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 multi-step 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 2-8°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 2-8°C
Working Concentration
This isotype control antibody should be used at the same concentration as the primary antibody.
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.
Description
Specificity
This Rat IgG2b isotype control (anti-Trinitrophenol + KLH) antibody has been tested against selected species' cells and tissues to assure minimal cross reactivity.
Leinco Antibody Advisor
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The term "clone 1-2" is ambiguous. It could refer to an antibody clone (used for targeting specific proteins in vivo), a genetic labeling method (e.g., CLoNe for clonal lineage tracing), or even a specific cell line or engineered variant. Based on your context"in vivo mouse studies"the most likely interpretations are:
Antibody Clone for Targeting Mouse Proteins
A Genetic Labeling/Tracing System
There are no direct matches in the search results for clone 1-2 specifically. However, here's how similar clones (e.g., antibody or clonal tracing systems) are used in mouse in vivo studies:
1. Antibody Clone Usage in In Vivo Mouse Studies
Antibody clones are monoclonal antibodies targeting specific proteins (like PD-1, CD90.2) on mouse cells. Clones such as RMP1-14 (PD-1) or 30-H12 (CD90.2) are commonly named with a number-letter code; e.g., "RMP1-14" or "30-H12".
These antibodies are administered to mice to:
Block signaling pathways (e.g., immune checkpoint inhibition using anti-PD-1 antibodies).
Deplete cell populations (e.g., anti-CD90.2 is used to deplete Thy1.2+ T cells).
The chosen clone impacts the experiment by its species of origin, binding affinity, and functional effects.
Example:
Clone 30-H12 (anti-CD90.2): Used for in vivo depletion or identification of Thy1.2-expressing cells in mice.
2. Clonal Labeling Methods (e.g., CLoNe)
If "clone 1-2" refers to clonal lineage analysis, such as the CLoNe (Clonal Labeling of Neural Progenies) technique:
CLoNe is used to tag and follow the progeny of single progenitor cells in various mouse tissues, especially neural tissue.
Researchers introduce a targeting vector (often using Cre/loxP system) at a controlled concentration to label individual progenitors and their lineages with unique genetic or fluorescent tags.
This enables:
Tracking of cell lineage and fate.
Analysis of clonal relationships and cell behavior in development or disease.
Key features:
Multiple clones can be analyzed in one animal.
Clones are defined by unique combination of labels, allowing discrimination between different progenitor-derived lineages.
If you meant a clone NOT covered here (like a specific hybridoma, cell line, or genetically engineered cell):
Please provide additional details (e.g., target antigen, genetic marker, cell type, or context).
With clarification, a more targeted answer can be provided.
Summary:
Antibody clones like "30-H12" and "RMP1-14" are injected to modulate or track immune cells in mice.
Clonal labeling techniques such as CLoNe allow tracking of cell lineage using unique genetic tags.
Clone 1-2 itself is not found in the referenced literature. Please clarify if you meant a specific antibody, labeling method, or cell line.
Commonly Used Antibodies and Proteins in Conjunction with 1-2
When researchers refer to 1-2, they likely mean monoclonal antibodies (mAbs) or peptide–antibody complexesespecially given the context of antibody research, structure, and cross-reactivity. Here, we outline the types of antibodies and proteins most frequently referenced alongside 1-2 in the literature, based on recent structural, immunological, and therapeutic studies.
Antibodies and Proteins in Antibody–Peptide Recognition
Monoclonal Antibodies (e.g., H1-74, HCV1, 10E8, 2F5, 4E10): These are commonly studied for their ability to bind antigens and peptides. For example, the H1-74 mAb interacts with multiple influenza hemagglutinin (HA) peptides and synthetic variants, illustrating both specificity and cross-reactivity depending on key amino acid residues in the complementarity-determining region (CDR). HCV1 targets a linear epitope in HCV E2, while 10E8, 2F5, and 4E10 are HIV antibodies that bind to the membrane-proximal external region (MPER) of Env, often influenced by membrane lipids.
Polyclonal Antibodies: Used in diagnostic and therapeutic contexts, such as anti-toxins for botulism and Rh(D) immunoglobulins.
Recombinant Antibodies: Used in research, diagnostics, and therapeutics. Examples include MAbs to CD markers (CD20, CD34), tumor markers (EGFR, B-Raf), and checkpoint inhibitors (anti-PD-1, e.g., Nivolumab, Pembrolizumab).
Secondary Antibodies (Conjugated to Enzymes or Fluorescent Dyes): Commonly used in assays like ELISA, Western blot, and immunohistochemistry. Conjugates include horseradish peroxidase, alkaline phosphatase, fluorescent dyes (Alexa Fluor, DyLight, Cy, etc.), and biotin.
Proteins and Peptides Used in Conjunction with Antibodies
Fusion Proteins and Artificial Antigens: Engineered for immunization, diagnostics, and epitope mapping. These are often synthetic peptides or recombinant proteins that mimic natural epitopes.
Enzyme Conjugates (e.g., Horseradish Peroxidase, Alkaline Phosphatase): Frequently used with secondary antibodies in detection systems.
Membrane Proteins and Lipids: In the case of antibodies like 10E8, 2F5, and 4E10, membrane lipids are critical co-factors for HIV neutralizing activity.
