Search: 1000 results found for "fibrinogen"

Description:

FK506 Binding Protein 6, Mouse Anti Human

FKBP36, EC 5.2.1.8, FKBP-6, PPIase, MGC87179, FK506-binding protein 6, Rotamase.

Product # :

ANT-499

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
FKBP6 is part of the immunophilin protein family, and is involved in immunoregulation and basic cellular functions involving protein folding and trafficking. FKBP6 is widely expressed in all tissues, FKBP6 is present at utmost levels in testis, liver, kidney, skeletal muscle and heart. Deletion of FKBP6 contributes to hypercalcemia and growth delay in Williams-Beuren syndrome.
Synonyms
FKBP36, EC 5.2.1.8, FKBP-6, PPIase, MGC87179, FK506-binding protein 6, Rotamase.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human FKBP6 mAb, clone PAT9B7A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human FKBP6 protein 1-327 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
Clone
PAT9B7A
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
NCK1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Aspartylglucosaminidase Human Recombinant, sf9

Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.

Product # :

ENZ-990

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Description

AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH HH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active

Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.

Product # :

PRO-2523

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Description

SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SERPINA5 protein solution (0.5mg/ml) contains 150mM NaCl, 10% glycerol & 20 mM MES buffer (pH6.0).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.

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Introduction
SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease.
Synonyms
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Platelet Factor-4 Human Recombinant (CXCL4), His Tag

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-015

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Description

PF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (32-101 a.a) and having a molecular mass of 10kDa.PF4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PF4 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Frizzled Class Receptor 10 Human Recombinant

FZ-10, CD350, Fz10, FzE7, frizzled-10, hFz10, FZD10, frizzled class receptor 10.

Product # :

PRO-2819

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Description

FZD10 Human Recombinant is a single, glycosylated, polypeptide chain (21-225 a.a) containing a total of 444 amino acids and having a molecular mass of 50.0 kDa. FZD10is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The FZD10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Synonyms
FZ-10, CD350, Fz10, FzE7, frizzled-10, hFz10, FZD10, frizzled class receptor 10.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ISSMDMERPG DGKCQPIEIP MCKDIGYNMT RMPNLMGHEN QREAAIQLHE FAPLVEYGCH GHLRFFLCSL YAPMCTEQVS TPIPACRVMC EQARLKCSPI MEQFNFKWPD SLDCRKLPNK NDPNYLCMEA PNNGSDEPTR GSGLFPPLFR PQRPHSAQEH PLKDGGPGRG GCDNPGKFHH VEKSASCAPL CTPGVDVYWS REDKRLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALPAPIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.
Background
Frizzled-10 (FZD10) is a member of the Frizzled family of G protein-coupled receptors (GPCRs) that play critical roles in the Wnt signaling pathway, which is essential for various developmental processes, cell proliferation, and differentiation. Recombinant human FZD10 (rhFZD10) has been developed to facilitate research into its biological functions and potential therapeutic applications, particularly in the context of cancer and regenerative medicine. This paper provides a comprehensive overview of the scientific research on recombinant human FZD10, focusing on its biological functionality, detailed description, and physical properties.
Recombinant human FZD10 is primarily used to investigate the role of FZD10 in Wnt signaling and its implications in health and disease.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glycoprotein Ib Platelet Subunit Beta Human Recombinant

GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.

Product # :

