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Magic™ Recombinant Human GP1BB Membrane Protein in Virus-Like Particles (MP-VLPs) (CAT#: S01YF-0622-KX72)

Datasheet
This product is recombinant Human GP1BB in VLPs form. This product is produced from HEK293 by co-expressing the retroviral structural core polyprotein (gag) and the target membrane protein. MP-VLPs display highly-expressed copies of membrane proteins in their native conformation, providing an alternative to membrane protein stable cell lines, membrane preparations, detergent-solubilized proteins and other membrane protein preparation strategies. MP-VLPs can be used for a wide range of applications in antibody production, antibody discovery, antibody characterization, binding assays and functional assays.

Product Specifications

  • Host Species
  • Human
  • Target Protein
  • GP1BB
  • Protein Length
  • Full length
  • Protein Class
  • Cell adhesion
  • TMD
  • 1
  • Sequence
  • CPAPCSCAGTLVDCGRRGLTWASLPTAFPVDTTELVLTGNNLTALPPGLLDALPALRTAHLGANPWRCDCRLVPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYLAEDELRAACAPGPLCWGALAAQLALLGLGLLHALLLVLLLCRLRRLRARARARAAARLSLTDPLVAERAGTDES

Product Description

  • Application
  • ELISA; Antibody Production; Antibody Discovery; Antibody Characterization; Binding Assays; Functional Assays
  • Expression Systems
  • HEK293 expression system
  • Tag
  • 10xHis tag at the C-terminus
  • Protein Format
  • Membrane Protein-Virus Like Particles (MP-VLPs)
  • Buffer
  • PBS, 6% Trehalose, pH 7.4

Target

  • Target Protein
  • GP1BB
  • Full Name
  • Glycoprotein Ib platelet subunit beta
  • Introduction
  • Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described; however, the authenticity of this product has been questioned. Yet another less abundant GPIb beta mRNA species of 3.5 kb, expressed in nonhematopoietic tissues such as endothelium, brain and heart, was shown to result from inefficient usage of a non-consensus polyA signal in the neighboring upstream gene (SEPT5, septin 5). In the absence of polyadenylation from its own imperfect site, the SEPT5 gene produces read-through transcripts that use the consensus polyA signal of this gene.
  • Alternative Names
  • GP1BB; BS; CD42C; GPIBB; BDPLT1; GPIbbeta; platelet glycoprotein Ib beta chain; GP-Ib beta; antigen CD42b-beta; glycoprotein Ib (platelet), beta polypeptide; glycoprotein Ib platelet beta subunit; nuclear localization signal deleted in velocardiofacial syndrome; platelet membrane glycoprotein Ib beta; truncated platelet membrane glycoprotein Ib beta; Glycoprotein Ib platelet subunit beta

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