Protein sprouty homolog 2 Antibodies

Protein sprouty homolog 2 (SPRY2)

May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis. .

Gene Information

Human
Gene Name:	SPRY2
Uniprot:	O43597
Entrez:	10253

Family

Belongs to:
sprouty family

Alternative Names

hSPRY2; MGC23039; protein sprouty homolog 2; sprouty (Drosophila) homolog 2; sprouty 2; sprouty homolog 2 (Drosophila); SPRY2; spry-2

Molecular Weight

Mass (kDA):
34.688 kDA

Genomic Context

Human
Location:	13q31.1
Sequence:	13; NC_000013.11 (80335976..80341126, complement)

Subcellular Localizations

Cytoplasm, cytoskeleton. Cell projection, ruffle membrane. Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated ith EGF (epidermal growth factor).

Diseases

• Neoplasms
• Malignant Neoplasms
• Cell Transformation, Neoplastic
• Carcinoma
• Cell Invasion
• Malignant Paraganglionic Neoplasm
• Tumor Angiogenesis
• Liver Carcinoma
• Malignant Tumor Of Colon
• Colonic Neoplasms
• Adenocarcinoma
• Carcinogenesis
• Hyperplasia

• Liver Neoplasms
• Melanoma
• Hypoxia
• Lung Neoplasms
• Lymphoma
• Tissue Adhesions
• Prostatic Neoplasms

Pathways

• Cell Proliferation
• Cell Migration
• Cell Growth
• Lung Development
• Angiogenesis
• Cell Death
• Localization
• Pathogenesis
• Endocytosis
• Methylation
• Regeneration
• Cell Cycle
• Lung Morphogenesis

• Lung Growth
• Secretion
• Cell Adhesion
• Cell Differentiation
• Oocyte Maturation
• Reverse Transcription
• Muscle Cell Proliferation

PTMs

• Phosphorylation
• Ubiquitination
• Methylation
• Dephosphorylation

• Cleavage
• Nitrosylation
• Hydroxylation
• Palmitoylation

Research Areas

• Growth and Development
• Neuronal Cell Markers
• Signal Transduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SPRY2

Best Uses of the SPRY2 Marker

What is the Boster Bio Anti-Spry-2/SPRY2Marker? This article will address the applications, validation, ICC and characterization of this versatile marker. This article will also provide a brief overview of the SPRY2 Antigen. ICC is an international standard for the measurement of a protein's affinity for its target. This marker can both be used for quantitative and qualitative analysis.

Boster Bio Anti-Spry-2/SPRY2 Marker

The Boster Bio Anti-Spry-2/ SPRY2 Marker is a highly specific and sensitive antibody for detecting Protein sprouty homolog 1. It reacts with EGF-stimulated cells and was developed in the Mouse and Rabbit species. There are many types of Boster Bio Antibodies. The monoclonal Boster Antibody and the polyclonal Boster Antibody are two types.

A recent study investigated the effects of miR-21-5p on Spry1 expression. It was found that mice with reduced Spry1 expression had a lower likelihood of TMJ-related cartilage destruction than wild type mice. The study was conducted in an established TMJOA system. It was found that miR-21-5p inhibits Spry1 transcription, leading to increased MMP-13 and VEGF expression, as well as phosphorylation of ERKMAPK signalling pathway components.

Validation

We have validated the SPRY2 marker using multiple tissues and applications. Our results show upregulation of SPRY2 in Gag-specific T cells and M-1-specific T cells, but not in nonspecific CD8+ T cells. These results suggest that SPRY2-positive cell are less polyfunctional ex vivo. This will be discussed further in the following section. The validation of SPRY2 was conducted using two separate antibodies, one for WB and one for IP.

First, we tested the effects of SPRY2 inhibition upon HIV-specific T cell lines. We found that reducing SPRY2 expression in HIV-specific T cells enhanced polyfunctionality of T cells. To test this, we sorted PBMCs derived from seven HLA+-A2-positive subjects into Gag-specific CTL. These results were then compared to those of M1specific CTL. The HIV-specific polyfunctionality of HIV-specific T cells was correlated to the upregulation in SPRY2.

