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1000 results found for “Serum Amyloid A”
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Name :
LECT1 (214-333) HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1857Price :
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Shipped with Ice Packs
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.
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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Name :
LITAF HumanDescription:
Lipopolysaccharide-Induced TNF Factor Human Recombinant
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
Product # :
PRO-1350Price :
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Description
LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LITAF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.
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Synonyms
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.
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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Name :
HBA2 HumanDescription:
Hemoglobin, Alpha 2 Human Recombinant
Hemoglobin alpha chain, hemoglobin alpha 2, hemoglobin subunit alpha, Alpha-globin, alpha-2 globin, HBH.
Product # :
PRO-1183Price :
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Description
HBA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 179 amino acids (1-142) and having a molecular mass of 19.5 kDa.HBA2 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HBA2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 2M urea and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HBA2 is a member of the globin family. HBA2 takes part in oxygen transport from the lung to the different peripheral tissues. The coding sequences of HBA2 and HBA1 are equal but have a small difference over the 5' untranslated regions and the introns, and a large difference over the 3' untranslated regions. HbA is constituted from two alpha chains and two beta chains which in standard adult life hold about 97% of the total hemoglobin; alpha chains associate with delta chains to create HbA-2 that with HbF (fetal hemoglobin) form the remaining 3% of adult hemoglobin. Alpha thalassemia is caused by removal of each of the alpha genes or removal of both HBA2 and HBA1; nondeletion alpha thalassemias has also been reported.
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Synonyms
Hemoglobin alpha chain, hemoglobin alpha 2, hemoglobin subunit alpha, Alpha-globin, alpha-2 globin, HBH.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMVL SPADKTNVKA AWGKVGAHAG EYGAEALERM FLSFPTTKTY FPHFDLSHGS AQVKGHGKKV ADALTNAVAH VDDMPNALSA LSDLHAHKLR VDPVNFKLLS HCLLVTLAAH LPAEFTPAVH ASLDKFLASV STVLTSKYR
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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Name :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
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Shipped at Room temp
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Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
Citations
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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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Name :
HBsAg Native, ayDescription:
Hepatitis B Surface Antigen, Native ay
Product # :
HBS-003Price :
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Description
HbsAg ay subtype purified Human Hepatitis B positive plasma, having a Mw weight corresponding to p24, gp27, p33 and gp36 as shown on SDS-PAGE.
Source
Human Hepatitis B positive plasma.
Formulation
Sterile Filtered solution containing 15mM NaN3, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins and is commonly referred to as the Australian Antigen. HBsAg is an essential parameter to diagnose hepatitis B disease in the clinic and to monitor antiviral treatment.
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Physical Appearance
Filtered opalscent solution.
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Stability
HBsAg should be stored at 4°C. DO NOT FREEZE.
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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Name :
SERPINA5 Human, ActiveDescription:
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-2523Price :
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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.
Citations
More Info
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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.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
GDNF HumanDescription:
Glial-Derived Neurotrophic Factor Human Recombinant
ATF1, ATF2, HFB1-GDNF, GDNF.
Product # :
CYT-305Price :
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Shipped at Room temp
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Description
Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
sds-page
Citations
More Info
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Introduction
GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake. -
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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.
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Solubility
It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
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Background
What is the molecular weight/Mw of GDNF HUMAN Protein?
GDNF HUMAN Protein has a total Mw of 30kDa.
What is the source or expression system of GDNF HUMAN Protein?
Escherichia Coli.
What is the Purity of GDNF HUMAN Protein?
GDNF HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN Protein?
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
What is the amino acid sequence of GDNF HUMAN Protein?
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
What applications can GDNF HUMAN Protein be used in?
GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN Protein?
The endotoxin level is minimal, GDNF 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.
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Name :
ANXA2 HumanDescription:
Annexin A2 Human
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
Product # :
PRO-1573Price :
Quantity :
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Shipped at Room temp
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Description
The Human Annexin A2 produced from Human Adipose Tissue has a molecular mass of 38.472kDa (calculated without glycosylation) containing 338 amino acid residues.
Source
Human Adipose Tissue.
Formulation
ANXA2 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl and pH 6.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.
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Synonyms
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
STVHEILCKL SLEGDHSTPP SAYGSVKAYT NFDAERDALN IETAIKTKGV DEVTIVNILT NRSNAQRQDI AFAYQRRTKK ELASALKSAL SGHLETVILG LLKTPAQYDA SELKASMKGL GTDEDSLIEI ICSRTNQELQ EINRVYKEMY KTDLEKDIIS DTSGDFRKLM VALAKGRRAE DGSVIDYELI DQDARDLYDA GVKRKGTDVP KWISIMTERS VPHLQKVFDR YKSYSPYDML ESIRKEVKGD LENAFLNLVQ CIQNKPLYFA DRLYDSMKGK GTRDKVLIRI MVSRSEVDML KIRSEFKRKY GKSLYYYIQQ DTKGDYQKAL LYLCGGDD.
