- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
PRO-2776
Synonyms
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
Description
HAPLN1 Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 345 amino acids (16-354 a.a.) and having a molecular mass of 39.3kDa. HAPLN1 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
HAPLN1 protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤ 1 ug/ml and is measured by its binding ability in a functional ELISA with Hyaluronic acid.
Amino acid sequence
DHLSDNYTLD HDRAIHIQAE NGPHLLVEAE QAKVFSHRGG NVTLPCKFYR DPTAFGSGIH KIRIKWTKLT SDYLKEVDVF VSMGYHKKTY GGYQGRVFLK GGSDSDASLV ITDLTLEDYG RYKCEVIEGL EDDTVVVALD LQGVVFPYFP RLGRYNLNFH EAQQACLDQD AVIASFDQLY DAWRGGLDWC NAGWLSDGSV QYPITKPREP CGGQNTVPGV RNYGFWDKDK SRYDVFCFTS NFNGRFYYLI HPTKLTYDEA VQACLNDGAQ IAKVGQIFAA WKILGYDRCD AGWLADGSVR YPISRPRRRC SPTEAAVRFV GFPDKKHKLY GVYCFRAYNH HHHHH.
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Background
Abstract: This research paper provides an in-depth analysis of the HAPLN1 human recombinant protein, exploring its molecular characteristics, biological functions, and potential therapeutic applications. The hyaluronan and proteoglycan link protein 1 (HAPLN1), with its multifarious roles in cellular processes and extracellular matrix organization, has captured the attention of biomedical researchers worldwide. This report attempts to consolidate current knowledge, emphasizing the complexity of the HAPLN1 molecule, and outlines areas that warrant further investigation.
Keywords: HAPLN1, Hyaluronan, Proteoglycan, Recombinant protein, Extracellular matrix, Biomedical research, Therapeutics
Introduction The science of recombinant DNA has catapulted biological and medical research into new horizons. This paper focuses on the HAPLN1 human recombinant, a critical protein known to modulate cell interactions and behaviors, among other roles. Our aim is to elucidate its intricate functions and implications for human health, fostering novel biomedical insights.
Molecular Characteristics of HAPLN1 HAPLN1, a member of the link module superfamily, is a critical player in the organization and stabilization of the extracellular matrix. Its uniqueness lies in its ability to interact with hyaluronan and proteoglycans, thus influencing numerous biological processes. This section explores the structural characteristics and molecular functions of HAPLN1, detailing the dynamics of this complex protein.
Biological Functions of HAPLN1 HAPLN1 performs myriad functions and is particularly significant in the development and homeostasis of various tissues, including the skin, cartilage, and brain. This chapter outlines the diverse roles of HAPLN1, explicating the mechanisms underlying these functions.
Therapeutic Applications of HAPLN1 Owing to its functional diversity, HAPLN1 presents a promising target for therapeutic interventions in a range of pathologies, including cancer and neurodegenerative diseases. In this section, we delve into the potential applications of HAPLN1, discussing the prospects and challenges of HAPLN1-targeted therapy.
Conclusion The HAPLN1 human recombinant has the potential to advance therapeutic strategies for numerous diseases. Further research will undoubtedly unveil more about this fascinating protein, paving the way for novel biomedical applications. This paper is a testament to the intricate beauty and potential of HAPLN1, showcasing the complexity and functional diversity of this significant protein.
Background
Bibliography:
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