Human HAPLN1 Antibody
Human HAPLN1 Antibody Summary
Asp16-Asn354
Accession # P10915
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Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: HAPLN1
HAPLN1 (also known as link protein and CRTL1) is a member of the hyaladherin family of hyaluronic acid (HA) binding proteins. Hyaluronan binding proteins are of two types; those with link modules, and those without. Link modules are 100 amino acid (aa) HA and protein-binding sequences that contain two alpha -helices and two antiparallel beta -sheets (1, 3). There are three categories of link module-containing proteins. “A” domain-type proteins contain one link module; “B” domain-type proteins contain one link module with an N- and C-terminal flanking region; and “C” domain-type proteins have an extended structure with one N-terminal V-type Ig-like domain followed by two link modules (2). The HAPLN family is a group of four C domain-type proteins that share approximately 50% aa identity (4). HAPLN1 is synthesized as a 354 aa precursor that contains a 15 aa signal sequence and a 339 aa mature region (4 - 6). It contains one Ig-like domain and two 95 aa link modules (6). It is variably glycosylated with a native molecular weight between 41 - 48 kDa (7, 8). Mature human HAPLN1 is 97%, 96%, 96%, 96%, and 96% aa identical to equine, porcine, rat, mouse and bovine HAPLN1, respectively. HAPLN1 contributes to extracellular matrix stability and flexibility (9). In cartilage, HALPN1 forms a ternary complex with HA and aggrecan. This creates a gel-like substance with remarkable resistance to deformation (3). In this complex, HA forms a linear backbone with perpendicularly attached aggrecan and HAPLN1. Aggrecan and HAPLN1 lie parallel to each other, while HA runs between the two HAPLN1 link modules (2, 3, 10). The Ig domain of HAPLN1 binds to aggrecan, while the two link modules of HAPLN1 bind to HA. Although HA and aggrecan will associate, the tendency is towards dissociation (2, 3, 8). HAPLN1 provides a stabilizing influence on HA-aggrecan associations, thus creating a long-lived ternary functional complex.
- Day, A.J. and G.D. Prestwich (2002) J. Biol. Chem. 277:4585.
- Seyfried, N.T. et al. (2005) J. Biol. Chem. 280:5435.
- Matsumoto, K. et al. (2003) J. Biol. Chem. 278:41205.
- Spicer, A.P. et al. (2003) J. Biol. Chem. 278:21083.
- Dudhia, J. and T.E. Hardingham (1990) Nucleic Acids Res. 18:1292.
- Osborne-Lawrence, S.L. et al. (1990) Genomics 8:562.
- Roughley, P.J. et al. (1982) J. Biol. Chem. 257:11908.
- Shi, S. et al. (2004) J. Biol. Chem. 279:12060.
- Binette, F. et al. (1994) J. Biol. Chem. 269:19116.
- Perkins, S.J. et al. (1992) Biochem. J. 285:263.
Product Datasheets
Citations for Human HAPLN1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 8
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Surfactant protein C is associated with perineuronal nets and shows age-dependent changes of brain content and hippocampal deposits in wildtype and 3xTg mice
Authors: S Schob, J Puchta, K Winter, D Michalski, B Mages, H Martens, A Emmer, KT Hoffmann, F Gaunitz, A Meinicke, M Krause, W Härtig
Journal of chemical neuroanatomy, 2021;0(0):102036.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC -
The protein tyrosine phosphatase RPTP?/phosphacan is critical for perineuronal net structure
Authors: GJ Eill, A Sinha, M Morawski, MS Viapiano, RT Matthews
J. Biol. Chem., 2020;295(4):955-968.
Species: Mouse
Sample Types: Whole Cells
Applications: ICC -
Synaptic coupling of inner ear sensory cells is controlled by brevican-based extracellular matrix baskets resembling perineuronal nets
Authors: M Sonntag, M Blosa, S Schmidt, K Reimann, K Blum, T Eckrich, G Seeger, D Hecker, B Schick, T Arendt, J Engel, M Morawski
BMC Biol., 2018;16(1):99.
Species: Mouse
Sample Types: Cell Lysates
Applications: Western Blot -
Extracellular matrix molecules exhibit unique expression pattern in the climbing fiber-generating precerebellar nucleus, the inferior olive.
Authors: Kecskes S, Gaal B, Racz E, Birinyi A, Hunyadi A, Matesz C
Neuroscience, 2015;284(0):412-21.
Species: Rat
Sample Types: Whole Tissue
Applications: IHC -
Saccadic Palsy following Cardiac Surgery: Possible Role of Perineuronal Nets.
Authors: Eggers S, Horn A, Roeber S, Hartig W, Nair G, Reich D, Leigh R
PLoS ONE, 2015;10(7):e0132075.
Species: Human
Sample Types: Whole Tissue
Applications: IHC -
Semaphorin 3A binds to the perineuronal nets via chondroitin sulfate type E motifs in rodent brains.
Authors: Dick, Gunnar, Tan, Chin Lik, Alves, Joao Nun, Ehlert, Erich M, Miller, Gregory, Hsieh-Wilson, Linda C, Sugahara, Kazuyuki, Oosterhof, Arie, van Kuppevelt, Toin H, Verhaagen, Joost, Fawcett, James W, Kwok, Jessica
J Biol Chem, 2013;288(38):27384-95.
Species: Mouse
Sample Types: Tissue Homogenates
Applications: Western Blot -
Perisynaptic aggrecan-based extracellular matrix coats in the human lateral geniculate body devoid of perineuronal nets.
Authors: Lendvai D, Morawski M, Bruckner G, Negyessy L, Baksa G, Glasz T, Patonay L, Matthews RT, Arendt T, Alpar A
J. Neurosci. Res., 2011;90(2):376-87.
Species: Human
Sample Types: Whole Tissue
Applications: IHC-Fr -
The altered expression of perineuronal net elements during neural differentiation.
Authors: Eskici N, Erdem-Ozdamar S, Dayangac-Erden D
Cell Mol Biol Lett, 0;23(0):5.
Species: Rat
Sample Types: Cell Lysates
Applications: Western Blot
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Very strong and specific staining.
