Human Recombinant F13 protein, His Tag (V2LY-0526-LY3995)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant F13 protein, His Tag consist of Amino Acid: 1-661 and predicts a molecular mass of 74.5 kDa.
Molecule Mass
74.5 kDa
Verified
HPLC
Sequence
Amino Acid: 1-661
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
More Infomation

Target

Full Name
Coagulation Factor XIII A Chain
Research Area
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.
Biological Process
Blood coagulation Source: ProtInc
Blood coagulation, fibrin clot formation Source: UniProtKB
Peptide cross-linking Source: UniProtKB
Cellular Location
Secreted; Cytoplasm. Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.
Involvement in disease
Factor XIII subunit A deficiency (FA13AD):
An autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.
PTM
The activation peptide is released by thrombin.

Xie, H., Wang, M., Jin, Y., Li, X., Jiang, S., & Yang, L. (2022). A novel F13A1 gene mutation (Arg208Pro) in a Chinese patient with factor XIII deficiency. Blood Coagulation & Fibrinolysis, 33(6), 337-341.

Katsaras, G. N., Gialamprinou, D., Chatziioannidis, I., Karagianni, P., & Mitsiakos, G. (2022). Coagulation factor XIII deficiency–Report of a newborn F13A1 Val34Leu polymorphism carrier. Journal of Pediatric and Neonatal Individualized Medicine (JPNIM), 11(2), e110238-e110238.

Kaartinen, M. T., Arora, M., Heinonen, S., Hang, A., Barry, A., Lundbom, J., ... & Pietiläinen, K. H. (2021). F13A1 transglutaminase expression in human adipose tissue increases in acquired excess weight and associates with inflammatory status of adipocytes. International Journal of Obesity, 45(3), 577-587.

Ercan, H., Mauracher, L. M., Grilz, E., Hell, L., Hellinger, R., Schmid, J. A., ... & Zellner, M. (2021). Alterations of the platelet proteome in lung cancer: Accelerated F13A1 and ER processing as new actors in hypercoagulability. Cancers, 13(9), 2260.

Kaartinen, M. T., Arora, M., Heinonen, S., Rissanen, A., Kaprio, J., & Pietiläinen, K. H. (2020). Transglutaminases and Obesity in Humans: Association of F13A1 to Adipocyte Hypertrophy and Adipose Tissue Immune Response. International journal of molecular sciences, 21(21), 8289.

Songdej, N., Del Carpio-cano, F., Mao, G., Wurtzel, J., Goldfinger, L., Lambert, M. P., & Rao, A. K. (2020). Transcription factor RUNX1 regulates factor FXIIIA subunit (F13A1) expression in megakaryocytic cells and platelet F13A1 expression is downregulated in RUNX1 haplodeficiency. Blood, 136, 25-26.

Ma, S., Chen, C., Liang, Q., Wu, X., Wang, X., Wu, W., ... & Ding, Q. (2019). Phenotype and genotype of FXIII deficiency in two unrelated probands: identification of a novel F13A1 large deletion mediated by complex rearrangement. Orphanet journal of rare diseases, 14(1), 1-10.

Ansani, L., Marchesini, J., Pestelli, G., Luisi, G. A., Scillitani, G., Longo, G., ... & Gemmati, D. (2018). F13A1 gene variant (V34L) and residual circulating FXIIIA levels predict short-and long-term mortality in acute myocardial infarction after coronary angioplasty. International journal of molecular sciences, 19(9), 2766.

Gemmati, D., Occhionorelli, S., Tisato, V., Vigliano, M., Longo, G., Gonelli, A., ... & Zamboni, P. (2018). Inherited genetic predispositions in F13A1 and F13B genes predict abdominal adhesion formation: Identification of gender prognostic indicators. Scientific reports, 8(1), 1-13.

Peltier, J., Roperch, J. P., Audebert, S., Borg, J. P., & Camoin, L. (2018). Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer. Clinical proteomics, 15(1), 1-11.

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For research use only. Not intended for any clinical use.

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