Description
Fibrinogen Polyclonal Antibody – Affinity Purified
Affinity’s Fibrinogen Polyclonal Antibody – Affinity Purified is the highest level of our Fibrinogen antibody family. During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen. The result is a very high-purity product with a substantially higher titre than whole or purified IgG. Our Fibrinogen Polyclonal Antibody – Affinity Purified is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and is intended for applications such as immunoblotting, immunostaining of cells and several types of immunoassays where the higher signal-to-noise ratio achieved with this enriched product is required.
Product Code: SAFG-AP
Retail Product Size:0.5mg vial
Host Animal: Sheep Anti-Human Fibrinogen Polyclonal Antibody – Affinity Purified
Species Cross Reactivity: View Chart
Product Datasheet: Fibrinogen Polyclonal Antibody, affinity purified anti-human Sheep IgG
Description of Fibrinogen (Fg)
Human fibrinogen is a 340 kDa plasma protein produced in the liver. Plasma concentrations are typically 1.7 – 3.5 g/L (5-10 μM). The intact fibrinogen molecule consists of two identical subunits, each consisting of three non-identical polypeptide chains denoted as Aα, Bβ and γ. The letters A and B in the Aα and Bβ chains designate, respectively, fibrinopeptide A (FpA, residues 1-16), and fibrinopeptide B (FpB, residues 1-14), which are cleaved by thrombin upon conversion of fibrinogen to fibrin. The fibrin monomers polymerize in a half-overlap fashion to form insoluble fibrin fibrils. The polymerised fibrin is subsequently stabilized by activated Factor XIII that forms amide linkages between γ chains and, to a lesser extent, α chains of the fibrin molecules.
Proteolysis of fibrinogen by plasmin initially liberates C-terminal residues from the Aα chain to produce fragment X (intact D-E-D, which is still clottable). Fragment X is further degraded to non-clottable fragments Y (D-E) and D. Fragment Y can be digested into its constituent D and E fragments. Proteolysis of crosslinked fibrin by plasmin results in fragment DD (D-Dimer consisting of the D domains of 2 fibrin molecules crosslinked via the γ chains), fragment E (central E domain) as well as DDE in which fragment E is non-covalently associated with DD. The molecular weights of the cleavage fragments produced from human crosslinked fibrin are: 184 kDa for fragment DD, 92 kDa for D, 50 kDa for E, 1.54 kDa for FpA and 1.57 kDa for FpB.
Most of the fibrinogen in the circulation consists of 2 copies of each chain (Aα2, Bβ2, γA2), but in normal plasma approximately 10% of the fibrinogen molecules contain one γA chain and one variant γ chain (termed γ′), in which the c-terminal AGDV residues are replaced with the amino acid sequence VRPEHPAETEYDSLYPEDDL. This variant fibrinogen is commonly referred to as fibrinogen gamma prime (γA/γ′) but has also been called fibrinogen 2 or peak 2 fibrinogen because it elutes separately from fibrinogen 1 (γA2) by ion exchange chromatography. Residues 414-427 of the γ′ chain of fibrin gamma prime (contain a high-affinity binding site for exosite II of thrombin, which allows the active site of bound thrombin to remain available to interact with substrates while demonstrating resistance to heparin mediated inhibition by antithrombin1-4.
References and Reviews
- Hantgan RR, Francis CW, Marder VJ; Fibrinogen Structure and Physiology; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 277-300, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
- Binnie CG, Lord ST; The Fibrinogen Sequences that Interact with Thrombin; Blood 81, pp 3186-3192, 1993.
- Pospisil CH, Stafford AR, Fredenburgh JC, Weitz JI; Evidence that both Exosites on Thrombin Participate in Its High Affinity Interaction with Fibrin; JBC 278, pp 21584-21591, 2003.
- Medved L, Weisel JW; Recommendations for Nomenclature on Fibrinogen and Fibrin; JTH 7, pp 355-359, 2009.
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单抗标签选择的一抗范围比较小一些,多抗标签选择的一抗范围可能相对大一些。而商品化二抗基本没什么差别。不管是选择什么样的抗体,在Western blot检测方面都是一样的
所以做Western blot的单抗和多抗标签并没有什么不同
例如 GST (1-109):
•epitope corresponding to amino acids 1-109 mapping at the N-terminus of GST of Schistosoma japonicum origin
•recommended for detection of GST fusion proteins and glutathione-S-transferase (GST) of Schistosoma japonicum origin by WB, IP, IF and ELISA
还有Schistosoma japonicum origin 跟我载体pGEX4T-1表达的融合蛋白可用Western Blot吗?它们有什么关系?
十分感谢
抗体指机体的免疫系统在抗原刺激下,由B淋巴细胞分化成的浆细胞所产生的、可与相应抗原发生特异性结合反应的免疫球蛋白.
载体,你说的是那种载体?生命科学载体有2种,一种是分布于膜上的载体蛋白,和物质运输有关.另一种是基因工程里面的携带外源DNA的一段DNA片段,例如质粒、噬菌体和动植物病毒.
所以,抗体全部是蛋白质,载体部分是蛋白质.
选择Flag标签抗体,主要根据实验的需要。一个抗体检测后应用类型越多,使用中选择余地就越大。要综合考虑抗体来源,特异性,稳定性,效价等等因素
想做个蛋白的定位,可是没有好抗体,就想做个转基因小鼠,在基因后面加一个标签。但是之前没有相关经验,不知道哪一种tag更好呢,更适合在小鼠里表达呢?因为我蛋白比较小,加GFP那么大的话可能会影响表达。比较小的tag例如HA,Flag还有His等,不知道哪个更适合一些?求大神们给些经验。