Recombinant Human PADI4 Protein (His Tag)

Name: Recombinant Human PADI4 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3639
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Synonym	PAD, PAD4, PADI5, PDI4, PDI5
Background	Protein-arginine deiminase type-4, also known as HL-6 PAD, Peptidylarginine deiminase IV, Protein-arginine deiminase type IV and PADI4, is a cytoplasm and nucleus protein which belongs to theprotein arginine deiminase family. PADI4 is expressed in CD34+ stem cells in normal tissues, and many more CD34+ cells expressing PADI4 are present in tumour tissues. PADI4 post-translationally converts peptidylarginine to citrulline, a process called citrullination. Studies have demonstrated the high expression of PADI4 in various malignant tumour tissues. PADI4 is also expressed at high levels in the blood of patients with some malignant tumours. Citrullination of histone, cytokeratin, antithrombin and fibronectin have been confirmed to be involved in abnormal apoptosis, high coagulation, and disordered cell proliferation and differentiation, all of which are main features of malignant tumours. PADI4 may play an important role in tumourigenesis. Genetic variations in PADI4 are a cause of susceptibility to rheumatoid arthritis (RA). It is a systemic inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures.
Description	A DNA sequence encoding the human PADI4 (Met1-Pro663) was expressed with a His tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met1-Pro663
Molecular Weight	The recombinant human PADI4 consists of 681 a.a. and predicts a molecular mass of 76.3 kDa.
Purity	>95% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.