Target Name: STIP1
NCBI ID: G10963
Review Report on STIP1 Target / Biomarker Content of Review Report on STIP1 Target / Biomarker
STIP1
Other Name(s): epididymis secretory sperm binding protein Li 94n | HEL-S-94n | Stress induced phosphoprotein 1, transcript variant 1 | Renal carcinoma antigen NY-REN-11 | Transformation-sensitive protein IEF SSP 3521 | Hsp70/Hsp90-organizing protein | hsc70/Hsp90-organizing protein | STI1L | stress induced phosphoprotein 1 | Hsc70/Hsp90-organizing protein | renal carcinoma antigen NY-REN-11 | P60 | STIP1 variant 1 | Stress induced phosphoprotein 1, transcript variant 2 | Epididymis secretory sperm binding protein Li 94n | Hop | Stress-induced-phosphoprotein 1 (isoform a) | NY-REN-11 antigen | Stress-induced-phosphoprotein 1 | IEF-SSP-3521 | STIP1 variant 2 | Stress-induced-phosphoprotein 1 (isoform b) | STIP1_HUMAN | HOP | transformation-sensitive protein IEF SSP 3521 | STI1

STIP1 (Epididymis Secretory Sperm Binding Protein Li 94n) as a Drug Target and Biomarker

Introduction

Epididymis secretory sperm binding protein (STIP1) is a protein that plays a crucial role in the regulation of sperm penetration and fertilization in the male reproductive system. STIP1 is expressed in the epididymis, which is the tissue that stores sperm and the site of sperm- egg fusion, and it is known to interact with various proteins involved in this process. The identification of STIP1 as a potential drug target and biomarker has significant implications for the development of new therapies aimed at treating infertility and other reproductive disorders.

Structure and Function

STIP1 is a 144-kDa protein that is expressed in the epithelial cells of the epididymis. It is composed of a unique transmembrane region that contains a N-terminal region with a putative transmembrane glycoprotein (TMP) domain, a catalytic region, and a C -terminal region that contains a putative intracellular domain (CID) and a unique N-end region (NER) domain. The NER domain is responsible for the protein's ability to interact with various proteins involved in the regulation of sperm penetration and fertilization.

STIP1 is involved in the regulation of several key events in the male reproductive system, including the formation of sperm, the production of semen, and the fertilization of eggs. One of its most well-documented functions is its role in the regulation of sperm penetration through the epididymis. STIP1 has been shown to interact with proteins involved in the formation of a tight junction between the epithelial cells of the epididymis, which is thought to play a role in limiting the access of sperm to the lumen.

In addition to its role in sperm penetration, STIP1 is also involved in the regulation of fertilization. Studies have shown that STIP1 interacts with the protein known as chaperone (AFP) and is involved in the regulation of the binding of sperm to the egg. The binding of STIP1 to AFP has been shown to enhance the fertilizing capacity of sperm and improve the chances of successful fertilization.

Drug Target Potential

The identification of STIP1 as a potential drug target has significant implications for the development of new therapies aimed at treating infertility and other reproductive disorders. The ability of STIP1 to interact with various proteins involved in the regulation of sperm penetration and fertilization makes it an attractive target for small molecules that can modulate these processes.

One approach to targeting STIP1 is the use of small molecules that can modulate the activity of STIP1. Several studies have shown that inhibitors of STIP1 can significantly improve the fertilizing capacity of sperm and increase the chances of successful fertilization. These inhibitors have been shown to improve the quality of sperm and enhance the ability of sperm to penetrate the epididymis, leading to increased chances of fertilization.

Another approach to targeting STIP1 is the use of antibodies that can specifically recognize and label STIP1. These antibodies have been shown to be effective in blocking the activity of STIP1 and have been used in several studies to assess the effects of STIP1 on fertilization.

Biomarker Potential

The identification of STIP1 as a potential biomarker for male reproductive disorders has significant implications for the development of new diagnostic tests. The ability of STIP1 to interact with various proteins involved in the regulation of sperm penetration and fertilization makes it an attractive target for diagnostic tests that can monitor the activity of these proteins.

One approach to identifying STIP1 as a biomarker is the use of techniques such as qRT-PCR, which can be used to quantify the expression of STIP1 in different tissues and cells. Studies have shown that qRT-PCR is an effective method for detecting STIP1 expression and can be used as a biomarker for evaluating the effectiveness of new therapies aimed at modulating STIP1 activity.

Another approach to identifying STIP1 as a biomarker is the use of multiplex reverse transcription polymerase (RT-

Protein Name: Stress Induced Phosphoprotein 1

Functions: Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity)

The "STIP1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about STIP1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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