Analytical Data
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Gene name
SRGN
- Application
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Alternative Names
SRGN;PRG;PRG1;Serglycin
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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
P10124
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Expression Region
1-158aa
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AA Sequence
MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCL EEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGS GSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQH GLEEDFML
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Molecular Weight
43 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
Related Products
Protein Description
SRGN, or serglycin, is a novel protein that plays a crucial role in various biological processes, including cell adhesion, inflammation, and extracellular matrix organization. Research on SRGN has gained momentum due to its implications in several disease states, including cancer, autoimmune disorders, and infections. This proteoglycan is primarily expressed in hematopoietic cells and has been implicated in modulating the functions of these cells, notably in immune responses. The structure of SRGN allows it to interact with various proteins and growth factors, suggesting a multifaceted role in cellular communication and signaling pathways. Understanding the mechanisms by which SRGN contributes to disease progression is of significant interest, as it may unveil new therapeutic targets. Recent studies have highlighted its involvement in tumor microenvironments, where it may facilitate cancer cell survival and metastasis. Additionally, SRGN's potential as a biomarker for certain conditions is being explored, promising to enhance diagnostic and prognostic capabilities in clinical settings. Consequently, SRGN represents a critical area of research within the fields of molecular biology and medicine, with ongoing investigations aimed at elucidating its functional significance and therapeutic potential.
