Analytical Data
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Gene name
ADAMTSL5
- Application
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Alternative Names
(ADAMTSL-5)(Thrombospondin type-1 domain-containing protein 6)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZMM2
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Expression Region
43-481aa
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Molecular Weight
56.0 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
ADAMTSL5, a member of the ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) family, has garnered significant interest in recent years due to its potential implications in various biological processes and diseases. This protein is known to play a crucial role in the extracellular matrix (ECM) remodeling, particularly in the context of connective tissue disorders, and it may influence cell migration, proliferation, and differentiation. Its expression has been studied in relation to conditions such as osteoarthritis, where it is believed to modulate cartilage homeostasis, and in cancer biology, where it could impact tumor microenvironment and metastasis. The reconstitution of ADAMTSL5 allows for a detailed investigation of its biochemical properties, functional roles, and interactions with other matrix components. Additionally, understanding the structural characteristics and enzymatic activity of ADAMTSL5 could lead to the development of novel therapeutic strategies targeting ECM-related pathologies. Current research is focused on elucidating the mechanistic pathways through which ADAMTSL5 operates, exploring its regulatory networks, and determining its potential as a biomarker for disease progression. This knowledge not only enhances our comprehension of ECM dynamics but also establishes a foundation for future studies aimed at unraveling the complexities of ADAMTSL5 in health and disease. Thus, the recombinant expression of ADAMTSL5 represents a pivotal step in advancing our understanding of its multifaceted roles in tissue physiology and pathology.
