Analytical Data
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Gene name
CSPG2
- Application
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Alternative Names
Chondroitin sulfate proteoglycan 2; Chondroitin sulfate proteoglycan core protein 2; Chondroitin sulfate proteoglycan core protein; cartilage; CSPG2; CSPG2_HUMAN; ERVR; GHAP; Glial hyaluronate binding protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13611
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Expression Region
1-354aa
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AA Sequence
MFINIKSILWMCSTLIVTHALHKVKVGKSPPVRGSLSGKVSLPCHFSTMPTLPPSYNTSEFLRIKWSKIEVDKNGKDLKETTVLVAQNGNIKIGQDYKGRVSVPTHPEAVGDASLTVVKLLASDAGLYRCDVMYGIEDTQDTVSLTVDGVVFHYRAATSRYTLNFEAAQKACLDVGAVIATPEQLFAAYEDGFEQCDAGWLADQTVRYPIRAPRVGCYGDKMGKAGVRTYGFRSPQETYDVYCYVDHLDGDVFHLTVPSKFTFEEAAKECENQDARLATVGELQAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFENQTGFPPPDSRFDAYCFKRKCLIPF
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Molecular Weight
65.7 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
CSPG2, also known as versican, is a large extracellular matrix proteoglycan that plays a crucial role in various biological processes, including cell adhesion, proliferation, and migration. Its structural diversity, stemming from alternative splicing and glycosylation, allows it to interact with a wide range of molecules, influencing cellular behavior in tissue development and repair. Dysregulation of CSPG2 has been implicated in several pathological conditions, including cancer, where it contributes to tumor growth, metastasis, and the formation of a favorable microenvironment. The study of recombinant CSPG2 proteins is vital for understanding their functional roles and mechanisms in health and disease. By producing these proteins in a laboratory setting, researchers can investigate their biological activities, evaluate their interactions with other extracellular matrix components, and assess their potential as therapeutic targets. Additionally, recombinant CSPG2 can serve as a tool for elucidating its role in signaling pathways and cellular processes, paving the way for innovative treatments for diseases associated with altered proteoglycan dynamics. Overall, research on recombinant CSPG2 proteins holds significant promise for advancing our understanding of extracellular matrix biology and its implications in various disorders.