PRO-2774

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Description

GP1BB Human Recombinant is a single, glycosylated, polypeptide chain (26-147 a.a) containing a total of 131 amino acids, having a molecular mass of 14.0 kDa. GP1BB is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The GP1BB solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSCPAPCSC AGTLVDCGRR GLTWASLPTA FPVDTTELVL TGNNLTALPP GLLDALPALR TAHLGANPWR CDCRLVPLRA WLAGRPERAP YRDLRCVAPP ALRGRLLPYL AEDELRAACA PGPLCHHHHH H.
Background
Glycoprotein 1b beta (GP1BB) is a crucial component of the platelet glycoprotein Ib-IX-V complex, playing a pivotal role in platelet function and hemostasis. This research aims to explore the structure, function, and implications of GP1BB protein in platelet adhesion, aggregation, and the development of thrombotic disorders. Understanding the molecular mechanisms and regulatory roles of GP1BB can provide valuable insights into its potential as a therapeutic target for thrombotic diseases.
Structure and Expression of GP1BB Protein:
GP1BB is a transmembrane protein consisting of an extracellular domain, a single transmembrane region, and a short cytoplasmic tail. It is predominantly expressed on the surface of platelets, where it interacts with von Willebrand factor (VWF) and other components of the glycoprotein Ib-IX-V complex. GP1BB is crucial for mediating platelet adhesion to damaged endothelium and the formation of stable platelet aggregates at the site of injury.
GP1BB and Platelet Adhesion:
GP1BB interacts with VWF, which is exposed upon vascular injury. This interaction facilitates the initial attachment of platelets to the damaged endothelium. GP1BB also participates in the formation of high-affinity bonds between platelets and VWF, contributing to the stabilization of platelet adhesion and the initiation of platelet aggregation. Dysregulation of GP1BB-mediated platelet adhesion can lead to abnormal clot formation and thrombotic disorders.
Implications of GP1BB in Thrombotic Disorders:
Defects or mutations in the GP1BB gene can result in Bernard-Soulier syndrome (BSS), a rare inherited bleeding disorder characterized by giant platelets, thrombocytopenia, and impaired platelet adhesion. BSS patients often experience excessive bleeding and bruising due to defective GP1BB function. On the other hand, abnormal activation or overexpression of GP1BB has been associated with increased risk of thrombotic events, such as myocardial infarction and stroke.
Therapeutic Strategies Targeting GP1BB:
Given its crucial role in platelet function and thrombotic disorders, GP1BB represents a potential target for therapeutic interventions. Strategies aimed at modulating GP1BB expression or function have been explored. This includes the development of monoclonal antibodies or small molecule inhibitors that selectively target GP1BB and interfere with its interaction with VWF or other binding partners. Such approaches aim to prevent excessive platelet adhesion and aggregation, reducing the risk of thrombotic events.
Challenges and Future Directions:
While targeting GP1BB shows promise, several challenges need to be addressed. The development of specific inhibitors or modulators of GP1BB that do not interfere with its physiological functions is crucial. Additionally, understanding the complex interplay between GP1BB and other platelet receptors and signaling pathways is essential for the development of effective therapeutic strategies.
Conclusion:
The study of GP1BB protein provides valuable insights into its central role in platelet adhesion, aggregation, and thrombotic disorders. Understanding the molecular mechanisms and functional implications of GP1BB opens avenues for the development of targeted therapies for thrombotic diseases. Further research on GP1BB protein, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to mitigate the risk of thrombotic events and improve patient outcomes.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Furin Human Recombinant

Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

Product # :

PRO-2199

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Description

FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Flagellin Recombinant

Product # :

PRO-1240

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Description

Flagellin Salmonella typhimurium Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids with Leu, Glu and a 6 × His at C-terminus and having a molecular mass of 52.7kDa.The Flagellin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

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Introduction
Flagellin arranges itself in a hollow cylinder to create the filament in bacterial flagellum. Flagellin is the key substituent of bacterial flagellum, and is found in large quantities on almost all flagellated bacteria.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flagellin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flagellin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Flagellin in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNLQ RVRELAVQSA NSTNSQSDLD SIQAEITQRL NEIDRVSGQT QFNGVKVLAQ DNTLTIQVGA NDGETIDIDL KQINSQTLGL DTLNVQQKYK VSDTAATVTG YADTTIALDN STFKASATGL GGTDQKIDGD LKFDDTTGKY YAKVTVTGGT GKDGYYEVSV DKTNGEVTLA GGATSPLTGG LPATATEDVK NVQVANADLT EAKAALTAAG VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY TADDGTSKTA LNKLGGADGK TEVVSIGGKT YAASKAEGHN FKAQPDLAEA AATTTENPLQ KIDAALAQVD TLRSDLGAVQ NRFNSAITNL GNTVNNLTSA RSRIEDSDYA TEVSNMSRAQ ILQQAGTSVL AQANQVPQNV LSLLRLEHHH HHH

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Description:

Interferon-Alpha 1b Human Recombinant

Product # :

CYT-283

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Description

Interferon-alpha 1b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids and having a molecular mass of 19.5 kDa. The Interferon-alpha 1b gene was obtained from human leukocytes. The IFN-a 1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution (50ug/ml) in PBS, pH 7.4, containing 4% mannitol and 1% HSA.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 10⁸ IU/ mg.

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Introduction
IFN-alpha 1b is produced by macrophages, IFN-alpha 1b has antiviral activities and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interferon alpha 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 1b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IFN alpha 1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Glu.
Background
What is the molecular weight/Mw of IFNA1 B Protein?
IFNA1 B Protein has a total Mw of 19.5kDa.

What is the source or expression system of IFNA1 B Protein?
Escherichia Coli.

What is the Purity of IFNA1 B Protein?
IFNA1 B Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA1 B Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 108 IU/ mg.

What is the amino acid sequence of IFNA1 B Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Glu.
What applications can IFNA1 B Protein be used in?
IFNA1 B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA1 B Protein?
The endotoxin level is minimal, IFNA1 B Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Human Thrombin

Product # :

PRO-339

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Description

Thrombin was purified from human plasma.

Source

Human Plasma.

