Armenian Hamster IgG Isotype Control [Clone PIP] — Purified in vivo PLATINUM™ Functional Grade

Armenian Hamster IgG Isotype Control [Clone PIP] — Purified in vivo PLATINUM™ Functional Grade

Product No.: P376

[product_table name="All Top" skus="P376"]

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Clone
PIP
Formats AvailableView All
Product Type
Isotype Control
Isotype
IgG1
Applications
FC
,
in vivo

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Antibody Details

Product Details

Host Species
Armenian Hamster
Recommended Dilution Buffer
Product Concentration
≥ 5.0 mg/ml
Endotoxin Level
<0.5 EU/mg as determined by the LAL method
Purity
≥98% 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 multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
Pathogen Testing
To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUM™ antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.
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.
Applications and Recommended Usage?
Quality Tested by Leinco
FC 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 Armenian Hamster IgG isotype control antibody has been tested against selected species' cells and tissues to assure minimal cross reactivity. Furthermore, this Low Endotoxin Functional Formulation, PLATINUM antibody is suitable for in vivo application and each lot is IMPACT I certified.

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.

Clone PIP is commonly used as an Armenian Hamster IgG isotype control antibody in in vivo experiments in mice, as well as to study the roles of the prolactin-inducible protein (PIP) in various biological processes.

Key in vivo applications of clone PIP in mice include:

  • Isotype Control in Antibody Studies: Clone PIP is widely used as a negative control in immunological experiments involving antibodies. Because it lacks specificity to mouse antigens and has minimal cross-reactivity, it helps distinguish non-specific background signals from specific antibody interactions. This is critical for validating the specificity of primary antibody binding in flow cytometry, histology, and other immune assays.

  • Investigating PIP Functions: Clone PIP is used experimentally to explore the biological functions of the prolactin-inducible protein in immunity, host defense, and cancer progression. Researchers utilize either PIP knockout mouse models or introduce PIP-expressing cell lines into syngeneic mice to assess the impact of PIP on tumor growth, immune modulation, and infection responses.

  • Syngeneic Tumor Models: By employing tumor models with cells that overexpress or lack PIP, researchers evaluate its role in tumor microenvironment dynamics and potential implications for cancer therapy and immunosurveillance.

Additional context:

  • Clone PIP as an isotype control is especially valued for its minimal cross-reactivity and matching IgG subclass, ensuring accurate interpretation of in vivo antibody-based experiments.
  • The background of this clone involves its lack of specificity to human, mouse, rat, or primate cell surface targets, making it suitable as a universal negative control in murine studies.

In summary, clone PIP’s core in vivo applications in mice are as a highly validated IgG isotype control and as an investigative tool for understanding the role of prolactin-inducible protein in immune responses, cancer, and host defense.

Commonly used antibodies or proteins with PIP in the literature depend heavily on the context—whether PIP refers to phosphatidylinositol phosphate(s) (usually phosphoinositides such as PI(4)P, PI(4,5)P2, etc.) or to prolactin-induced protein (also known as BRST-2, Gp17, or simply PIP). Both major usages have distinct sets of associated antibodies and proteins.


1. Phosphatidylinositol Phosphate (PIP) and Related Antibodies/Proteins

When PIP refers to phosphoinositides:

  • Anti-PIP antibodies (monoclonal and polyclonal) are often used alongside antibodies for other phosphoinositides, such as:
    • Anti-PI(4)P
    • Anti-PI(4,5)P2
    • Anti-cardiolipin (CL), due to cross-reactivity in certain clinical and biochemical assays
  • Phospholipid-associated proteins, frequently studied with PIP antibodies:
    • Phospholipase C (particularly PI-specific phospholipase C)
    • Phosphatidylinositol transfer proteins
    • Kinases and phosphatases that modify PIPs (e.g., PIP kinases/phosphatases)
    • PH domain-containing proteins (e.g., Akt, TAPP1) that bind to specific PIPs
    • Exocytosis and membrane trafficking proteins, such as CAPS, Munc13, and synaptotagmin1, which interact with PI(4,5)P2 during vesicle priming and secretion
  • Casein and phosphocholine are used in inhibition assays to study antibody specificity for phosphate moieties.

2. Prolactin-Induced Protein (PIP) and Related Antibodies/Proteins

When PIP refers to prolactin-induced protein, especially in cancer or breast biology:

  • Apoptosis-related proteins and their antibodies are commonly studied with anti-PIP:
    • CRADD, DAPK1, and CD40—these are markers and mediators of apoptotic signaling, often co-immunostained with PIP in tumor biology or cell death studies
  • Pan anti-JNK1/2 and tubulin antibodies are used as controls or for pathway studies in cellular experiments alongside anti-PIP
  • Antibodies targeting prolactin-induced protein (PIP) itself, such as:
    • Rabbit monoclonal anti-PIP (e.g., clone EP3810Y)
    • Commercial anti-PIP antibodies, often used in ELISA, immunofluorescence, and immunohistochemistry
  • Actin-binding proteins or cytoskeletal markers may sometimes be co-stained, given PIP’s alias as secretory actin-binding protein.

