Recombinant Human Coagulation Factor Xiii A Chain (F13A1) Protein (His)

Name: Recombinant Human Coagulation Factor Xiii A Chain (F13A1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10741P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Coagulation Factor Xiii A Chain (F13A1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00488
Target Symbol	F13A1
Synonyms	bA525O21.1 (coagulation factor XIII; A1 polypeptide); Coagulation factor XIII A chain; Coagulation factor XIII A1 polypeptide ; Coagulation factor XIII A1 subunit; Coagulation factor XIII; A polypeptide; Coagulation factor XIIIa; F13A; F13A_HUMAN; F13a1; Factor XIIIA; Fibrin stabilizing factor; A subunit; Fibrinoligase; FSF; A subunit; Protein glutamine gamma glutamyltransferase A chain ; Protein-glutamine gamma-glutamyltransferase A chain; TGase ; Transglutaminase A chain; Transglutaminase; plasma; Transglutaminase. plasma
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	GVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM
Expression Range	39-732aa
Protein Length	Full Length of Mature Protein
Mol. Weight	81.2kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
Subcellular Location	Cytoplasm. Secreted. Note=Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.
Protein Families	Transglutaminase superfamily, Transglutaminase family
Database References	HGNC: 3531 OMIM: 134570 KEGG: hsa:2162 STRING: 9606.ENSP00000264870 UniGene: PMID: 30223472 Inflammatory monocytes highly express Factor XIIIA, which promotes fibrin cross-linking to create a scaffold for lung squamous carcinomas cell invasion and metastases. PMID: 29777108 Effect of factor XIII levels and polymorphisms on the risk of myocardial infarction in young patients PMID: 29484525 Coagulation factor FXIII-A (FXIIIA) was found to express specifically in the fetal beta islets but not in the alpha/delta islets. PMID: 29424810 Factor XIIIa (AC-1A1) is a sensitive and specific nuclear marker for sebaceous differentiation...which can be utilized to aid in the diagnosis of sebaceous neoplasms. PMID: 28873247 Our meta-analysis supports an association between F13A1 Val34Leu and recurrent pregnancy loss. PMID: 28683377 A brief history of some key events in the conversion of fibrinogen to fibrin has been reviewed. (Review) PMID: 27519977 The results of this study suggest that these biomarker F13A1 can serve as a potential non-invasive early diagnosis platform reflecting PiB-PET imaging for Mild Cognitive Impairment and Alzheimer's Disease. PMID: 27392853 F13A1 gene mutations in 73 patients treated with recombinant FXIII-A2 PMID: 28520207 Results show that the missense mutations-causing mild FXIII de fi ciency influence different aspects of FXIII function and can be functionally categorized on the basis of their expression phenotype. PMID: 27363989 These findings provide insight into assembly of the fibrinogen/FXIII-A2B2 complex in both physiologic and therapeutic situations. PMID: 27561317 FXIIIa exhibits a preference for Q237 in crosslinking reactions within fibrinogen alphaC (233-425) followed by Q328 and Q366. PMID: 26951791 factor XIII Val34Leu polymorphism is associated with coronary artery diseases risk, especially myocardial infarction. Age and sex did not affect the relationship between factor XIII Val34Leu polymorphism and diseases risk (Meta-Analysis) PMID: 27665853 Mounting evidence now suggests that platelet FXIII-A modulates hemostasis by several different mechanisms. This condensed review discusses recent advances in the understanding of the novel intracellular and extracellular functions of platelet FXIII-A. [review] PMID: 27207415 It is a unique case showing the combination of a highly aggressive angiosarcoma and presence of inherited FXIII deficiency. It is also a rare example demonstrating the benefit of FXIII genotyping besides the expected acquired FXIII deficiency possibly due to neoplasm induced increased consumption by elevated crosslinking of fibrin fibers. PMID: 26540128 The Val34Leu polymorphism of FXIII was not found in Korean people, and compared with Caucasians, a noticeably low incidence of deep vein thrombosis was shown. PMID: 26802299 Genetic basis of severe factor XIII deficiency in a large cohort of Indian patients has been uncovered. PMID: 26852661 Our meta-analysis suggests that there is no evidence for strong association between FXIII Val34Leu polymorphisms and intracerebral hemorrhage--{review} PMID: 26121426 Deletion of 11 or more N-terminal amino acids disrupts intersubunit interactions, which may prevent FXIII-A2 homodimer formation. AP-FXIII plays an important role in the stability of the FXIII-A2 dimer. PMID: 26083359 Mutations in the activation peptide of full-length recombinant FXIII regulate activation rates by thrombin, and V34L influences in vivo thrombus formation by increased cross-linking of the clot. PMID: 26743168 Different FXIII-A dynamics and levels could be utilised as early prognostic indicators during acute MI, revealing the individual potential to heal and suggesting tailored treatments to avoid heart failure or its extreme consequence. PMID: 25947356 FXIII Val34Leu polymorphism has a protective effect against recurrent spontaneous abortion. PMID: 25862345 Report immunochromatographic test for detection of anti-factor