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Recombinant Human Protein transport protein Sec16B (SEC16B), Truncated

ACP12902

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP12902 Target NameSEC16B
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Protein LengthPartialPurity>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 IDQ96JE7
Background Information
  • Uniprot Id

    Q96JE7

  • Target Species

    Human

  • Target Name

    SEC16B

  • Target Full Name

    Protein transport protein Sec16B

  • Target Function

    Plays a role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. Involved in peroxisome biogenesis. Regulates the transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER to peroxisomes.

  • Target Subcellular Location

    Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein.

  • Target Protein Families

    SEC16 family

  • Target Tissue Specificity

    Ubiquitous.

  • Target Synonyms

    DKFZp686C2486; FLJ23871; FLJ25761; FLJ33652; FLJ36620; KIAA1928; Leucine zipper transcription regulator 2; LZTR 2; PGPR p117; Protein SEC16 homolog B; Protein transport protein Sec16B; Regucalcin gene promoter region related protein; Regucalcin gene promoter region related protein p117; Regucalcin gene promoter region-related protein p117; RGPR; RGPR p117; RGPR-p117; SC16B_HUMAN; SEC16 homolog B (S. cerevisiae); SEC16 homolog B; SEC16B; SEC16S

  • Target Background

    SEC16B is a mammalian homolog of S. cerevisiae Sec16 that is required for organization of transitional endoplasmic reticulum (ER) sites and protein export (Bhattacharyya and Glick, 2007 [PubMed 17192411]).

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