Recombinant Human PRELP Protein, CF

Catalog # Availability Size / Price Qty
6447-PR-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (2)
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Recombinant Human PRELP Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Recombinant Human PRELP (Catalog # 6447-PR) binds Recombinant Human Aggrecan with an ED50 of 10.0-120 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human PRELP protein
Gln21-Ile382, with an N-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
His
Predicted Molecular Mass
42.5 kDa
SDS-PAGE
55-65 kDa, reducing conditions

Product Datasheets

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6447-PR

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6447-PR

Formulation Supplied as a 0.2 μm filtered solution in PBS.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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 opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
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Background: PRELP

PRELP (Proline aRginine-rich End Leucine-rich repeat Protein; also Prolargin) is a 55-62 kDa secreted glycoprotein that belongs to the small leucine-rich proteoglycan (SLRG) superfamily of extracellular matrix (ECM) molecules (1-4). Within this family, it is considered a class II member, implying that it is unlikely to form dimeric structures (3). PRELP is synthesized as a 382 amino acid (aa) precursor that contains a 20 aa signal sequence plus a 362 aa mature region (1, 5). Like other SLRPs, PRELP contains an N-terminal extension (aa 72-107) coupled to multiple Leu-rich repeats (LRRs) (aa 95-382) (6). Unlike other SLRPs, PRELP does not contain any proteoglycan chains, and its N‑terminal extension is highly basic in charge. The N-terminus reportedly binds to negatively-charged heparin/heparin-sulfate, chondroitin sulfate, and Gram- bacterial cell walls, while the LRR region participates in protein-protein interactions (7-9). Although PRELP is known to be synthesized by only a few cell types, including osteoblasts, skeletal muscle and chondrocytes, its expression is likely to be more widespread, given its presence in the basement membrane (BM) of Bowman’s capsule, epididymal epithelium and the stratified squamous epithelium of the skin (1, 10, 11). The dual binding profile of PRELP is key to its function. In cartilage, PRELP likely links chondrocyte cell membrane heparin sulfate (HS) chains to endogenous type II collagen. Within the context of the BM, PRELP likely plays an anchoring role. The BM is composed of type IV collagen and laminin, linked together by nidogen. BM Perlecan reinforces this linkage by binding to all three components. PRELP, on the edge of the BM, can bind to free perlecan HS chains (via its N-terminus), and to underlying type I collagen (via its LRRs), thus forming an anchor for the BM (11). Notably, the N-terminus appears to do more than simply provide part of a linkage mechanism. In bone, osteoblast secreted PRELP is hypothesized to undergo proteolysis by enzymes such as LysC and glutamyl endopeptidase. This will generate 40‑75 aa N‑terminal fragments that can bind to chondroitin sulfate adducts that exist on the surface of prefusion osteoclast precursors. Following binding, PRELP is internalized, complexed to annexin-II, and translocated to the nucleus, where it interacts with NF kappa Bp65 to block osteoclast maturation (8). In addition, PRELP interacts with connective tissue extracellular matrix, part of which is Aggrecan (11). Aggrecan G3 domain contains CRP repeat, which is involved in regulation of complement activity, is found synovial fluid. PRELP inhibits the formation of the complement membrane attack complex through interaction with different components of complement system in synovial fluid (12). In tissue, PRELP may also undergo proteolytic processing during inflammation to release an N‑terminal fragment containing aa 21‑42 of the precursor (7). This sequence has been shown to possess potent antimicrobial activity by creating pores in bacterial cell walls. Mature human PRELP shares 91% aa identity with mouse PRELP (10).

References
  1. Bengtsson, E. et al. (1995) J. Biol. Chem. 270:25639.
  2. Merline, R. et al. (2009) J. Cell Commun. Signal. 3:323.
  3. McEwan, P.A. et al. (2006) J. Struct. Biol. 155:294.
  4. Neame, P.J. et al. (1999) Cell. Mol. Life Sci. 55:1327.
  5. Grover, J. et al. (1996) Genomics 38:109.
  6. SwissProt # P51888.
  7. Bengtsson, E. et al. (2000) J. Biol. Chem. 275:40695.
  8. Rucci, N. et. al. (2009) J. Cell Biol. 187:669.
  9. Malmsten, M. et al. (2006) Matrix Biol. 25:294.
  10. Grover, J. & P.J. Roughley (2001) Matrix Biol. 20:555.
  11. Bengtsson, E. et al. (2002) J. Biol. Chem. 277:15061.
  12. Happonen, KE. (2012) J Biol Chem. 287:8092-8100.
Long Name
Proline-arginine-Rich End Leucine-rich repeat Protein
Entrez Gene IDs
5549 (Human)
Alternate Names
55 kDa leucine-rich repeat protein of articular cartilage; MST161; MSTP161; PRELP; prolargin proteoglycan; Prolargin; proline arginine-rich end leucine-rich repeat protein; proline/arginine-rich end leucine-rich repeat protein; Proline-arginine-rich end leucine-rich repeat protein; SLRR2A; SLRR2AMGC45323

Citations for Recombinant Human PRELP Protein, CF

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.

2 Citations: Showing 1 - 2
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  1. A novel biomarker of MMP-cleaved prolargin is elevated in patients with psoriatic arthritis
    Authors: D Sinkeviciu, S Skovlund G, S Sun, T Manon-Jens, A Aspberg, P Önnerfjord, AC Bay-Jensen, S Kristensen, S Holm Niels
    Sci Rep, 2020-08-11;10(1):13541.
    Species: Human
    Sample Types: Serum
    Applications: ELISA Standard, ELISA Capture
  2. S100A6 and its extracellular targets in Wharton's jelly of healthy and preeclamptic patients.
    Authors: Jurewicz E, Kasacka I, Bankowski E, Filipek A
    Placenta, 2014-04-03;35(6):386-91.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay

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Recombinant Human PRELP Protein, CF
By Anonymous on 07/05/2022
Application: Immunoassay Standard

good standard for ELISA