Formulation

Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

Biological Activity

The specific activity was found to be 116 US Units/mg protein.

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Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
Physical Appearance
lyophilized powder.
Stability
Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IFN-alpha 7 Human Recombinant

IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

Product # :

CYT-196

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Quantity :

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source
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SDS-PAGE

Description

IFNA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a) and having a molecular mass of 22.3kDa.IFNA7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IFNA7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IFN alpha 7 (IFNA7) is a member of the alpha/beta IFN family. IFNA7 is generated by macrophages. IFN-alpha has antiviral functions. IFN promotes the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
Background
What is the molecular weight/Mw of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein has a total Mw of 22.3kDa.

What is the source or expression system of IFNA7 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA7 HUMAN Protein?
The biological functionality of IFNA7 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNA7 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
What applications can IFNA7 HUMAN Protein be used in?
IFNA7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA7 HUMAN Protein?
The endotoxin level is minimal, IFNA7 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Basigin Human Recombinant

Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.

Product # :

PRO-2516

Price :

Quantity :

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Description

BSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 428 amino acids (22-207a.a.) and having a molecular mass of 47.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BSG is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BSG protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.
Synonyms
Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPAAGTVFT TVEDLGSKIL LTCSLNDSAT EVTGHRWLKG GVVLKEDALP GQKTEFKVDS DDQWGEYSCV FLPEPMGTAN IQLHGPPRVK AVKSSEHINE GETAMLVCKS ESVPPVTDWA WYKITDSEDK ALMNGSESRF FVSSSQGRSE LHIENLNMEA DPGQYRCNGT SSKGSDQAII
TLRVRSHLAL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RAS-like, Estrogen-Regulated, Growth Inhibitor Human Recombinant

Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.

Product # :

PRO-106

Price :

Quantity :

Shipping Method :

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Description

RERG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RERG solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.
Synonyms
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Allergen Ara h 3.0101 Recombinant

Glycinin, Arah3.

Product # :

ALR-008

Price :

Quantity :

Shipping Method :

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Description

Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.
Synonyms
Glycinin, Arah3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-Basic Human Recombinant, Sf9

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-365

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Quantity :

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

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Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered liquid formulation.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 2 Protein?
Baculovirus.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.

What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interferon-gamma Canine Recombinant

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-404

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Recombinant IFNG Dog produced in E.coli cells is a non-glycosylated, homodimeric protein containing 143 amino acid chain and having a molecular mass of 16.9kDa. IFNG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IFNG was lyophilized from a 0.2µm filtered concentrated solution in 25mM Sodium Succinate, pH 5.0, 60mM NaCl, with 0.1% Tween-80.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNG should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IFNG in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK
Background
What is the molecular weight/Mw of IFNG CANINE Protein?
IFNG CANINE Protein has a total Mw of 16.9kDa.

What is the source or expression system of IFNG CANINE Protein?
Escherichia Coli.

What is the Purity of IFNG CANINE Protein?
IFNG CANINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNG CANINE Protein?
The ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of IFNG CANINE Protein?
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK

What applications can IFNG CANINE Protein be used in?
IFNG CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNG CANINE Protein?
The endotoxin level is minimal, IFNG CANINE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IFN Regulatory Factor-1 Human Recombinant

IRF-1, IRF1, MAR.

Product # :

CYT-449

Price :

Quantity :

Shipping Method :

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Description

IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
Synonyms
IRF-1, IRF1, MAR.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.

What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.

What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Hepatitis B Virus e-Antigen Recombinant

Product # :

HBV-272

Price :

Quantity :

Shipping Method :

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source
formulation
purity
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Description

Recombinant hepatitis B virus “e” antigen is fused to a His Tag and having a molecular mass of approximately 18kDa.

Source

Escherichia Coli.

Formulation

20mM Tris-Hcl, 0.5M NaCl and 0.8M imidazole.

Purity

Protein is >95%

More Info

Introduction
Hepatitis B virus is the main cause for human liver disease, chronic infection frequently causes liver cancer and cirrhosis. The HBV core gene codes 2 distinct protein products, a 21.5-kDa protein being assembled to form nucleocapsid particles designated HBcAg, which wraps the viral DNA as well as the viral polymerase and RNase H, and a precore protein, designated as HBeAg, which is directly to the endoplasmic reticulum, processed at N- and C-terminally and secreted as non-particulate e-anitgen (HBeAg). The pre-core protein contains an extra 29 N-terminal amino acids, serving as a signal peptide to direct the nascent polypeptide into secretory pathway. After the secretion, mature HBeAg is deleted at the residue 149 C-terminally and retains 10 precore residues N-terminally. HBcAg and HBeAg are distinctly recognized by antibodies but highly cross-reactive at the T-cell level.
The e antigen is found in the circulation, it is found during the active HBV infection, positive result indicates the risk for contagiousness, and is also used as indicator for the effectiveness of HBV treatment. Positive anti-HBeAg specifies an active stage of acute HBV infection that is in its final stages, the risk for contagiousness is dramatically reduced.
Stability
HBeAg although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
s klclgwlwgm didpykefga svellsflps dffpsirdll dtasalyrea lespehcsph htalrqailc
wgelmnlatw vgsnledpas relvvsyvnv nmglkirqll wfhiscltfg retvleylvs fgvwirtpta
yrppnapils tlpettvv
Purification Method
Purified by proprietary chromatographic technique.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Complement Factor H Human

Complement factor H, H factor 1, CFH, HF, HF1, HF2.

