/tumor studies
11B11 (antiIL4)1 mg/mouseIntraperitonealEvery 4–5 daysTumor and inflammatory models
(ScFv G11, U87MG)Not specifiedNot specifiedNot specifiedTumor targeting (glioblastoma)

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 (U87MG), without explicit dose/frequency details.
  • For standard antibody regimens in mice, the dose is often in the range of 100250 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.

References & Citations

1. Stern, LJ. et al. (2005) Proc Natl Acad Sci U S A.102(10):37449 PubMed
2. Woetmann, Anders et al. (2010) Experimental Dermatology 19: 1096–1102. Article Link
3. Meuer, S.C. et al. (1984) Cell 36:897
4. Peterson, A. and Sneed, B. (1987) Nature 329:842
5. Bierer, B.E. et al. (1989) Annu. Rev Immunol. 7:579
6. Krensky, C.F. et al. (1982) Proc. Natl. Acad. Sci. USA 79:7489
7. Krensky, C.F. et al. (1983) J. Immunol. 131:611

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