Executive Summary
osteopontin Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE
Human osteopontin peptide is a term encompassing various fragments and forms of the osteopontin (OPN) protein, a crucial player in numerous biological processes. This multifunctional protein, also known as bone sialoprotein (BSP 1 or BNSP), is encoded by the SPP1 gene in humans. Its significance spans from bone health to immune regulation and even the complex mechanisms of hair growth and inhibition.
Osteopontin itself is characterized as a secreted, glycosylated phosphoprotein found predominantly in mineralized tissues like bones and teeth. It's a major non-collagenous bone protein that exhibits a strong affinity for hydroxyapatite, suggesting its integral role in the bone matrix. The gene for osteopontin spans 7 exons and is approximately 5 kilobases in length. Beyond bone, OPN is present in many human tissues and body fluids, including skin, urine, milk, and blood, highlighting its widespread biological importance.
Investigating the Diverse Roles of Osteopontin Peptides
Research into human osteopontin peptide has unveiled a spectrum of functionalities. One area of intense study involves its role in inflammation. Osteopontin has been demonstrated to regulate inflammation both *in vitro* and *in vivo*, and its involvement in the pathophysiology of various conditions is well-documented.
Furthermore, specific osteopontin-derived peptides have garnered attention for their potent effects on hair growth. For instance, the FOL-005 peptide has been identified as a molecule that stimulates hair growth. This discovery was made through the use of ligand-receptor glyco-capture technology, which led to the identification of neuropilin-1 (NRP-1) as a binding partner. Conversely, other osteopontin-derived peptides have been shown to act as an effective, novel inhibitory principle for human hair growth. Studies have indicated that these inhibitory peptides can work, at least in part, by decreasing the production of fibroblast growth factor-7 in the outer root sheath of hair follicles. This dual action – stimulation and inhibition – underscores the intricate regulatory capacity of osteopontin peptides in hair follicle biology.
Applications and Research Tools
The distinct properties of human osteopontin peptide lend themselves to various applications in scientific research. For example, PEP-1622, a peptide corresponding to 18 amino acids near the amino terminus of SPP1, can be utilized as a blocking peptide. This makes it a valuable tool for researchers working with polyclonal antibodies targeting osteopontin. Similarly, other osteopontin peptides are commercially available for blocking the activity of specific osteopontin antibodies, facilitating precise experimental designs.
For researchers aiming to study osteopontin in its active form, Recombinant Human Osteopontin protein (Active) is available. This recombinant protein is a Human Full Length protein, typically ranging from 17 to 314 amino acids, with high purity and low endotoxin levels. The availability of such recombinant human osteopontin allows for controlled investigations into its biological functions.
The field also utilizes tools like the RayBio Human Osteopontin (SPP1) ELISA Kit, designed for the quantitative analysis of osteopontin in various biological samples such as cell culture supernatants, plasma, and serum. This kit is typically ready for shipment within 1-2 business days, enabling prompt experimental progress.
Osteopontin's Broader Biological and Clinical Significance
Beyond hair growth and inflammation, osteopontin plays a role in other physiological processes. It is widely expressed and is particularly prominent in mineralized tissues. Here, it has been observed to inhibit bone mineralization and potentially play a role in preventing kidney stone formation, while simultaneously promoting inflammation and cellular activities.
The overexpression of osteopontin has also been noted in a variety of cancers, including lung, breast, colorectal, stomach, ovarian, melanoma, and mesothelioma. This association suggests potential diagnostic or therapeutic implications related to osteopontin.
In the context of early life development, osteopontin (OPN), as a whey protein, is believed to contribute to early life immune function. Its acidic glycoprotein nature and strong calcium-binding capabilities further enhance its diverse biological roles.
Understanding Variations and Specific Peptides
The study of human osteopontin peptide involves examining specific sequences and their functions. For instance, Osteopontin Peptide (NB100-1883PEP) is a commercially available reagent. Another example is a synthetic peptide corresponding to a sequence at the C-terminus of human Osteopontin, which differs from its mouse counterpart by eight amino acids.
The research into hyperphosphorylation of Human Osteopontin is also an active area, exploring the effects of phosphorylation on its function as an extracellular target of the Fam20C kinase.
In summary, the human osteopontin peptide represents a complex and versatile molecule with profound implications across various biological
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