Analytical Data
-
Gene name
PROC
- Application
-
Alternative Names
PROC；Vitamin K-dependent Protein C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P04070
-
Expression Region
43-461aa
-
AA Sequence
ANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP
-
Molecular Weight
54.2 kDa
-
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
PROC, or protein C, is a vitamin K-dependent plasma protein that plays a crucial role in the regulation of coagulation and the maintenance of hemostatic balance. Its biochemical function primarily involves the inactivation of factors Va and VIIIa, which are essential for the amplification of thrombin generation and clot formation. The study of PROC and its recombinant forms has gained significant traction due to their therapeutic potential in treating disorders related to coagulation, particularly in patients with deficiencies of natural anticoagulants leading to increased thrombotic risks. The production of recombinant PROC (rPROC) offers a promising approach to providing a stable and effective treatment option, potentially circumventing issues such as supply limitations from human plasma. Advances in biotechnology have enabled the development of more efficient expression systems for rPROC, allowing for enhanced yield and functional activity. Additionally, understanding the structure-function relationship of PROC has important implications for designing novel anticoagulant therapies. Recent research has also focused on the role of PROC in inflammation and cell signaling, broadening the scope of its clinical application. As thrombotic diseases remain a major global health issue, ongoing studies into PROC's mechanistic pathways and therapeutic applications continue to be vital in the landscape of coagulation research.