3. Other Relevant Antibody Combinations and Protein Partners

  • In experimental platforms (e.g., multiplexed immunoassays), PIP antibodies are paired with optimized antibody pairs for detection, sometimes using biotinylated secondary reagents and labeled streptavidin.
  • Markers of organelle identity and proteins linked to membrane trafficking can be detected in parallel with PIP antibodies to elucidate cellular localization and function.

Summary Table — Common Associated Antibodies/Proteins (by PIP context):

PIP ContextCommonly Used Antibodies/Proteins
Phosphoinositide PIPsAnti-PI(4)P, Anti-PI(4,5)P2, Anti-cardiolipin, phospholipase C, PI transfer proteins, kinases/phosphatases, PH domain proteins (Akt, TAPP1), casein/phosphocholine, synaptotagmin1, Munc13, CAPS
Prolactin-Induced ProteinAnti-PIP (e.g., clone EP3810Y), Anti-CRADD, Anti-DAPK1, Anti-CD40, Pan anti-JNK1/2, Anti-tubulin, actin-binding proteins

The most relevant antibodies or proteins used alongside PIP are selected based on biological pathway or experimental context, with those above representing the major groupings in published research.

The term "PIP" appears across diverse areas of scientific research, each with distinct key findings depending on the specific context. Here are the major discoveries from different PIP-related studies:

Plant Peptide Research

In plant biology, PIP (Plant Immunogenic Peptide) family research has revealed significant functional divergence between subfamilies. AtPIP1 demonstrates the strongest root growth inhibition activity, while AtPIP2 shows superior pathogen resistance capabilities. This functional distinction is partially attributed to the SGP motif, where proline hydroxylation modification enhances PIP function. The research suggests that AtPIP2 could potentially be used for crop protection in agricultural settings, as it induces immunity more efficiently without causing severe root growth penalties.

Breast Cancer Biology

Studies on Prolactin-Induced Protein (PIP) in breast cancer have uncovered its crucial role in regulating tumor cell proliferation. When PIP was silenced in luminal A breast cancer cells, researchers observed decreased phosphorylation of several key proteins including focal adhesion kinase (FAK), ephrin B3 (EphB3), FYN, and hemopoietic cell kinase. The PIP-activated gene network forms intricate connections with cMYC and cJUN, which serve as master transcriptional regulators of cell proliferation. Additionally, high PIP expression levels have been shown to sensitize breast cancer cells to anti-cancer drugs, enhancing treatment efficacy.

Microbial Pathogenesis

In bacterial research, the pip gene was identified as essential for producing the antifungal metabolite phenazine-1-carboxamide (PCN) in Pseudomonas chlororaphis. Mutants lacking functional pip failed to produce this important antimicrobial compound.

Pathotype Identification

The PIP-eco pipeline represents a genomic tool for E. coli pathotype identification, achieving a 70.9% assignment rate for single pathotypes and successfully identifying hybrid pathotypes in bacterial populations. This tool has proven particularly effective in detecting ExPEC/AIEC groups and their hybrid combinations with other pathotypes.

Currently, there is limited specific information available on how dosing regimens of clone PIP vary across different mouse models. However, general principles in dosing regimens for mouse models can be inferred from similar studies:

  1. Dosing Considerations: In mouse models, dosing regimens are often tailored to achieve specific pharmacokinetic (PK) profiles that mimic human conditions as closely as possible. This involves adjusting dosages based on factors like the drug's half-life, the desired concentration-time exposure, and the biological similarity between mice and humans.

  2. Examples from Similar Studies:

    • Paclitaxel: In models of paclitaxel-induced peripheral neuropathy, a dosing regimen of 2 mg/kg administered on days 1, 3, 5, and 7 is commonly used to replicate clinical symptoms.
    • Piperacillin: In studies involving piperacillin, dosages can vary significantly, with examples including 120 or 240 mg/kg administered intravenously at different frequencies.
  3. General Principles for Antibodies:

    • For antibodies like those targeting PD-1 or PD-L1, typical dosing ranges are between 100 to 500 μg per mouse, administered intraperitoneally, often every 3-4 days.
  4. Specific to Clone PIP:

    • The specific mention of "Clone PIP" does not provide direct dosing information in the search results. However, if "Clone PIP" refers to a specific antibody or protein, dosing regimens might follow similar intraperitoneal or intravenous administration routes and schedules found in immunological studies.

Without direct information on "Clone PIP," it is challenging to provide specific dosing regimens for this clone across different mouse models. It is essential to consult specific research articles or protocols related to "Clone PIP" for detailed dosing information.

References & Citations

1. Schreiber, RD. et al. (2017) Cancer Immunol Res. 5(2):106-117. PubMed
2. Oldstone, MBA. et al. (2017) Proc Natl Acad Sci U S A. 114(14): 3708–3713. PubMed
2. Schreiber, RD. et al. (2015) PLoS One.10(5):e0128636. PubMed
Flow Cytometry
in vivo Protocol

Certificate of Analysis

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Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.