Analytical Data
-
Gene name
CRTAP
- Application
-
Alternative Names
CASP; LEPREL3; Leprecan-Like 3
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9CYD3
-
Expression Region
Gln26~Ala400
-
Molecular Weight
74kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
CRTAP (Cartilage Associated Protein) is an essential protein involved in the biosynthesis and maturation of collagen, particularly type I collagen, which is pivotal for maintaining the structural integrity of connective tissues. Mutations in the CRTAP gene have been linked to osteogenesis imperfecta (OI), a genetic disorder characterized by fragile bones due to abnormal collagen development. This highlights the critical role of CRTAP in bone formation and stability. Research has focused on elucidating the functional mechanisms of CRTAP and its interactions with other chaperones and enzymes in collagen processing. The recombination and expression of CRTAP protein in various model systems have advanced our understanding of its role in collagen synthesis and its potential implications in therapeutic interventions for collagen-related disorders. By studying the recombinant form of CRTAP, scientists aim to uncover its structural properties, cellular localization, and functional interactions that could pave the way for new treatments for OI and related diseases. This research also serves to enhance our knowledge of extracellular matrix biology and the impact of chaperone proteins in tissue development and maintenance.
