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Mouse Anti-F13A1 Recombinant Antibody (F13A1/1448) (CBMAB-F2765-CQ)

This product is a mouse antibody that recognizes F13A1. The antibody F13A1/1448 can be used for immunoassay techniques such as: WB, FC, ELISA, IF, IHC-P.
See all F13A1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
F13A1/1448
Antibody Isotype
IgG2b, κ
Application
WB, FC, ELISA, IF, IHC-P

Basic Information

Immunogen
Recombinant fragment of human Factor XIIIa protein (aa46-181)
Specificity
Human
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Concentration
0.2 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Coagulation Factor XIII A Chain
Introduction
This gene encodes the coagulation factor XIII A subunit. 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 plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. 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.
Entrez Gene ID
2162
UniProt ID
P00488
Alternative Names
Coagulation Factor XIII A Chain; Protein-Glutamine Gamma-Glutamyltransferase A Chain; Coagulation Factor XIII, A1 Polypeptide; Coagulation Factor XIIIa; Transglutaminase A Chain; EC 2.3.2.13; F13A; BA525O21.1 (Coagulation Factor XIII, A1 Polypeptide);
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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