MUC16 Human

Mucin-16 (CA125) Human
Cat. No.
BT2414
Source

Human carcinoma cell line.

Synonyms
Appearance

Clear colorless to pale blue frozen solution.

Purity

Greater than 60%.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

The Human Mucin-16 (CA125) was purified from Human carcinoma cell line.

Product Specs

Introduction
MUC16, also known as CA125, is a mucin protein that can exist in either a type I transmembrane or secreted form. These forms are utilized to track the effectiveness of epithelial ovarian cancer treatments. The CA125 molecule exhibits heterogeneity in terms of size and charge, likely due to the ongoing deglycosylation of its side chains throughout its existence in bodily fluids. MUC16 is most likely a glycoprotein primarily composed of O-linkages.
Description
This Human Mucin-16 (CA125) was extracted and purified from a human carcinoma cell line.
Physical Appearance
The product appears as a clear solution, either colorless or pale blue, in a frozen state.
Formulation
MUC16 is provided in a solution of 0.05M sodium phosphate buffer with a pH of 7.5, containing 0.09% NaN3 and 0.15M NaCl.
Stability
While Human MUC16 remains stable at 4°C for up to 1 week, it is recommended to store it at -20°C for long-term preservation.
Purity
The purity of this product exceeds 60%.
Human Virus Test
The tissue sample used in the production of this product has undergone rigorous testing and is confirmed negative for HIV-1 & 2 antibodies, HBsAg (Hepatitis B surface antigen), and Hepatitis-C antibodies.
Source

Human carcinoma cell line.

Product Science Overview

Introduction

Mucin-16, also known as CA125, is a high-molecular-weight glycoprotein encoded by the MUC16 gene. It is a member of the mucin family, which comprises glycoproteins produced by epithelial cells to protect and lubricate the surfaces of various organs. MUC16 is particularly significant due to its role as a biomarker for ovarian cancer .

Structure

MUC16 is the largest membrane-associated mucin, consisting of more than 22,000 amino acids . It is composed of three distinct domains:

  1. N-terminal domain: This domain is entirely extracellular and highly O-glycosylated.
  2. Tandem repeat domain: This domain contains repeating amino acid sequences rich in serine, threonine, and proline.
  3. C-terminal domain: This domain includes multiple extracellular SEA (sea urchin sperm protein, enterokinase, and agrin) modules, a transmembrane domain, and a cytoplasmic tail .

The extracellular region of MUC16 can be released from the cell surface through proteolytic cleavage, which is thought to occur at a site within the SEA modules .

Function

MUC16 is expressed on the ocular surface, respiratory tract, and female reproductive tract epithelia. Its high glycosylation creates a hydrophilic environment that acts as a lubricating barrier against foreign particles and infectious agents on the apical membrane of epithelial cells . Additionally, the cytoplasmic tail of MUC16 interacts with the cytoskeleton by binding to members of the ERM protein family .

Clinical Significance

MUC16 is best known for its application as a tumor marker, particularly in ovarian cancer. Elevated levels of CA125 in the blood can indicate the presence of ovarian cancer or other conditions, both malignant and benign . The identification of CA125 as MUC16 has led to various studies investigating its expression, functional, and mechanistic involvement in multiple cancer types .

Therapeutic Implications

Efforts have been made to develop MUC16-targeted therapies, primarily using antibodies against the tandem repeat domains of MUC16. However, these approaches have met with limited success . Recent studies have focused on disrupting the functional cooperation of MUC16 and its interacting partners, such as using a novel immunoadhesin HN125 to interfere with MUC16 binding to mesothelin .

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