STARD5 Human

StAR-Related Lipid Transfer Domain Containing 5 Human Recombinant
Cat. No.
BT21220
Source
Escherichia Coli.
Synonyms
StAR-Related Lipid Transfer (START) Domain Containing 5, START Domain-Containing Protein 5, StARD5.
Appearance
Sterile Filtered clear 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

STARD5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 236 amino acids (1-213 a.a) and having a molecular mass of 26.2kDa. STARD5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
STARD5, a member of the STARD protein family, plays a crucial role in lipid transport and metabolism. This family, comprising 15 members, is characterized by the presence of a START domain. Classified into six subfamilies based on their START domain sequences, STARD5 proteins share around 30% amino acid identity. Although not regulated by sterols, STARD5 expression is induced by endoplasmic reticulum (ER) stress.
Description
Recombinant Human STARD5, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 236 amino acids (1-213 a.a), including a 23 amino acid N-terminal His-tag, resulting in a molecular weight of 26.2 kDa. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The STARD5 protein solution (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0), containing 0.1M NaCl, 1mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms
StAR-Related Lipid Transfer (START) Domain Containing 5, START Domain-Containing Protein 5, StARD5.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDPALAA QMSEAVAEKM LQYRRDTAGW KICREGNGVS VSWRPSVEFP GNLYRGEGIV YGTLEEVWDC VKPAVGGLRV KWDENVTGFE IIQSITDTLC VSRTSTPSAA MKLISPRDFV DLVLVKRYED GTISSNATHV EHPLCPPKPG FVRGFNHPCG CFCEPLPGEP TKTNLVTFFH TDLSGYLPQN VVDSFFPRSM TRFYANLQKA VKQFHE

Product Science Overview

Introduction

The StAR-related lipid transfer (START) domain is a protein module of approximately 210 amino acids that binds a variety of lipids, including sterols . The START domain is conserved through evolution in plants and animals and serves as a versatile binding interface for lipids that function in many distinct processes . In humans, the START domain is found in 15 distinct proteins, either alone or associated with other protein domains .

StAR-Related Lipid Transfer Domain Containing 5 (STARD5)

StAR-related lipid transfer domain containing 5 (STARD5) is a protein encoded by the STARD5 gene in humans . The protein is 213 amino acids long and consists almost entirely of a START domain . STARD5 is part of the StarD4 subfamily of START domain proteins, sharing 34% sequence identity with STARD4 .

Function

STARD5 binds both cholesterol and 25-hydroxycholesterol and appears to function to redistribute cholesterol to the endoplasmic reticulum and/or the plasma membrane . The protein is most prevalent in the kidney and liver, where it is found in Kupffer cells . Increased levels of STARD5 increase free cholesterol in the cell .

Cholesterol homeostasis is regulated, at least in part, by sterol regulatory element-binding proteins (SREBPs) and liver X receptors (LXRs) . Upon sterol depletion, LXRs are inactive, and SREBPs are cleaved, after which they bind promoter SREs and activate genes involved in cholesterol biosynthesis and uptake . Sterol transport is mediated by vesicles or by soluble protein carriers, such as steroidogenic acute regulatory protein (STAR) .

Structural Insights

The crystal structures of several START domain proteins have been solved, revealing a conserved helix-grip fold that forms an inner tunnel wide enough to accommodate the hydrophobic lipid . The C-terminal end of the domain plays a fundamental role, forming a lid over a deep lipid-binding pocket that shields the ligand from the external environment .

Physiological and Pathological Roles

Mammalian START proteins have diverse expression patterns and can be found free in the cytoplasm, attached to membranes, or in the nucleus . They appear to function in various physiological processes, such as lipid transfer between intracellular compartments, lipid metabolism, and modulation of signaling events . Mutation or misexpression of START proteins is linked to pathological processes, including genetic disorders, autoimmune diseases, and cancer .

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