prospec

AMN Human

  • Name
  • Description
  • Pricings
  • Quantity
  • AMN Human
  • Amnion Associated Transmembrane Protein Human Recombinant
  • Shipped with Ice Packs

Catalogue number

PRO-1330

Synonyms

Protein amnionless, AMN, PRO1028, amnionless.

Introduction

Amnion Associated Transmembrane Protein (AMN) is a type I transmembrane protein. The AMN protein is essential for efficient absorption of vitamin B12. AMN is assumed to modulate bone morphogenetic protein (BMP) receptor function by acting as an accessory or coreceptor thus facilitating or hindering BMP binding. A complex of AMN and cubilin forms the cubam receptor.

Description

AMN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 361 amino acids (20-357 a.a) and having a molecular mass of 38.2kDa.
AMN 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

AMN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

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 90.0% as determined by SDS-PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSVSKLWVP NTDFDVAANW SQNRTPCAGG AVEFPADKMV SVLVQEGHAV SDMLLPLDGE LVLASGAGFG VSDVGSHLDC GAGEPAVFRD SDRFSWHDPH LWRSGDEAPG LFFVDAERVP CRHDDVFFPP SASFRVGLGP GASPVRVRSI SALGRTFTRD EDLAVFLASR AGRLRFHGPG ALSVGPEDCA DPSGCVCGNA EAQPWICAAL LQPLGGRCPQ AACHSALRPQ GQCCDLCGAV VLLTHGPAFD LERYRARILD TFLGLPQYHG LQVAVSKVPR SSRLREADTE IQVVLVENGP ETGGAGRLAR ALLADVAENG EALGVLEATM RESGAHVWGS S.

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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