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Recombinant Human N-acetylmuramoyl-L-alanine amidase (PGLYRP2)

ACP08829

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP08829 Target NamePGLYRP2
Target SynonymsPGLYRP2; PGLYRPL; PGRPL; UNQ3103/PRO10102; N-acetylmuramoyl-L-alanine amidase; EC 3.5.1.28; Peptidoglycan recognition protein 2; Peptidoglycan recognition protein long; PGRP-LFormLyophilized powder
Expression SystemCustom Production. Please inquire and provide the desire expression system.Expression Range22-576aa
Mol Weight61.9kDProtein LengthFull Length of Mature Protein
Purity>85% (SDS-PAGE)Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ96PD5
Background Information
  • Uniprot Id

    Q96PD5

  • Target Species

    Human

  • Target Name

    PGLYRP2

  • Target Full Name

    N-acetylmuramoyl-L-alanine amidase

  • Target Function

    May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity.

  • Target Subcellular Location

    Secreted. Membrane.

  • Target Protein Families

    N-acetylmuramoyl-L-alanine amidase 2 family

  • Target Tissue Specificity

    Strongly expressed in liver and fetal liver, and secreted into serum. Expressed to a much lesser extent in transverse colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach and testis. Isoform 2 is not detected in the liver or serum.

  • Target Research Area

    Immunology

  • Target Synonyms

    PGLYRP2; PGLYRPL; PGRPL; UNQ3103/PRO10102; N-acetylmuramoyl-L-alanine amidase; EC 3.5.1.28; Peptidoglycan recognition protein 2; Peptidoglycan recognition protein long; PGRP-L

  • Target Background

    This gene encodes a peptidoglycan recognition protein, which belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. This protein hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in bacterial cell wall glycopeptides, and thus may play a scavenger role by digesting biologically active peptidoglycan into biologically inactive fragments.

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