SRM Human

Spermidine Synthase Human Recombinant
Cat. No.
BT25224
Source
Escherichia Coli.
Synonyms
Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

SRM Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (1-302 a.a.) and having a molecular mass of 36kDa. The SRM is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Spermidine synthase (SRM) is an enzyme that plays a crucial role in the biosynthesis of spermidine, a polyamine involved in cell growth and differentiation. SRM catalyzes the transfer of a propylamine group from S-adenosylmethioninamine to putrescine, completing the final step in spermidine synthesis. Polyamines like putrescine, spermine, and spermidine are essential for various cellular processes.
Description
Recombinant human spermidine synthase (SRM) is a purified protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 322 amino acids (with a 20 amino acid His tag at the N-terminus) and has a molecular weight of 36 kDa. The protein is purified using proprietary chromatographic techniques and is greater than 95% pure as determined by SDS-PAGE.
Physical Appearance
The product is a sterile, colorless solution.
Formulation
The SRM solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 10% glycerol, 2mM DTT, and 0.1M NaCl.
Stability
For short-term storage (2-4 weeks), store the solution at 4°C. For longer periods, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
The purity is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND VS.

Product Science Overview

Introduction

Spermidine synthase (Spds) is an enzyme that plays a crucial role in the biosynthesis of polyamines, which are essential for various cellular processes such as cell growth, differentiation, and proliferation. The enzyme catalyzes the transfer of an aminopropyl group from decarboxylated S-adenosylmethionine (dcSAM) to putrescine, resulting in the formation of spermidine .

Structure and Function

Spermidine synthase is a member of the aminopropyl transferase family and is highly specific for its substrates. The enzyme typically exists as a dimer in solution and does not require any cofactors for its activity . The human recombinant form of spermidine synthase has been extensively studied to understand its structure and function.

The enzyme’s active site contains conserved aspartate residues that are crucial for substrate binding and catalysis. These residues help in the proper positioning of the substrates, ensuring efficient transfer of the aminopropyl group . The reaction mechanism of spermidine synthase is believed to follow an S_N2 mechanism, although there is some debate about whether it occurs via a ping-pong or ternary-complex mechanism .

Recombinant Expression

Human recombinant spermidine synthase is typically expressed in bacterial systems such as Escherichia coli. The recombinant enzyme is purified and characterized to study its biochemical properties and structural features. The molecular mass of the purified enzyme is approximately 33 kDa, and it shows optimal activity at physiological pH and temperature .

Biological Significance

Polyamines, including spermidine, are involved in numerous cellular processes. They play a role in stabilizing DNA, regulating ion channels, and modulating enzyme activities. Spermidine, in particular, has been shown to have anti-aging properties and is involved in autophagy, a cellular process that degrades and recycles damaged cellular components .

Applications

The study of human recombinant spermidine synthase has significant implications for biomedical research. Understanding the enzyme’s structure and function can aid in the development of therapeutic strategies for diseases associated with polyamine metabolism. Additionally, spermidine synthase inhibitors are being explored as potential treatments for cancer and parasitic infections .

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