We also found that SPRY2 knockdown didn't have any effect on CD107a or MIP-1b levels. We also found that virus-transduced t cells with SPRY2 knockdown had significantly higher levels of polyfunctional T cells than control-transduced t cells. This result was consistent to previous findings. The SPRY2 knockdown virus decreased the MFI of SPRY2 in CD8+ T cells compared with control-transduced T cells.

Applications

Sprouty2, an feedback regulator of receptor-tyrosine kinase kinase signals, has been shown to be associated with cell proliferation as well as drug resistance in glioblastoma cells. However, the precise mechanisms involved in SPRY2's involvement in GBM remain poorly understood. We therefore analyzed the expression of SPRY2 using publicly available databases. The effects of RNA interference targeting SPRY2 in cell proliferation was compared in GBM stemlike cells from patients and GBM established cells. We also evaluated the role of SPRY2 for both loss and gain-function in xenografts.

SPRY2 expression was greater in GBMs than in normal brain tissues. SPRY2 knockdown significantly reduced cell proliferation in GBM and normal Astrocytes. Furthermore, silencing of SPRY2 led to an increase in ERK activation and DNA replica stress in GBM cells. In xenograft bearing mice, SPRY2 function was also inhibited. The expression of SPRY2 protein and mRNA levels in GBM patients was well correlated.

The expression of SPRY2 genes is upregulated in CD8+ cells during high-antigen stimulation. However, it does not affect CD107a or MIP-1b production. Additionally, SPRY2 knockdown reduces the number of polyfunctional cells. This effect is dependent on the ERK/MAPK pathway. SPRY2 is an effective tool for cancer immunotherapy. It is available in many versions.

SPRY2 is expressed by HIV-specific T cells. This is how HIV-specific cells have low levels of polyfunctionality. To test this hypothesis, we isolated PBMCs form seven HLA A2-positive patients. We then compared their CD8+ responses. We found that CD8+ T cell responses to HIV-specific immune reactions were more potent when high levels of SPRY2 expression was observed than those with low levels.

ICC

Although SPRY2 has been used in ICCs, its clinical relevance remains unclear. It is an essential modulator in the FGF–FGFR4–ERK pathway. But how does SPRY2 interact and interact with FGFR2 What is the clinical relevance of this gene, and how does it interact with FGFR2? We will examine the evidence regarding the clinical significance of SPRY2-containing tumors. SPRY2 was originally used to identify tumors within mice in 1996. It is also used for distinguishing a subset cancer cells from paired normal tissue.

SPRY2 and SPRY4 are members of the Sprouty gene family. These genes are essential for the development of human embryonic cells stem cells. SPRY2 & 4 are the most expressed Sprouty gene in hESCs. Knockouts of either gene led to decreased cell proliferation and higher cell death. However, SPRY4 knockouts resulted is enhanced survival and differentiation. Both SPRY2KD cells and SPRY4KO cells had defects that resulted in cell membrane destruction and mitochondrial fusion.

The decrease in expression of Sprouty genes in AGS cells leads to an increase in RTK Signaling. The cells also exhibited altered sensitivity to growth factors, as SPRY2-KO cells induced significantly higher cell numbers in response to FGF2, while SPRY4-KO cells did not increase in number. These findings suggest that ICC uses for the SPRY2 marker might have therapeutic potential.

These experiments support previous studies showing that Spry2 is an excellent candidate marker for identifying hESCs. SPRY2 also has important clinical uses. It modulates biological reactions controlled by HIFasubunits. The SPRY2 marker has been identified as a key diagnostic determinant of breast cancer. However, further research is needed in order to fully understand how SPRY2 contributes to the development of hESCs.

Immunofluorescence

SPRY2 can be found in many tissues and cells. Its expression is regulated by miR-23b, a non-coding RNA that regulates the b-catenin/TCF4 signaling pathway. As an indicator of protein expression, it is detected with a PCR-based reverse transcription-quantitative PCR (RT-qPCR) technique. Primers were created to detect the target proteins E-cadherin and N-cadherin as well as vimentin and GAPDH.