Streptavidin/Biotin Systems: Used to amplify detection signals in immunoassays.
IgG, F(ab)?, and Fab Fragments: Commonly used to study antigen binding without effector functions or for specific detection in assays.
Application Areas
Structural Biology: Studies on antibody–peptide complexes, such as those cited above, focus on how antibodies recognize and bind peptides, often revealing mechanisms of cross-reactivity and conformational variability.
Diagnostics: Antibodies are used in ELISA, IHC, flow cytometry, and Western blotting, often in combination with secondary antibodies and enzyme conjugates.
Therapeutics: Monoclonal antibodies, antibody–drug conjugates, and polyclonal preparations are used for treating cancers, autoimmune diseases, and infectious diseases.
Used for structure-function studies, diagnostics, therapeutics
Polyclonal Antibodies
Anti-toxins, Rh(D) Ig
Used in prophylaxis and therapy
Secondary Antibodies
HRP, AP, Alexa Fluor, DyLight, Cy, Biotin
Used in immunoassays for signal detection
Fusion/Artificial Proteins
Engineered peptides, recombinant antigens
For immunization and epitope mapping
Enzyme Conjugates
HRP, AP
Signal amplification in assays
Membrane Proteins/Lipids
Involved in MPER antibody activity
Critical for certain neutralizing antibodies
Biotin/Streptavidin
Used in detection systems
Signal amplification
Key Points
Monoclonal antibodies and engineered peptides are central to studies of antibody–antigen interactions, including cross-reactivity and conformational binding.
Secondary antibodies conjugated to enzymes or fluorophores are ubiquitous in immunoassays.
Membrane proteins and lipids can be critical for the activity of certain antibodies, especially in viral contexts.
Recombinant and polyclonal antibodies are widely used in diagnostics and therapeutics.
If 1-2 refers to a specific antibody pair or a published set of antibodies, please clarify for a more targeted answer. The above covers the most common and relevant proteins and antibodies referenced in antibody research literature.
Key findings from two representative scientific citations about "clone" focus on both laboratory cloning techniques and issues related to "cloned journals":
In-house Production and Efficiency of Cloning Vectors: A study demonstrated that a self-made pJET1.2/blunt cloning vector enables efficient, low-cost, and high-fidelity cloning of DNA fragments of varying sizes, comparable to commercial alternatives. The process is straightforward, does not require phosphorylation before ligation, and significantly simplifies DNA cloning workflows in molecular biology labs.
Authors' Motivations and Awareness in Cloned Journal Publications: Research into "cloned journals" (unauthorized copies of reputable journals) found that 79% of surveyed authors agreed with multiple reasons for publishing in these journals, the most common being low-cost open access (86% agreement). Strikingly, a similar proportion were aware of the negative consequences, including hampering scientific progress (69% agreement), yet many still pursued such publications for academic credit.
These findings highlight major issues in both practical cloning methods and the ethics of journal cloning in scientific communication.
Dosing regimens for clone 1-2 antibodies in mouse models can vary depending on the mouse strain, disease model, and experimental objectives, but specific details about clone 1-2 are not available in the provided search results. In general, antibody dosing strategies are tailored to optimize efficacy, pharmacokinetics, and immune response based on the mouse model and the type of antibody or therapeutic agent used.
General context from antibody and drug dosing regimens in mice:
Standard antibody doses for common clones (e.g., anti-PD-1, anti-PD-L1) typically range from 100 to 500 ?g per mouse per dose, with intraperitoneal injection as a common route.
Dosing intervals may be every 3–4 days or several times per week, with schedules adjusted for pharmacodynamics and expected immune response.
In pharmacokinetic studies involving model-based humanized regimens, total daily doses can be as high as 117 mg/kg/day, split into multiple smaller doses throughout the day to compensate for the shorter half-life in mice. Doses may be further adjusted depending on the disease context (bloodstream vs. lung infection models), animal weight, and anticipated volume of distribution.
How regimens vary:
Strain differences: Dosing may be adjusted based on mouse strain differences in metabolism, immune response, or size.
Disease models: Dosing is sometimes higher or more frequent in infection or cancer models to achieve target drug exposure or immune modulation.
Type of clone and antibody: The optimal dose and schedule depend on whether the antibody is blocking, depleting, or agonistic, and on its target.
Key variables in adjusting regimens:
Mouse weight: Dose is often normalized per kg.
Injection route: Intraperitoneal is common for antibodies; intravenous, subcutaneous, or oral for some drugs.
Target exposure: Regimens are sometimes designed to match human pharmacokinetic profiles by modeling drug distribution and clearance in mice.
Scheduling: Splitting doses may be necessary for compounds with short half-lives.
Since none of the results specifically detail clone 1-2, these general principles from in vivo antibody dosing guides can be applied to experimental design with clone 1-2, with further adjustment according to published data or preliminary titration.
If more specific clone 1-2 information is needed, consulting targeted publications or supplier protocols is recommended, as regimens for particular clones may have unique optimization guidelines.
References & Citations
1.) Shin, Haina et al. (2018) J Virol. 92(7): e00038-18. PubMed
2.) Hawman DW, et al. (2021) Microorganisms 9(2):279 Journal Link