Clone:
REAL830
Type of antibody:
Releasable fluorochromes, Primary antibodies, Recombinant antibodies
Applications:
MICS, IHC, IF
Alternative names:
Myelin Proteolipid Protein, PLP, Lipophilin, Plp1

Specifications for PLP Antibody, anti-human/mouse/rat, REAdye_lease™

Overview

Clone REAL830 is an antibody fragment derived from the full PLP antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAdye_lease Complex to bind markers with high avidity.
Clone REAL830 recognizes the PLP antigen, a multi-pass transmembrane Myelin Proteolipid Protein also known as Lipophilin. PLP is an important myelin protein from the central nervous system, which is involved in the formation, stabilization and maintenance of the multilamellar structure of myelin.
For removal of REAdye_lease fluorochromes for optional relabeling with different fluorochrome-conjugated REAdye_lease antibodies use the REAlease Support Kit (130-120-675).

Alternative names

Myelin Proteolipid Protein, PLP, Lipophilin, Plp1

Detailed product information

Technical specifications

CloneREAL830
Clonalitymonoclonal
Isotype controlControl Antibody
Hostcell line
Type of antibodyReleasable fluorochromes, Primary antibodies, Recombinant antibodies
Specieshuman, mouse, rat
AntigenPLP
Alternative names of antigenMyelin Proteolipid Protein, PLP, Lipophilin, Plp1
Distribution of antigenneural cells

Resources for PLP Antibody, anti-human/mouse/rat, REAdye_lease™

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for PLP Antibody, anti-human/mouse/rat, REAdye_lease™

Publications

  1. Popot, J. L. et al. (1991) Major Myelin proteolipid: the 4-alpha-helix topology. J. Membr. Biol. 120(3): 233-246
  2. Schliess, F. and Stoffel, W. (1991) Evolution of the myelin integral membrane proteins of the central nervous system. Biol. Chem. Hoppe-Seyler 372(9): 865-874
  3. Weimbs, T. et al. (1992) Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Biochemistry 31(49): 12289-12296

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