Recombinant Human HAPLN1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human HAPLN1 Protein, CF Summary

Details of Functionality
Measured by its ability to bind biotinylated hyaluronan in a functional ELISA.
Source
Mouse myeloma cell line, NS0-derived human HAPLN1 protein
Asp16-Asn354, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Asp16
Protein/Peptide Type
Recombinant Proteins
Gene
HAPLN1
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
39.8 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
45-52 kDa, reducing conditions
Publications
Read Publications using
2608-HP in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human HAPLN1 Protein, CF

  • Cartilage link protein
  • Cartilage-link protein
  • Cartilage-linking protein 1
  • CRTL1
  • CRTL1cartilage linking protein 1
  • HAPLN1
  • hyaluronan and proteoglycan link protein 1
  • Proteoglycan link protein

Background

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.

  1. Day, A.J. and G.D. Prestwich (2002) J. Biol. Chem. 277:4585.
  2. Seyfried, N.T. et al. (2005) J. Biol. Chem. 280:5435.
  3. Matsumoto, K. et al. (2003) J. Biol. Chem. 278:41205.
  4. Spicer, A.P. et al. (2003) J. Biol. Chem. 278:21083.
  5. Dudhia, J. and T.E. Hardingham (1990) Nucleic Acids Res. 18:1292.
  6. Osborne-Lawrence, S.L. et al. (1990) Genomics 8:562.
  7. Roughley, P.J. et al. (1982) J. Biol. Chem. 257:11908.
  8. Shi, S. et al. (2004) J. Biol. Chem. 279:12060.
  9. Binette, F. et al. (1994) J. Biol. Chem. 269:19116.
  10. Perkins, S.J. et al. (1992) Biochem. J. 285:263.

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Publications for HAPLN1 (2608-HP)(3)

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Bioinformatics

Gene Symbol HAPLN1
Uniprot