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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Name :
SIRPA Human, HEKDescription:
Signal-Regulatory Protein Alpha Human Recombinant, HEK
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptorSHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
Product # :
PRO-2755Price :
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Description
SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The SIRPA solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human CD47.
Citations
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA. -
Synonyms
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR. -
Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY HHHHHH.
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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Name :
VAMP2 Human, (1-94)Description:
Synaptobrevin-2 Human Recombinant, (1-94)
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
Product # :
PRO-2644Price :
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Description
VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
The VAMP2 solution (0.5mg/1ml) contains 0.1mM PMSF, 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Synaptobrevin-2 or VAMP2 is a protein that has a proline-rich N-terminal part, highly conserved hydrophilic domain, a transmembrane anchor and a C-terminal.VAMP2 found in the transmembrane region of the cell, in the cytoplasmic surface of the synaptic vesicle. The protein is mainly found in the Langerhans islets in the pancreas and glomerular cells in the kidney. A SNARE complex is created within the protein’s N-terminal domain and the target membrane-associated T.
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Synonyms
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.
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.
- View Data Sheet
Name :
F8 ProteinDescription:
Coagulation Factor-VIII Human Recombinant
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Antihemophilic Facor Human Recombinant produced in CHO is a glycosylated polypeptide chain having 2332 amino acids. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
CHO cells (Chinese Hamster Ovarian Cells).
Formulation
Each 250IU vial was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 7,058 IU/mg.Citations
More Info
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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
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Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute 250IU lyophilized Factor-VIII in 5ml sterile 18M-cm H2O, which can then be further diluted to other aqueous solutions.
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.
- View Data Sheet
Name :
Activin A HumanDescription:
Activin A Human Recombinant
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
Product # :
CYT-569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 15.2 kDa.What is the source or expression system of Activin A Protein?
E.ColiWhat is the Purity of Activin A Protein?
Activin A Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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.
- View Data Sheet
Name :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
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Shipped with Ice Packs
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Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
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Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
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Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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.
- View Data Sheet
Name :
Borrelia Afzelii OspADescription:
Borrelia Afzelii Outer Surface Protein A Recombinant
Product # :
BOR-011Price :
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Description
Recombinant Borrelia Afzelii Outer Surface Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 30kDa. Borrelia Afzelii OspA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Afzelii OspA is supplied in 20mM HEPES buffer pH-8.0 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
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.
- View Data Sheet
Name :
IL17A Human, Sf9Description:
Interleukin 17A Human Recombinant, Sf9
Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.
Product # :
CYT-895Price :
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Shipped with Ice Packs
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Description
IL17A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-155 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 138 amino acids and having a molecular mass of 15.9kDa.IL17A shows multiple bands between 13.5-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL17A protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM EDTA and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 7 ng/ml. The activity is determined by the IL-6 ELISA in a using NIH/3T3 mouse embryonic fibroblast cells.
Citations
More Info
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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
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Synonyms
Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
GITIPRNPGC PNSEDKNFPR TVMVNLNIHN RNTNTNPKRS SDYYNRSTSP WNLHRNEDPE RYPSVIWEAK CRHLGCINAD GNVDYHMNSV PIQQEILVLR REPPHCPNSF RLEKILVSVG CTCVTPIVHH VAHHHHHH
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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Name :
SAE1/SAE2 HumanDescription:
SAE1/SAE2 Human Recombinant
Product # :
ENZ-1161Price :
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Description
SAE1/SAE2 Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 2 subunits (SAE1 subunit molecular mass is 41kDa & SAE2 subunit molecular mass is 91kDa). The subunits associate to form a complex. The SAE1/SAE2 is expressed with a -10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SAE1/SAE2 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SAE1 and SAE2 form heterodimers which take part in the posttranslational modification of proteins (sumoylation). This process regulates protein structure as well as intracellular localization of the target. SAE1/SAE2 may indicate on dermatomyositis (DM) as autoantibodies against those 2 proteins have been found in patients.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.
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coating concentration
0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with anti SAE1/SAE2 autoantibody positive sample & Polyclonal anti-SAE1 and anti-SAE2 antibodies.
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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Name :
Ara h 2.0201Description:
Allergen Ara h 2.0201 (Conglutin-7) Recombinant
Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.
Product # :
ALR-007Price :
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Description
Recombinant Allergen Ara h 2.0201 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20,000 Dalton. Ara h 2.0201 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Ara h 2.0201 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.
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Synonyms
Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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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.