XIII A subunit antibodies that can diagnose 90 % of cases with autoimmune haemorrhaphilia XIII. PMID: 25740658 These results indicate that FXIIIa activity can be modulated by fibrinolytic enzymes, and suggest that changes in fibrinolytic activity may influence cross-linking of blood proteins. PMID: 26359437 Suggest that FXIIIa positive dermal dendrocytes may be the main antigen presenting cells in indeterminate leprosy. PMID: 25365500 there is an evidence for association between factor XIII Val34Leu polymorphism and CSX PMID: 23677728 These findings expose a newly recognized, essential role for fibrin crosslinking during whole blood clot formation and consolidation and establish FXIIIa activity as a key determinant of thrombus composition and size. PMID: 26324704 Results show that FXIII-B Arg95 variant is associated with an increased risk of abdominal aortic aneurysms (AAA) suggesting a possible role for FXIII in AAA pathogenesis. PMID: 25384012 The results demonstrate that FXIII-A Val34Leu polymorphism does not influence the occurrence of atherothrombotic ischemic stroke, but has an effect on the severity of its outcome. PMID: 24686102 His343Gln was a novel missense mutation occurring in the core domain of the FXIII A subunit. This is the first report of genetically confirmed FXIII deficiency in Korea, with novel and recurrent F13A1 mutations. PMID: 25004025 study suggested that FXIIIA Val34Leu polymorphism was a protective factor for myocardial infarction in caucasians PMID: 24042156 Genotype 163TT of FXIII-A gene as a new independent risk factor for the development of Venous Thromboembolism in young women living in the North-West region of Russia. PMID: 26035561 This study presents the covalent structure of single-stranded fibrin oligomers cross-linked by FXIIIa. PMID: 25896761 a cohort of 27 individuals was analysed and four novel mutations leading to congenital FXIII deficiency were reported PMID: 24329762 FXIII-A has a functional role through exposure on the activated platelet membrane where it exerts antifibrinolytic function by cross-linking alpha2AP to fibrin PMID: 25331118 8 new heterozygous missense mutations (Pro166Leu, Arg171Gln, His342Tyr, Gln415Arg, Leu529Pro, Gln601Lys, Arg703Gln and Arg715Gly) may affect catalysis, barrel domain integrity or activation peptide cleavage, depending on domain. PMID: 24889649 results demonstrate the utility of eQTL mapping in the identification of novel asthma genes and provide evidence for the importance of FADS2, NAGA, and F13A1 in the pathogenesis of asthma. PMID: 24934276 FXIII Val34Leu and PAI-1 4G/5G polymorphisms are prevalent in Egyptian women, with unexplained primary first trimester Recurrent miscarriage and combined polymorphisms statistically increasing the risk. PMID: 24702949 FXIII-A serves as a preadipocyte-bound proliferation/differentiation switch that mediates effects of hepatocyte-produced circulating pFN. PMID: 24934257 plasma FN assembly into bone matrix in vitro requires FXIIIA transglutaminase activity making pFN assembly an active, osteoblast-mediated process. PMID: 24246248 this study presents for the first time an in depth and time-resolved analysis of the FXIIIa substrate proteome in plasma. PMID: 24443567 Patients with advanced-stage NSCLC exhibited higher coagulation FXIII activity than healthy controls and early-stage NSCLC patients. PMID: 24142643 These data suggest that plasma transglutaminase factor XIII may play a key role in fetal development of vertebrates via cross-link of Fas antigen. PMID: 24216108 Data suggest that Factor XIII (composed of subunits F13A and F13B) increases rigidity/strength of fibrin clot, protects fibrin clot against shear stress in circulation, and protects fibrin from prompt elimination by fibrinolytic system. [REVIEW] PMID: 24476525 Studies indicate that mutations in the factor XIII-A (FXIII-A) gene causing congenital factor XIII deficiency. PMID: 23929307 Overproduction of FXIII-A by M2 macrophages might contribute to the excessive fibrin deposition in the submucosa of nasal polyps (NP), which might contribute to the tissue remodeling and pathogenesis of chronic rhinosinusitis with NP. PMID: 23541322 The Fctor XIIIa R260C mutant has significantly altered conformations, resulting in the rapid degradation by the proteasome inside the synthesizing cells PMID: 23279035 No association has been found between FXIII-A Val34Leu genotype and the risk for peripheral arterial disease in a Hungarian cohort of patients. PMID: 23518792 The prevalence of a F13A1 gene intron 1 variant (IVS1+12C>A) was found with greater frequency in patients with a mild FXIII deficiency with no detectable F13A1 or F13 B mutations than in those with heterozygous F13A1 mutations or in normal controls. PMID: 23508224 The results suggest an increase in FXIII activity as the number of repetitions of the short tandem repeat polymorphism in the F13A01 gene increased up to allele 5. PMID: 22909824

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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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Recombinant Human Coagulation Factor Xiii A Chain (F13A1) Protein (His)

Recombinant Human Coagulation Factor Xiii A Chain (F13A1) Protein (His)

Product Overview

Target Details

FAQs