BAG3 Human

BCL2-Associated Athanogene 3 Human Recombinant
Cat. No.
BT23162
Source
Escherichia Coli.
Synonyms
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
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
Quick Inquiry

Description

BAG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 595 amino acids (1-575 a.a.) and having a molecular mass of 63.7 kDa. The BAG3 protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques.

Product Specs

Introduction
BAG3, a member of the BAG family, functions as a nucleotide exchange factor for HSP70/HSC70, promoting substrate release and inhibiting their chaperone activity. This protein exhibits anti-apoptotic properties. BAG proteins, including BAG3, cooperate with Hip to bind to the ATPase domain of Hsc70/Hsp70, facilitating substrate release. While all BAG proteins share a conserved BAG domain of approximately 45 amino acids near their C-terminus, they display significant variation in their N-terminal regions. BAG3 possesses a WW domain at its N-terminus and the characteristic BAG domain at its C-terminus. The BAG domains of BAG1, BAG2, and BAG3 specifically interact with the Hsc70 ATPase domain both in vitro and in mammalian cells. They exhibit high affinity binding to this domain, inhibiting Hsc70's chaperone activity in a Hip-repressible manner. BAG3 acts as a protein-refolding cochaperone, and its expression is upregulated in response to prolonged cellular stress caused by calcium balance dysregulation. Notably, BAG3 has demonstrated the ability to mitigate stress-induced apoptosis.
Description
This product consists of recombinant human BAG3 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain encompassing 595 amino acids (residues 1-575) with a molecular weight of 63.7 kDa. A 20 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved through standard chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The BAG3 protein is supplied in a buffer consisting of 20mM Tris (pH 8), 1mM EDTA, 10% glycerol, and 0.1mM PMSF.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage periods. Repeated freezing and thawing should be avoided.
Purity
The purity of the BAG3 protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP.

Product Science Overview

Structure and Function

BAG3 is composed of several functional domains:

  • BAG Domain: This domain is responsible for binding to Hsp70/Hsc70, thereby regulating their chaperone activity.
  • WW Domain: This domain mediates protein-protein interactions and is involved in signaling pathways.
  • Proline-Rich Region: This region is important for interactions with SH3 domain-containing proteins.

BAG3 is primarily localized in the cytoplasm but can also be found in the nucleus under certain conditions. It is involved in the regulation of apoptosis by interacting with BCL2, an anti-apoptotic protein, and modulating its activity. BAG3 also plays a role in autophagy, a cellular process that degrades and recycles damaged organelles and proteins.

Role in Disease

BAG3 has been implicated in various diseases, particularly in cancer and neurodegenerative disorders. In cancer, BAG3 is often overexpressed and contributes to tumor cell survival, proliferation, migration, and invasion. For example, in colorectal cancer, BAG3 has been shown to promote tumor cell proliferation, migration, invasion, and chemoresistance . In pancreatic ductal adenocarcinoma, BAG3 enhances tumor growth by activating the mitogen-activated protein kinase (MAPK) signaling pathway .

In neurodegenerative diseases, BAG3 is involved in the clearance of misfolded proteins and the maintenance of cellular homeostasis. Mutations in the BAG3 gene have been associated with myofibrillar myopathy, a muscle disorder characterized by the accumulation of protein aggregates in muscle fibers.

Therapeutic Potential

Given its role in various diseases, BAG3 is considered a potential therapeutic target. In cancer, targeting BAG3 could inhibit tumor growth and enhance the effectiveness of chemotherapy. In neurodegenerative diseases, enhancing BAG3 activity could promote the clearance of misfolded proteins and protect against cellular stress.

Human Recombinant BAG3

Human recombinant BAG3 is a form of the protein that is produced using recombinant DNA technology. This involves inserting the BAG3 gene into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. Recombinant BAG3 can be used in research to study its function and interactions with other proteins, as well as in drug development to screen for potential inhibitors or activators.

In conclusion, BCL2-Associated Athanogene 3 is a multifunctional protein with significant roles in apoptosis, autophagy, and cellular stress responses. Its involvement in various diseases makes it a promising target for therapeutic interventions.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

Related Products

BAG1 Human
BCL2-Associated Athanogene 1 Human Recombinant
Cat. No.
BT23030
Source
Escherichia Coli.
BAG2 Human
BCL2-Associated Athanogene 2 Human Recombinant
Cat. No.
BT23111
Source
Escherichia Coli.
THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.