Human HAPLN1 Antibody Summary
Asp16-Asn354
Accession # P10915
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.
Reconstitution Calculator
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
Citation 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.
1 Citation: Showing 1 - 1
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Protumorigenic role of HAPLN1 and its IgV domain in malignant pleural mesothelioma.
Authors: Ivanova AV, Goparaju CM, Ivanov SV
Clin. Cancer Res., 2009-04-07;15(8):2602-11.
Species: Human
Sample Types: Recombinant Protein
Applications: Western Blot
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