SEPT5 Human

Septin-5 Human Recombinant
Cat. No.
BT22000
Source
Escherichia Coli.
Synonyms
Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta chain.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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.
Shipped with Ice Packs
In Stock

Description

SEPT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 45.2 kDa.
The SEPT5 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
SEPT5, a member of the septin family, is a nucleotide-binding protein originally identified in yeast for its role in cell division regulation. Highly conserved across yeast, Drosophila, and mice, septins appear to govern cytoskeletal organization. Disrupting septin function impairs cytokinesis, leading to a surge in multinucleated or polyploid cells.
Description
Recombinant human SEPT5, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 392 amino acids (residues 1-369) with a molecular weight of 45.2 kDa. This SEPT5 protein is fused to a 23-amino acid N-terminal His-tag and purified using proprietary chromatographic methods.
Physical Appearance
A clear, sterile solution.
Formulation
The SEPT5 protein is supplied at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8), 0.3 M NaCl, 1 mM DTT, and 40% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90% as determined by SDS-PAGE analysis.
Synonyms
Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta chain.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSTGLRY KSKLATPEDK QDIDKQYVGF ATLPNQVHRK SVKKGFDFTL MVAGESGLGK STLVHSLFLT DLYKDRKLLS AEERISQTVE ILKHTVDIEE KGVKLKLTIV DTPGFGDAVN NTECWKPITD YVDQQFEQYF RDESGLNRKN IQDNRVHCCL YFISPFGHGL RPVDVGFMKA LHEKVNIVPL IAKADCLVPS EIRKLKERIR EEIDKFGIHV YQFPECDSDE DEDFKQQDRE LKESAPFAVI GSNTVVEAKG QRVRGRLYPW GIVEVENQAH CDFVKLRNML IRTHMHDLKD VTCDVHYENY RAHCIQQMTS KLTQDSRMES PIPILPLPTP DAETEKLIRM KDEELRRMQE MLQRMKQQMQ DQ

Product Science Overview

Introduction

Septin-5 is a member of the septin family of GTP-binding proteins, which are highly conserved across species, including yeast, Drosophila, and mammals . Septins play crucial roles in various cellular processes, such as cytokinesis, cell polarity, and vesicle trafficking. Septin-5, in particular, has been implicated in the regulation of cytoskeletal organization and neurotransmitter release.

Gene and Protein Structure

The SEPTIN5 gene encodes the Septin-5 protein, which is involved in several cellular pathways, including the regulation of activated PAK-2p34 by proteasome-mediated degradation and ERK signaling . The gene is located on chromosome 22q11.2, a region associated with DiGeorge syndrome and other developmental disorders .

Function and Mechanism

Septin-5 is known to interact with other septin proteins to form hetero-oligomeric complexes that can assemble into filaments and higher-order structures. These structures are essential for maintaining cell shape, polarity, and intracellular transport. In neurons, Septin-5 is involved in the regulation of synaptic vesicle exocytosis, which is critical for neurotransmitter release .

Clinical Significance

Mutations or dysregulation of the SEPTIN5 gene have been associated with various neurological disorders. For instance, autoantibodies targeting Septin-5 have been identified in patients with autoimmune cerebellar ataxia, a condition characterized by loss of balance, incoordination, and eye movement abnormalities . This autoimmune response can lead to significant neurological impairment, but some patients have shown improvement with immunotherapy .

Recombinant Septin-5

Recombinant human Septin-5 is produced using molecular cloning techniques, where the SEPTIN5 gene is inserted into an expression vector and introduced into a host cell system, such as E. coli or mammalian cells. The recombinant protein is then purified for use in various research applications, including studies on protein-protein interactions, cellular signaling pathways, and the development of therapeutic interventions .

Research and Applications

Research on Septin-5 has provided valuable insights into its role in cellular processes and its potential as a therapeutic target. Studies have shown that Septin-5 is involved in the regulation of neurotransmitter release, making it a potential target for treating neurological disorders . Additionally, the use of recombinant Septin-5 in research has facilitated the study of its structure and function, contributing to our understanding of septin biology and its implications in health and disease .

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