Recombinant Human Coagulation factor XIII A chain(F13A1)

Code CSB-EP007919HU
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Source E.coli
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Code CSB-EP007919HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP007919HU
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Source Baculovirus
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Code CSB-MP007919HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names F13A1
Uniprot No. P00488
Alternative Names 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 Region 39-732
Target Protein Sequence GV NLQEFLNVTS VHLFKERWDT NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF RVEYVIGRYP QENKGTYIPV PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD TYKFQEGQEE ERLALETALM YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VQFTNPLKET LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG ELDVQIQRRP SM
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

Customer Reviews and Q&A

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 Q&A
Q:

I need the lyophilized powder of Human Coagulation Factor XIIIa (Activated) which can be reconstituted and used as and when required.
Let me know how many micrograms of Activated Factor XIIIA you recommend for 1 ml of whole blood.
What is the difference between the four sources mentioned by you i.e yeast,etc & which one is as close as Human Factor XIIIA.

A:
Thanks for your inquiry. As to how many micrograms of Activated Factor XIIIA you recommend for 1 ml of whole blood, sorry, as we haven't validated the activity of this protein,
so we can't recommend the suitable dose to you, and we can't 100% guarantee its activity.
However, as what we provide is the active region of this protein, and it will be purified under very mild condition, in theory, it should be active.
This protein has less post-translational modification and theoretically the protein expressed by the eukaryotic expression system should be active,
We recommend the protein expressed by the mammalian expression system, which is closest to the structure of the native protein.
So you can consider to purchase a small size of MP protein to have a try.

Target Data

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.
Gene References into Functions
  1. Overall, genetically-determined FXIIIA levels have a significant long-term prognostic role, suggesting that a pharmacogenetics approach might help to select those AMI patients at risk of poor prognosis in the need of dedicated treatments. PMID: 30223472
  2. 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
  3. Effect of factor XIII levels and polymorphisms on the risk of myocardial infarction in young patients PMID: 29484525
  4. Coagulation factor FXIII-A (FXIIIA) was found to express specifically in the fetal beta islets but not in the alpha/delta islets. PMID: 29424810
  5. 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
  6. Our meta-analysis supports an association between F13A1 Val34Leu and recurrent pregnancy loss. PMID: 28683377
  7. A brief history of some key events in the conversion of fibrinogen to fibrin has been reviewed. (Review) PMID: 27519977
  8. 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
  9. F13A1 gene mutations in 73 patients treated with recombinant FXIII-A2 PMID: 28520207
  10. 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
  11. These findings provide insight into assembly of the fibrinogen/FXIII-A2B2 complex in both physiologic and therapeutic situations. PMID: 27561317
  12. FXIIIa exhibits a preference for Q237 in crosslinking reactions within fibrinogen alphaC (233-425) followed by Q328 and Q366. PMID: 26951791
  13. 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
  14. 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
  15. 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
  16. 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
  17. Genetic basis of severe factor XIII deficiency in a large cohort of Indian patients has been uncovered. PMID: 26852661
  18. Our meta-analysis suggests that there is no evidence for strong association between FXIII Val34Leu polymorphisms and intracerebral hemorrhage--{review} PMID: 26121426
  19. 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
  20. 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
  21. 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
  22. FXIII Val34Leu polymorphism has a protective effect against recurrent spontaneous abortion. PMID: 25862345
  23. Report immunochromatographic test for detection of anti-factor XIII A subunit antibodies that can diagnose 90 % of cases with autoimmune haemorrhaphilia XIII. PMID: 25740658
  24. 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
  25. Suggest that FXIIIa positive dermal dendrocytes may be the main antigen presenting cells in indeterminate leprosy. PMID: 25365500
  26. there is an evidence for association between factor XIII Val34Leu polymorphism and CSX PMID: 23677728
  27. 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
  28. 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
  29. 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
  30. 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
  31. study suggested that FXIIIA Val34Leu polymorphism was a protective factor for myocardial infarction in caucasians PMID: 24042156
  32. 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
  33. This study presents the covalent structure of single-stranded fibrin oligomers cross-linked by FXIIIa. PMID: 25896761
  34. a cohort of 27 individuals was analysed and four novel mutations leading to congenital FXIII deficiency were reported PMID: 24329762
  35. 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
  36. 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
  37. 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
  38. 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
  39. FXIII-A serves as a preadipocyte-bound proliferation/differentiation switch that mediates effects of hepatocyte-produced circulating pFN. PMID: 24934257
  40. plasma FN assembly into bone matrix in vitro requires FXIIIA transglutaminase activity making pFN assembly an active, osteoblast-mediated process. PMID: 24246248
  41. this study presents for the first time an in depth and time-resolved analysis of the FXIIIa substrate proteome in plasma. PMID: 24443567
  42. Patients with advanced-stage NSCLC exhibited higher coagulation FXIII activity than healthy controls and early-stage NSCLC patients. PMID: 24142643
  43. 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
  44. 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
  45. Studies indicate that mutations in the factor XIII-A (FXIII-A) gene causing congenital factor XIII deficiency. PMID: 23929307
  46. 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
  47. The Fctor XIIIa R260C mutant has significantly altered conformations, resulting in the rapid degradation by the proteasome inside the synthesizing cells PMID: 23279035
  48. 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
  49. 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
  50. 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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Involvement in disease Factor XIII subunit A deficiency (FA13AD)
Subcellular Location Cytoplasm, Secreted
Protein Families Transglutaminase superfamily, Transglutaminase family
Database Links

HGNC: 3531

OMIM: 134570

KEGG: hsa:2162

STRING: 9606.ENSP00000264870

UniGene: Hs.335513

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