INPPL1 Antibodies

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (INPPL1)

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to generate PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear.

While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence doesn't affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity.

Gene Information

Human
Gene Name:	INPPL1
Uniprot:	O15357
Entrez:	3636

Family

Belongs to:
inositol 1,4,5-trisphosphate 5-phosphatase family

Alternative Names

EC 3.1.3; EC 3.1.3.n1; inositol polyphosphate phosphatase-like 1; Inositol polyphosphate phosphatase-like protein 1; INPPL1; INPPL-1; phosphatidylinositol-34,5-trisphosphate 5-phosphatase 2; Protein 51C; SH2 domain-containing inositol phosphatase 2; SH2 domain-containing inositol-5'-phosphatase 2; SHIP2; SHIP-2; SHIP251C protein

Molecular Weight

Mass (kDA):
138.599 kDA

Genomic Context

Human
Location:	11q13.4
Sequence:	11; NC_000011.10 (72223861..72239147)

Tissue Specificity

Widely expressed, most prominently in skeletal muscle, heart and brain. Present in platelets. Expressed in transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes.

Subcellular Localizations

Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, lamellipodium. Nucleus. Nucleus speckle. Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cyt

Diseases

• Diabetes Mellitus
• Neoplasms
• Diabetes Mellitus, Non-insulin-dependent
• Leukemia
• Tissue Adhesions
• Insulin Resistance
• Malignant Neoplasms
• Insulin Sensitivity
• Obesity
• Myeloid Leukemia
• Autoimmunity
• Inflammation
• Myeloid Leukemia, Chronic

• Autoimmune Reaction
• Lymphoma
• Fibromyalgia
• Leukemia, Myelocytic, Acute
• Leukemogenesis
• Atherosclerosis
• Hypertensive Disease

Interacting Proteins

• AR
• BCAR1
• EPHA2
• GAB1
• HID1

• MET
• SORBS1

Pathways

• Cell Activation
• Localization
• Cell Proliferation
• Cell Growth
• Pathogenesis
• Mast Cell Degranulation
• Mast Cell Activation
• Cell Cycle
• Secretion
• Cell Adhesion
• Cytokine Production
• Cell Death
• Cell Migration

• Phagocytosis
• Cell Development
• Immune Response
• Endocytosis
• B Cell Activation
• Macrophage Activation
• Hypersensitivity

PTMs

• Phosphorylation
• Dephosphorylation
• Cleavage

• Reduction
• Biotinylation
• Ubiquitination

• Myristoylation

Research Areas

• Immune System Diseases
• Immunology
• Innate Immunity

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/INPPL1

Boster Bio - Best Uses Of The INPPL1 Marker

In this article we will discuss Boster Bio and its products: High-affinity primary antibodies, INPPL1 marker, and the INPPL1 antibody. These products can be used in a variety of applications, from diagnostics to drug discovery. We will also discuss Boster Bio's reputation and future plans. Read on to learn more! Let's get started! Steven Boster was a PhD student at the University of Texas at Austin when he developed his first product in 1993. His products for this discipline included hundreds of primary antibodies. By the late 1990s, his company was the largest catalog antibody manufacturer in China. Today, Steven Boster is the president and CEO of Boster Bio, the world's leading provider of high-sensitivity ELISA kits.

High-affinity primary antibodies

This study was conducted on the use of high-affinity primary antibodies that utilize the INPPL1 marker as a biomarker for antibody internalization. Incubated with scFv-Fc proteins, serum-starved U2OSR1 cells were washed in PBS and HSLP buffer (2 M NaCl, 40 mAc, pH 4.0). Next, cells were fixed with 4% PFA and permeabilized using 0.1% Triton X-100 in PBS.

Detection of SHIP2 in immersion-fixed paraffin-embedded sections of breast cancer tissue was performed using a 3 ug/mL antibody and 1 hour at room temperature. DAB and hematoxylin were used for visualization. SHIP2 was detected in cancer cells localized to the cytoplasm. High-affinity primary antibodies using the INPPL1 marker were developed to detect SHIP2.

The INPPL1 marker is a unique immunoglobulin molecule that is present on most cells. It is found in primary macrophages, platelets, and transformed myeloid cells but not in peripheral blood monocytes. Hence, the use of this biomarker to identify the antigens in tumor cells is important for targeting immunotherapy. If the antigens are identified correctly, the antibodies can be targeted to specific tissues.

The INPPL1 gene is controlled by the transcription factor Sp1 in GC cells. Overexpression of the gene results in amplification of DNA fragments. The DNA fragments were amplified using PCR and Western blot analysis. The data shown are representative of three independent experiments. The data presented were normalized to the levels of INPPL1 in input DNA. All bands were quantified using NIH Image J and the values shown are representative of 3 experiments.

By internalizing engineered antibodies, the engineered antibody is likely to be effective against FGFR1-overproducing tumor cells. This research may also aid the design of targeting molecules for ADCs. With the use of these antibodies, cancer treatments may become a reality. With the help of engineered antibodies, the immune system can target cancer cells and improve the quality of life of its patients.

In addition to detecting IgG-a/B cell activation, SHIP also inhibits the activity of the BCR. In addition, SHIP can interact directly with the FcgRIIB ITIM through its SH2 domain. This interaction is required for the inhibitory function of FcgRIIB, but it requires other proteins to form a stable complex. It also contributes to negative regulation of the IgG receptor.

INPPL1 marker

The INPPL1 gene is one of the most frequently mutated genes in human cancer cells. Its mutation is often associated with BRAF, NRAS, or HRAS. Other mutations found in tumor cells include DNAh20, FCGRT, and OTUD4.