Recombinant Human Fibrinogen Gamma Chain (FGG) Protein (His&Myc)

Name: Recombinant Human Fibrinogen Gamma Chain (FGG) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11041P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Fibrinogen Gamma Chain (FGG) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02679
Target Symbol	FGG
Synonyms	FGG; FIBG_HUMAN; Fibrinogen gamma chain; Fibrinogen gamma polypeptide; fibrinogen gamma-b chain
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	YVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
Expression Range	27-453aa
Protein Length	Full Length of Mature Protein
Mol. Weight	55.9 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Subcellular Location	Secreted.
Database References	HGNC: 3694 OMIM: 134850 KEGG: hsa:2266 STRING: 9606.ENSP00000336829 UniGene: PMID: 29995659 DNA sequencing revealed a novel heterozygous CCTTTGATG deletion in the exon 8 of FGG, leading to the deletion of Ala289, Phe290, and Asp291 in fibrinogen gamma-chain PMID: 29748775 The simultaneous retention of fibrinogen and APOB-lipoproteins in FSD can be detected in routinely stained histological sections. The analysis of protein structures unraveled the pathomorphogenesis of this unexpected phenomenon. Fibrinogen gamma chain mutations provoke conformational changes in the region of the globular domain involved in the "end-to-end" interaction, thus impairing the D-dimer formation PMID: 29244742 The D356V (D330V) mutation located in the C-terminus was predicted to be highly deleterious and to affect the function of the protein. The obtained computational results suggest that the substitution of the neutral amino acid valine for the acidic amino acid aspartic acid at position 356 results in an unwound conformation within 50 ns, which might contribute to defective polymerization. PMID: 27677677 Fibrinogen gamma acts as thrombomodulin II. (Review) PMID: 27784620 Gene analysis of the fibrinogen phenotype reveals the importance of polygenic co-regulation. PMID: 27771416 Fibrinogen gamma chain and complement factor H were found to be bound as a protein complex in the plasma of a patient with advanced ovarian cancer PMID: 28551622 Our data indicate that the amplitude and maximal velocity of coagulation curves from plasma samples from FGG p.Arg301(275)Cys dysfibrinogenemic patients were comparable to those from plasma samples with fibrinogen in the normal range, whereas the amplitude of coagulation curves from patients with acquired low fibrinogen levels was lower PMID: 28318107 These results suggest that among the elderly, gamma ' fibrinogen does not add much to cardiovascular disease prediction beyond traditional risk factors and total fibrinogen level. PMID: 27180117 rs2066865 polymorphism has an important role in the development of venous thromboembolism in the white race PMID: 28353616 Gene polymorphisms FGG C>T (rs6536024) were not associated with height, weight, or morbid obesity among European subjects. PMID: 27999448 A lower plasma concentration of gamma' gamma fibrinogen in healthy adults does not appear to increase venous thromboembolism risk. PMID: 26916295 In addition to the reduction of FG concentration expected by the nature of the mutation also a functional defect (hypodysfibrinogenemia) was found. Moreover this mutation seems to increase the risk of thrombosis warranting long term anticoagulation possibly in a combination with antiplatelet drugs. PMID: 26540127 congenital dysfibrinogenemia with a novel mutation in fibrinogen gamma chain (gamma322 Phe-->Ile, Fibrinogen Beijing) and haemophilia B in a family PMID: 25982359 5877G>A mutation in the exon 8 of the FGG gene is underlies the pathogenesis of congenital dysfibrinogenemia in a Chinese family. PMID: 27060305 Case Reports: clustering of mutations causing fibrinogen storage disease in the fibrinogen gamma chain between residues 284 and 375. PMID: 26039544 Data indicate that mutations of the fibrinogen (Fg) gene seem to aggregate to the D region of fibrinogen gamma chain (FGG) PMID: 26663050 Letter/Case Report: FGG 320Asp-Glu substitution that displayed both a quantitative and functional defect and presented as hypodysfibrinogenaemia. PMID: 25042726 Low FI levels are strongly associated with rare CFI variants and age-related macular degeneration. PMID: 25788521 Report role of gamma'-fibrinogen in control of hemostatic clot growth in the venous circulation. PMID: 25614284 Letter/Case Report: FGG 339CysSer mutation causes only hypofibrinogenaemia. Accompanying functionality change is due to increased sialylation and inheritance of the B448Lys allele. PMID: 25588350 Suggest gamma' fibrinogen concentrations reflect general inflammation that accompanies and may contribute to atherosclerotic CVD, instead of gamma' fibrinogen being a causal risk factor. PMID: 26494231 This study shows that homocysteine influences blood clot properties alone and in combination with total fibrinogen but not with fibrinogen