prospec
ADAT2 Human

ADAT2 Human

  • Name
  • Description
  • Cat#
  • Pricings
  • Quantity
  • ADAT2 Human

  • Adenosine Deaminase, tRNA-specific 2 Human Recombinant
  • ENZ-561
  • Shipped with Ice Packs

Catalogue number

ENZ-561

Synonyms

DEADC1, TAD2.

Introduction

Adenosine Deaminase (ADA), also recognized as ADAT2 is an enzyme that takes part in purine metabolism. ADAT2 is necessary for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. ADAT2 is involved in the deamination of adenosine-34 to inosine in numerous tRNAs. ADAT2 is part of the cytidine and deoxycytidylate deaminase protein family, ADAT2 employs zinc as a cofactor. ADAT2 is a 191 amino acid enzyme that exists as two isoforms formed by alternative splicing events.

Description

Recombinant Human ADAT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191 a.a) and having a molecular mass of 23.2 kDa.
ADAT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile filtered colorless solution.

Formulation

The ADAT2 (0.5mg/ml) protein contains 20mM Tris-HCl buffer pH-8, 2mM DTT, 50mM NaCl 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 90% as determined by Analysis by SDS-PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK SKVRKKECQK S.

Safety Data Sheet

Usage

ProSpecs 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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