Analytical Data
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Gene name
COL13
- Application
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Alternative Names
COL13；Zinc finger Protein CONSTANS-LIKE 13
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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
O82256
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Expression Region
1-332aa
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AA Sequence
MEAEEGHQRD RLCDYCDSSV ALVYCKADSA KLCLACDKQV HVANQLFAKH FRSLLCDSCN ESPSSLFCET ERSVLCQNCD WQHHTASSSL HSRRPFEGFT GCPSVPELLA IVGLDDLTLD SGLLWESPEI VSLNDLIVSG GSGTHNFRAT DVPPLPKNRH ATCGKYKDEM IRQLRGLSRS EPGCLKFETP DAEIDAGFQF LAPDLFSTCE LESGLKWFDQ QDHEDFPYCS LLKNLSESDE KPENVDRESS VMVPVSGCLN RCEEETVMVP VITSTRSMTH EINSLERNSA LSRYKEKKKS RRYEKHIRYE SRKVRAESRT RIRGRFAKAA DP
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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
COL13, or collagen type XIII, is a crucial component of the extracellular matrix and plays significant roles in tissue development, stability, and repair mechanisms. It is mainly expressed in various tissues, particularly in skeletal muscle, skin, and fibroblasts, where it contributes to cell adhesion, migration, and signaling processes. The research on COL13 recombinant proteins has gained momentum due to its potential implications in understanding and treating various pathologies, including muscular dystrophies, fibrosis, and certain types of cancer. Advanced biotechnological methods have enabled the production of recombinant COL13, allowing for in-depth studies of its molecular structure and function. This research not only elucidates the biological significance of COL13 in normal physiological conditions but also sheds light on its roles in disease pathogenesis. Furthermore, the ability to generate COL13 under controlled laboratory conditions paves the way for developing therapeutic strategies, including tissue engineering and regenerative medicine approaches. By harnessing the properties of COL13, researchers aim to improve wound healing, enhance tissue regeneration, and explore novel treatments for degenerative diseases, marking COL13 as a promising target in biomedical research.