gamma' isoform in Africans. PMID: 25688462 investigated molecular basis of dysfibrinogenaemia in a Chinese pedigree; sequencing results of proband revealed a novel heterozygous IVS9+1delG mutation of FGG gene; same results were found in her mother sister and daughter; concluded the mutation is responsible for the proband's dysfibrinogenaemia PMID: 25551304 Data indicate that leptin receptor gene (LEPR) single-nucleotide polymorphisms (SNPs) rs4291477 significantly associated with serum fibrinogen. PMID: 25296580 A novel mutation in FGG gene is associated with congenital hypofibrinogenemia. PMID: 26037343 Final clot structure may contribute to increased cardiovascular disease (CVD) risk in vivo through associations with other CVD risk factors independent from total or gamma' fibrinogen concentration. PMID: 25213709 Novel fibrinogen mutations (gammaTrp208Leu and gammaLys232Thr) leading to congenital hypofibrinogenemia in two unrelated Chinese families have been described. PMID: 24914742 Exploratory multilocus polygenic analyses with p <0.05 showed an association of optimism with SNPs in MAOA, IL10, and FGG genes, and an association of resilience with a SNP in MAOA. PMID: 24791650 While the gamma Ser313Gly mutation manifested as dysfibrinogenemia with a thrombotic background, the gamma Phe204Val mutation manifested as hypofibrinogenemia without clinical symptoms. PMID: 25074738 observed increased APC resistance in carriers of fibrinogen gamma gene (FGG) haplotype 2, which is associated with reduced levels of the alternatively spliced fibrinogen gamma' chain. We then studied the effects of fibrinogen and its gamma' chain on APC resistance. PMID: 24951429 novel causitive mutation is identified in a New Zealand family with hypofibrinogenaemia PMID: 24352576 elevated levels of gammaA/gammaA fibrinogen promote arterial thrombosis in vivo, whereas gammaA/gamma' does not PMID: 24916154 Reduced plasminogen binding and delayed activation render gamma'-fibrin more resistant to lysis than gammaA-fibrin. PMID: 25128532 report of 2 hypofibrinogenemias, Shizuoka III and Kanazawa II, caused by heterozygous nonsense mutation at the fibrinogen gamma-chain, gamma23X and gamma376X, respectively; analysis demonstrated the transcribed aberrant mRNAs from both gamma23X and gamma376X genes are degraded by nonsense-mediated mRNA decay and not translated to the truncated polypeptide PMID: 24011387 A heterozygous point mutation located in exon 3 of the FGG gene c.140C>T (p.Thr21Ile)was found in a patient and her mother, both of whom had hypofibrinogenemia. PMID: 24556703 A novel FGG mutation is associated with hypofibrinogenemia. PMID: 23492915 A decreased number of factor XIIIa+ cells is found in the lower dermis following pulsed dye laser treatment. PMID: 23645504 Results indicate that the alphaC domain of fibrinogen harbors a Zn(2+)-dependent heparin binding site. PMID: 23990470 Data indicate that the adhesive alpha-granule proteins fibrinogen and thrombospondin are concentrated in a fibrin polymerization-dependent "cap" on phosphatidylserine-expressing platelets that promotes their incorporation into thrombi. PMID: 23995838 Letter/Case Report: deep vein thrombosis associated with novel substitution (gamma346Gly-->Val) at an absolutely conserved site in the fibrinogen gamma chain. PMID: 23348147 fibrinogen gamma' may contribute to the development of portal vein thrombosis PMID: 23306717 Clot lysis time showed a stronger relationship with fibrinogen gamma' than with total fibrinogen, whereby increased fibrinogen gamma' delayed clot lysis. PMID: 23422752 HepG2 cell gamma' fibrinogen is disproportionately up-regulated by inflammatory responses induced by interleukin-6. PMID: 23036532 A novel congenital Fibrinogen Melbourne hypodysfibrinogenemia caused by g326Cys-Phe in the fibrinogen gamma chain, presenting as massive splanchnic venous thrombosis, has been described in one patient and his asymptomatic father. PMID: 22760446 Fibrinogen gamma' is associated with the formation of mechanically weaker, non-uniform clots composed of thin fibers. This is caused by direct disruption of protofibril formation by gamma'. PMID: 22463367 Fibrinogen residue gammaAla341 is important for the proper conformation of the gamma-module, maintaining calcium-binding site and 'A-a' interactions. PMID: 22437918 mechanical unraveling of fibrin(ogen) is determined by the combined molecular transitions that couple stepwise unfolding of the gamma chain nodules and reversible extension-contraction of the alpha-helical coiled-coil connectors PMID: 22078561 gamma' fibrinogen is associated with prevalent cardiovascular disease and with SNPs exclusively in and near the fibrinogen gene locus. PMID: 21757653 potential biomarker for assessing a patient's inflammatory state and associated cardiovascular disease risk PMID: 21174007

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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