prospec

ATP5H Human

  • Name
  • Description
  • Pricings
  • Quantity
  • ATP5H Human
  • ATP Synthase Mitochondrial Fo Complex Subunit D Human Recombinant
  • Shipped with Ice Packs

Catalogue number

PRO-1631

Synonyms

ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.

Introduction

ATP5H is a member of the ATPase d subunit family and encodes the d subunit of the F0 complex. Electron transport complexes of the respiratory chain create a proton gradient across the membrane which induces ATP5H to transform ADP to ATP. Two alternatively spliced isoforms of ATP5H, encoded by a gene that maps to human chromosome 17q25.1, are known. ATP5H is restricted to mitochondrial inner membrane.

Description

ATP5H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (1-161) and having a molecular mass of 20.9kDa.
ATP5H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile filtered colorless solution.

Formulation

The ATP5H solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. 
Store, frozen at -20°C for longer periods of time. 
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.

Purity

Greater than 85% as determined by SDS-PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSMAGRKLA LKTIDWVAFA EIIPQNQKAI ASSLKSWNET LTSRLAALPE NPPAIDWAYY KANVAKAGLV DDFEKKFNAL KVPVPEDKYT AQVDAEEKED VKSCAEWVSL SKARIVEYEK EMEKMKNLIP FDQMTIEDLN EAFPETKLDK KKYPYWPHQP IENL

Safety Data Sheet

Usage

ProSpec'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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