Analytical Data
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Gene name
HAPLN1
- Application
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Alternative Names
HAPLN1;CRTL1;Hyaluronan and proteoglycan link Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10915
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Expression Region
16-354aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSDHLSDNYTLDHDRAIHIQAENGPHLLV EAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLKEV DVFVSMGYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLEDYGRYKCEVI EGLEDDTVVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFD QLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWD KDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQI FAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKH KLYGVYCFRAYN
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Molecular Weight
41 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HAPLN1, or hyaluronan and proteoglycan binding 1, is a key extracellular matrix protein that plays a significant role in the structure and function of various tissues. It interacts with hyaluronic acid and proteoglycans, contributing to the integrity of the extracellular matrix (ECM) and influencing cell behavior, including proliferation, migration, and differentiation. Research into HAPLN1 has gained momentum due to its involvement in crucial biological processes and its implications in various diseases, including cancer, where altered expression levels of HAPLN1 have been observed. Additionally, studies have suggested that HAPLN1 may be involved in inflammatory responses and tissue repair mechanisms. The development of recombinant HAPLN1 proteins has facilitated investigations into its functional properties and potential therapeutic applications. Recombinant techniques allow for the production of HAPLN1 in controlled environments, enabling researchers to examine its structural characteristics and biological activities in detail. These studies aim to elucidate HAPLN1’s precise roles in health and disease, paving the way for novel therapeutic strategies targeting ECM components to manipulate cellular behavior in regenerative medicine and oncology. Understanding HAPLN1’s mechanisms may also provide insights into tissue engineering and the development of biomaterials that mimic the ECM, enhancing regenerative outcomes. As such, the ongoing research on HAPLN1 recombinant proteins continues to promise significant advancements in both basic and applied biomedical sciences, that are essential for future innovations in treatments involving ECM-targeting strategies.
