SH3GLB2 Human

SH3-domain GRB2-like endophilin B2 Human Recombinant
Cat. No.
BT26012
Source
E.coli.
Synonyms
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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.
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Description

SH3GLB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a.) and having a molecular mass of 46.4 kDa. SH3GLB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Endophilin-B2, also known as SH3GLB2, is a protein that belongs to the endophilin B family. Endophilins, including SH3GLB2, are associated with proteins like amphiphysin, synaptojanin, and dynamin, playing a role in the trafficking of presynaptic vesicles at nerve terminals. The expression patterns of endophilins align with their functions at neuronal synapses. SH3GLB2 is expressed ubiquitously, with the highest levels found in the brain, adult lung, ovary, and spinal cord. Notably, reduced levels of SH3GLB2 are observed in Down syndrome, potentially indicating brain dysgenesis.
Description
Recombinant SH3GLB2 (human origin) is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain encompassing 418 amino acids (residues 1-395a.a.) with a molecular weight of 46.4 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The SH3GLB2 protein solution is provided at a concentration of 0.5 mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 30% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 2-4 weeks), keep refrigerated at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freezing and thawing.
Purity
Purity exceeds 85.0% as assessed by SDS-PAGE analysis.
Synonyms
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDFNMKK LASDAGIFFT RAVQFTEEKF GQAEKTELDA HFENLLARAD STKNWTEKIL RQTEVLLQPN PSARVEEFLY EKLDRKVPSR VTNGELLAQY MADAASELGP TTPYGKTLIK VAEAEKQLGA AERDFIHTAS ISFLTPLRNF LEGDWKTISK ERRLLQNRRL DLDACKARLK KAKAAEAKAT TVPDFQETRP RNYILSASAS ALWNDEVDKA EQELRVAQTE FDRQAEVTRL LLEGISSTHV NHLRCLHEFV KSQTTYYAQC YRHMLDLQKQ LGRFPGTFVG TTEPASPPLS STSPTTAAAT MPVVPSVASL APPGEASLCL EEVAPPASGT RKARVLYDYE AADSSELALL ADELITVYSL PGMDPDWLIG ERGNKKGKVP VTYLELLS.

Product Science Overview

Gene and Protein Structure

The SH3GLB2 gene is located on chromosome 9q34.11 . The gene encodes a protein that consists of 395 amino acids . The structure of SH3GLB2 includes:

  • An N-terminal domain
  • A central coiled-coil region
  • A C-terminal SH3 domain

The SH3 domain is crucial for protein-protein interactions, allowing SH3GLB2 to bind to other proteins and participate in cellular signaling pathways .

Expression and Localization

SH3GLB2 is expressed in various tissues, including the brain, lung, colon, and mammary gland . It is predominantly found in the cytoplasm and nucleoplasm of cells . The expression patterns of SH3GLB2 are consistent with its roles in neuronal synapses and other cellular functions .

Function and Mechanism

SH3GLB2 plays a significant role in the regulation of endocytic vesicle trafficking and autophagosome formation . It is involved in the transport of vesicles to late endosomes or lysosomes, which are essential steps in the degradation and recycling of cellular components . Despite its similarities with endophilin B1, SH3GLB2 is not essential for mitochondrial apoptosis .

Clinical Significance

Mutations or dysregulation of SH3GLB2 have been associated with certain diseases, including:

  • Primary Ovarian Insufficiency 17
  • Primary Ciliary Dyskinesia 17

These associations highlight the importance of SH3GLB2 in maintaining normal cellular functions and its potential role in disease mechanisms.

Research and Applications

Recombinant SH3GLB2 is used in various research applications to study its function and interactions. It is produced using recombinant DNA technology, which allows for the expression of the protein in a controlled laboratory environment . This recombinant protein is valuable for biochemical studies, drug development, and understanding the molecular mechanisms underlying its functions.

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