Analytical Data
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Gene name
PCCb
- Application
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Alternative Names
PCCb；Propionyl-CoA carboxylase beta chain. mitochondrial
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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
P05166
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Expression Region
7-266aa
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AA Sequence
VAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFIT
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Molecular Weight
28 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
PCCb (procollagen C-proteinase enhancer protein 1) has garnered significant attention in the field of biomedical research due to its crucial role in collagen biosynthesis and tissue remodeling. As a key regulator of procollagen processing, PCCb is essential for the proper maturation of collagen fibers, which are vital for maintaining the structural integrity of various tissues, including skin, cartilage, and bones. Aberrations in PCCb expression or function can lead to numerous pathological conditions, including fibrosis, osteogenesis imperfecta, and various degenerative diseases. Recent advancements in molecular biology techniques have enabled researchers to explore the mechanisms by which PCCb interacts with procollagen, enhancing our understanding of its role in extracellular matrix (ECM) dynamics. Studies have shown that PCCb may act as a molecular chaperone, facilitating the correct folding and assembly of procollagen molecules. Moreover, the potential therapeutic applications of modulating PCCb function are being explored, particularly in regenerative medicine and tissue engineering, where enhancing collagen synthesis could promote wound healing and improve tissue repair. Ongoing research aims to unravel the precise molecular pathways involving PCCb and evaluate its potential as a biomarker for collagen-related disorders. Understanding the multifaceted roles of PCCb in ECM biology can pave the way for innovative therapeutic strategies targeting connective tissue diseases and pave the foundation for future studies aimed at harnessing its properties for clinical applications.
