Factor XIIIa Antibody (YA1631)(PBS only)
(Synonyms: Coagulation factor XIIIa; F13A; F13a1; Fibrin stabilizing factor; A subunit; Fibrinoligase; TGase; Transglutaminase A chain)Factor XIIIa Antibody (YA1631) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Factor XIIIa.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 |
Product Details
Factor XIIIa Antibody (YA1631) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Factor XIIIa.
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Host Rabbit
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 83 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 83 kDa
Recombinant protein of human Factor XIIIa
Affinity Purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis of extracts from Jurkat(lane 2(20ug) and Jurkat(lane 3(40ug) using Factor XIIIa Antibody (HY-P81886) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Background
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Function
Factor XIIIA (FXIII-A) is the catalytic subunit of coagulation factor XIII and acts as a transglutaminase that forms ε- (γ-glutamyl) lysyl cross-links in protein substrates[1]. In plasma, FXIII circulates as FXIII-A2B2, where A subunits provide catalytic activity and B subunits act as non-enzymatic carrier subunits[2]. Mechanistically, thrombin and Ca2+ convert plasma FXIII into active FXIIIa, which stabilizes fibrin clots, links α2-antiplasmin to fibrin, and protects clots from fibrinolysis[1][3]. Beyond hemostasis, FXIII-A supports wound healing, tissue repair, pregnancy maintenance, and angiogenesis, making it relevant for coagulation biology and regenerative research[1][2]. In disease models, FXIII deficiency impaired wound healing and aggravated cardiac rupture after myocardial infarction in mice[4]. In inflammatory disease, macrophage-derived FXIII-A linked extravascular coagulation to COPD-associated inflammation, while macrophage-derived foam cells expressed cellular FXIII-A in atherosclerosis-related models[5][6]. Compared with FXIII-B, FXIII-A is the enzymatic isoform and therefore provides the primary experimental target for activity assays, genetic models, and inhibitor studies[2][3]. For experimental applications, tridegin inhibits plasma and platelet FXIIIa, and structure-function studies support its use as a peptide scaffold for FXIIIa inhibitor design[7][8].
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Subcellular Localization
Cytoplasm; Secreted
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Subunit
Tetramer of two A chains (F13A1) and two B (F13B) chains
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SwissProt ID
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Synonyms
Coagulation factor XIIIa; F13A; F13a1; Fibrin stabilizing factor; A subunit; Fibrinoligase; TGase; Transglutaminase A chain
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Research Field
Cardiovascular
Documentation
References
[1]. Muszbek L, et al. Factor XIII: a coagulation factor with multiple plasmatic and cellular functions. Physiol Rev. 2011 Jul;91(3):931-72. [Content Brief]
[2]. Alshehri FSM, et al. Factor XIII-A: An Indispensable \"Factor\" in Haemostasis and Wound Healing. Int J Mol Sci. 2021 Mar 17;22(6):3055. [Content Brief]
[3]. Komáromi I, et al. Factor XIII: novel structural and functional aspects. J Thromb Haemost. 2011 Jan;9(1):9-20. [Content Brief]
[4]. Nahrendorf M, et al. Factor XIII deficiency causes cardiac rupture, impairs wound healing, and aggravates cardiac remodeling in mice with myocardial infarction. Circulation. 2006 Mar 7;113(9):1196-202. [Content Brief]
[5]. Bazzan E, et al. Macrophages-derived Factor XIII links coagulation to inflammation in COPD. Front Immunol. 2023 Apr 25;14:1131292. [Content Brief]
[6]. Somodi L, et al. Cellular FXIII in Human Macrophage-Derived Foam Cells. Int J Mol Sci. 2023 Mar 2;24(5):4802. [Content Brief]
[7]. Finney S, et al. Tridegin, a new peptidic inhibitor of factor XIIIa, from the blood-sucking leech Haementeria ghilianii. Biochem J. 1997 Jun 15;324 ( Pt 3)(Pt 3):797-805. [Content Brief]
[8]. Böhm M, et al. Novel insights into structure and function of factor XIIIa-inhibitor tridegin. J Med Chem. 2014 Dec 26;57(24):10355-65. [Content Brief]
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