Analytical Data
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Gene name
HSPG
- Application
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Alternative Names
HSPG；HSPG1；Syndecan-2
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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
P98160
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Expression Region
4197-4391aa
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AA Sequence
DAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS
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Molecular Weight
24.4 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
Heparan sulfate proteoglycans (HSPGs) are crucial components of the extracellular matrix and cell surfaces, playing vital roles in various biological processes, including cell signaling, adhesion, migration, and differentiation. Their structure consists of a core protein that is covalently linked to heparan sulfate glycosaminoglycan chains, allowing for diverse interactions with a wide range of ligands, including growth factors, morphogens, and pathogens. Research into HSPG recombinant proteins has gained significant attention due to their potential therapeutic applications. By engineering HSPG variants with specific glycan modifications, scientists aim to elucidate their functional roles and regulatory mechanisms in physiological and pathological contexts, such as in cancer progression, inflammation, and viral infections. Recombinant HSPGs offer controlled systems for studying protein interactions, drug delivery mechanisms, and tissue engineering applications. Moreover, they hold promise in developing targeted therapies that exploit HSPG's biological properties, enabling more precise interventions in disease treatment. Overall, the study of recombinant HSPGs contributes to a deeper understanding of cellular communication and the development of innovative strategies to manipulate these processes for therapeutic benefits.
