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Fibrinogen gamma chain (E1U3Z) XP® Rabbit mAb (BSA and Azide Free) #38915
Filter:
- WB
- IHC
Western blot analysis of extracts from various cell lines using Fibrinogen gamma chain (E1U3Z) XP® Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower). Absence of signal in extracts from DU 145 and NCI-H1299 cells is predicted from RNAseq and confirms the specificity of the antibody for fibrinogen gamma chain protein. Data were generated using the standard formulation of this product.
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 50 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- Related Products
Product Information
Product Usage Information
This product is the carrier free version of product #45850. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.
For standard formulation of this product see product #45850
For standard formulation of this product see product #45850
Storage
Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.
Specificity / Sensitivity
Fibrinogen gamma chain (E1U3Z) XP® Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total fibrinogen gamma chain protein. This antibody may cross-react with an unidentified protein of 70 kDa in some cell extracts.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser190 of human fibrinogen gamma chain protein.
Background
Fibrinogen is a large, multimeric plasma glycoprotein that is constitutively synthesized by liver hepatocytes. As a key component of blood clots, fibrinogen plays a central role in hemostasis and thrombosis. In total, six polypeptide chains (2Aα, 2Bβ, and 2γ) are produced intracellularly in a coordinated manner, which are then covalently linked together by a network of disulfide bonds to form a fibrinogen heterohexamer (1). Research studies have shown that expression of the three fibrinogen genes is upregulated as part of the acute phase inflammatory response (2,3).
Upon engagement of the clotting cascade, thrombin-mediated cleavage of the fibrinogen Aα and Bβ chains creates fibrin monomers and a platform for the polymerization of fibrin monomers into protofibrils and an insoluble web of stable fibrin fibers (4,5). Whereas thrombin is the enzyme that drives fibrin polymerization and clot formation, plasmin is the enzymatic counterpart that facilitates fibrinolysis and clot breakdown (6).
In addition to its position as a central node in the normal coagulation cascade, dysregulated fibrin deposition has been observed in pathological conditions such as cancer and viral infection (7,8).
The fibrinogen gamma chain is expressed as two isoforms that result from alternative mRNA splicing, the γA chain and the γ' chain. Research studies have shown that the fibrinogen gamma chain plays important roles in shaping the architecture of fibrin clots and modulates the innate immune response through interaction with its receptor, CD11b, expressed on neutrophils and monocytes (9,10).
Upon engagement of the clotting cascade, thrombin-mediated cleavage of the fibrinogen Aα and Bβ chains creates fibrin monomers and a platform for the polymerization of fibrin monomers into protofibrils and an insoluble web of stable fibrin fibers (4,5). Whereas thrombin is the enzyme that drives fibrin polymerization and clot formation, plasmin is the enzymatic counterpart that facilitates fibrinolysis and clot breakdown (6).
In addition to its position as a central node in the normal coagulation cascade, dysregulated fibrin deposition has been observed in pathological conditions such as cancer and viral infection (7,8).
The fibrinogen gamma chain is expressed as two isoforms that result from alternative mRNA splicing, the γA chain and the γ' chain. Research studies have shown that the fibrinogen gamma chain plays important roles in shaping the architecture of fibrin clots and modulates the innate immune response through interaction with its receptor, CD11b, expressed on neutrophils and monocytes (9,10).
- Chapin, J.C. and Hajjar, K.A. (2015) Blood Rev 29, 17-24.
- Dalmon, J. et al. (1993) Mol Cell Biol 13, 1183-93.
- Huber, P. et al. (1990) J Biol Chem 265, 5695-701.
- Lord, S.T. (2011) Arterioscler Thromb Vasc Biol 31, 494-9.
- Yang, Z. et al. (2000) Proc Natl Acad Sci U S A 97, 14156-61.
- Cesarman-Maus, G. and Hajjar, K.A. (2005) Br J Haematol 129, 307-21.
- Fernandez, P.M. et al. (2004) Semin Thromb Hemost 30, 31-44.
- Merad, M. and Martin, J.C. (2020) Nat Rev Immunol 20, 355-362.
- Yakovlev, S. et al. (2000) Biochemistry 39, 15721-9.
- Siebenlist, K.R. and Mosesson, M.W. (1994) J Biol Chem 269, 28414-9.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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