Recombinant Human Factor XIII Protein (His Tag)

Name: Recombinant Human Factor XIII Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1969
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P05160
Synonym	Coagulation factor 13, Coagulation factor XIII, FXIIIB
Background	Coagulation factor XIII B chain, also known as Fibrin-stabilizing factor B subunit, Protein-glutamine gamma-glutamyltransferase B chain, Transglutaminase B chain and F13B, is a secreted protein which contains 1 Sushi ( CCP / SCR ) domains. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as a plasma carrier molecules. Platelet factor XIII is composed of just 2 A subunits, which are identical to those of plasma origin. The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin. Factor XIII acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion. Defects in F13B are the cause of factor XIII subunit B deficiency ( FA13BD ) which is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.
Description	A DNA sequence encoding the human F13B (P05160) (Met 1-Thr 661) was expressed, fused with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Glu 21
AA Sequence	Met 1-Thr 661
Molecular Weight	The secreted recombinant human F13B consists of 652 a.a. and predictes a molecular mass of 74.5 kDa. In SDS-PAGE under non-reduced conditions, the apparent molecular mass of rh F13B is approximately 65 kDa.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, 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.

Target Details

Target Function	The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin.
Subcellular Location	Secreted.
Database References	HGNC: 3534 OMIM: 134580 KEGG: hsa:2165 STRING: 9606.ENSP00000356382 UniGene: Hs.435782
Associated Diseases	Factor XIII subunit B deficiency (FA13BD)

Gene Functions References

In VTE patients the changes of FXIII level and their effect on the risk of VTE show considerable sex-specific differences. Intron K polymorphism results in decreased FXIII levels, but does not influence the risk of VTE. PMID: 28865246
The results suggest that plasma FXIII levels are subjected to multifactorial regulation with age, fibrinogen level and FXIII-B intron K polymorphism being the major determinants. Their effect on FXIII levels might influence the risk of thrombotic diseases. PMID: 27821352
Genetic markers associated with low FXIIIB levels increase risk of ischemic stroke cardioembolic subtype. PMID: 26159793
The FXIII-B intron K nt29756 G allele was associated with significant protection against CAS and MI in patients with a fibrinogen level in the upper tertile. PMID: 25569091
Changes in plasma levels of FXIIIB are associated with cognitive decline in the elderly. PMID: 26088309
Here, we update the knowledge about the pathophysiology of factor XIII deficiency and its therapeutic options. [review] PMID: 24503678
Case Report: congenital FXIII-B deficiency in which alloantibodies developed to exogenous FXIII-B. PMID: 23407795
FXIIIb subunit is found to be within normal range in eight Tunisian famillies with congenital factor XIII deficiency caused by two mutations, while expression of the FXIIIA subunit gene is decreased or undetectable. PMID: 19937244
Develop ELISA/chemoluminescence assay demonstrating that FXIII-A and FXIII-B are low concentration components of tear proteome. PMID: 20079358
role of FXIIIB in modifying catalytic activity of FXIIIA2 during factor XIII mediated crosslinking of fibrinogen PMID: 11816711
F13 B subunit antigen may have a role in susceptibility to stroke based on this study of family members of patients in South Asia PMID: 15634282
Genetic variants of factor XIIIb were evaluated on the effects of survival in myocardial infarction. PMID: 17515963
at least 3 out of the 10 Sushi domains of FXIII-B have the distinct function of forming a homodimer and a heterotetramer, which should be ascribed to the differences in their amino acid sequences PMID: 18652485
A specific colorimetric assay for measuring FXIIIB activity is reported. PMID: 19646949

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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.

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