Product # :

PRO-2700

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Quantity :

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source
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Description

Human Complement Factor H produced in Human plasma having a total molecular mass of 155kDa.

Source

Human Plasma.

Formulation

CFH protein solution contains PBS, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Physical Appearance
Sterile filtered solution.
Stability
CFH Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epigen Human Recombinant, His Tag

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Product # :

CYT-794

Price :

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Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K
Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 12.1kDa.

What is the source or expression system of EPIGEN Protein?
Escherichia Coli.

What is the Purity of EPIGEN Protein?
EPIGEN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EPIGEN Protein?
The biological functionality of EPIGEN Protein will be determined in the future.

What is the amino acid sequence of EPIGEN Protein?
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ebola Zaire Recombinant Protein

Product # :

EVD-078

Price :

Quantity :

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Description

Nucleoprotein (NP) of Ebola virus has strong antigenicity in immune reactions. C-terminal of EBO-Z nucleoprotein was expressed and purified from E. coli, it migrated at 15kDa on SDS-PAGE and pI is 4.87. Ebola Zaire is fused to a c-terminal his tag and purified by a proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Ebola Zaire protein solution is supplied in Phosphate buffer and 0.02% sodium azide.

Purity

>95% pure as determined by 12% SDS-PAGE (Coomassie blue stain).

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Introduction
Ebolavirus (EVD) belongs to the Filoviridae family of proteins which is comprised of a single-strand, non-infectious RNA genome. EVD genome is about 19,000 base pairs long and covers 7 genes in the order 3'-UTR-NP-VP35-VP40-GP-VP30-VP24-L-5'-UTR. There are 4 different ebolaviruses such as: Zaire (EBO-Z), Sudan (EBO-S), Cote d’Ivoire (EBO-CI) and Reston (EBO-R) that differ in amino acid sequence and location of where the gene overlaps. Similar to filoviruses and ebolavirions, EVD is a filamentous element that could appear in 3 forms: shepherd's crook, U shape or a 6 shape. Ebolaviruses may be coiled, toroid, or branched. Most ebolavirions are 80nm wideand 14,000nm long.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Applications
Immunoassay.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Annexin A1 Human Recombinant

ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

Product # :

PRO-679

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Description

ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.
Synonyms
ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Hepatitis B Virus Core (1-186 a.a.) Recombinant

Product # :

HBV-232

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Description

The E.coli derived recombinant protein contains the HBV core immunodominant region amino acids 1-186, and fused to a His tag at N- terminus.

Formulation

25mM Tris-HCl pH-8.0, 1.5mM EDTA, 1.5mM Urea and 50% glycerol.

Purity

HBV Core protein is >90% pure as determined by 10% PAGE (Coomassie staining).

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Introduction
Hepatitis B is one of a few known non-retroviralviruses which employ reverse transcriptionas a part of its replication process. (HIV, a completely unrelated virus, also uses reverse transcription, but it is a retrovirus.) HBV invades the cell by binding to surface receptor and become internalized. The viral core particles then migrate to the hepatocyte nucleus and the partially double-stranded, relaxed circular genomes (RC-DNA) are repaired to form a covalently closed circular DNA (cccDNA), which is the template for viral genomic and sub-genomic RNAs by cellular RNA polymerase II. Of these, the pregenomic RNA(pgRNA is selectively packaged into progeny capsids and is then reverse-transcribed into new RC-DNA. The core can either bud into the endoplasmic reticulum to be enveloped or exported from the cell or recycled back into the genome for conversion to cccDNA.
Stability
HBV Core protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Specificity
Immunoreactive with sera HBV-infected individuals.
Purification Method
HBV Core protein was purified by proprietary chromatographic technique.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IFN-Alpha 2b Human Recombinant

IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

Product # :

CYT-205

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IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Background
IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.
There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.
The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.
All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.
What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

What is the source or expression system of IFN A 2B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

What is the amino acid sequence of IFN A 2B HUMAN Protein?
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
What applications can IFN A 2B HUMAN Protein be used in?
IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN Protein?
The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN alpha 2b as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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