- View Data Sheet
Name :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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.
- View Data Sheet
Name :
S100A1 MouseDescription:
S100 Calcium Binding Protein A1 Mouse Recombinant
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
Product # :
PRO-237Price :
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Description
S100A1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-94 a.a) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).S100A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. -
Synonyms
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSELESAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK ELDENGDGEV DFKEYVVLVA ALTVACNNFF WETS.
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.
- View Data Sheet
Name :
AHSG HumanDescription:
Alpha-2-HS-Glycoprotein Human Recombinant
PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.
Product # :
PRO-1450Price :
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Description
AHSG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (19-367 a.a) and having a molecular mass of 39.7kDa (Molecular size on SDS-PAGE will appear higher).AHSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AHSG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.
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Synonyms
PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAPHGPGL IYRQPNCDDP ETEEAALVAI DYINQNLPWG YKHTLNQIDE VKVWPQQPSG ELFEIEIDTL ETTCHVLDPT PVARCSVRQL KEHAVEGDCD FQLLKLDGKF SVVYAKCDSS PDSAEDVRKV CQDCPLLAPL NDTRVVHAAK AALAAFNAQN NGSNFQLEEI SRAQLVPLPP STYVEFTVSG TDCVAKEATE AAKCNLLAEK QYGFCKATLS EKLGGAEVAV TCTVFQTQPV TSQPQPEGAN EAVPTPVVDP DAPPSPPLGA PGLPPAGSPP DSHVLLAAPP GHQLHRAHYD LRHTFMGVVS LGSPSGEVSH PRKTRTVVQP SVGAAAGPVV PPCPGRIRHF KV.
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.
- View Data Sheet
Name :
AICDA HumanDescription:
Activation-Induced Cytidine Deaminase Human Recombinant
Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
Product # :
ENZ-651Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
AICDA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198) and having a molecular mass of 26.1kDa.AICDA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AICDA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Activation-Induced Cytidine Deaminase (AICDA) belongs to the the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. AICDA is necessary for a number of crucial steps of B-cell terminal differentiation needed for efficient antibody responses. AICDA has a role in the epigenetic regulation of gene expression by participating in DNA demethylation. AICDA is strongly expressed in the lymph nodes and tonsils.
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Synonyms
Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSLLMNRRK FLYQFKNVRW AKGRRETYLC YVVKRRDSAT SFSLDFGYLR NKNGCHVELL FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVADFLRG NPNLSLRIFT ARLYFCEDRK AEPEGLRRLH RAGVQIAIMT FKDYFYCWNT FVENHERTFK
AWEGLHENSV RLSRQLRRIL LPLYEVDDLR DAFRTLGL.
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.
- View Data Sheet
Name :
SGTA HumanDescription:
Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha Human Recombinant
alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.
Product # :
PRO-807Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
SGTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-313 a.a.) and having a molecular mass of 35.1 kDa. SGTA protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SGTA Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.
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Synonyms
alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR SRTPSASNDD QQELEHHHHH H.
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.
- View Data Sheet
Name :
TFF1 HumanDescription:
Trefoil Factor-1 Human Recombinant
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Product # :
CYT-586Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.
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 a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.Citations
More Info
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Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
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Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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.
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Solubility
It is recommended to reconstitute the lyophilized TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
PNTIDVPPEEECEF.
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.
- View Data Sheet
Name :
PRKAA1 HumanDescription:
Protein Kinase, AMP-Activated, Alpha 1 Human Recombinant
5'-AMP-activated protein kinase catalytic subunit alpha-1, Protein Kinase, AMP-Activated, Alpha 1, PRKAA1, AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, Tau-protein kinase PRKAA1, AMPK1, 5-AMP-activated protein kinase catalytic subunit alpha-1 isoform 1, AMPK, AMPKa11.
Product # :
PKA-074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRKAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279a.a) and having a molecular mass of 34.3kDa.PRKAA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PRKAA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Protein Kinase, AMP-Activated, Alpha 1 (PRKAA1) is a protein coding gene which is the catalytic subunit of AMPK. AMPK is an energy sensor protein kinase which regulates cellular energy metabolism. AMPK adjusts the activity of various important metabolic enzymes by direct phosphorylation. Among its other features, AMPK protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.
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Synonyms
5'-AMP-activated protein kinase catalytic subunit alpha-1, Protein Kinase, AMP-Activated, Alpha 1, PRKAA1, AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, Tau-protein kinase PRKAA1, AMPK1, 5-AMP-activated protein kinase catalytic subunit alpha-1 isoform 1, AMPK, AMPKa11.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMRRLSSW RKMATAEKQK HDGRVKIGHY ILGDTLGVGT FGKVKVGKHE LTGHKVAVKI LNRQKIRSLD VVGKIRREIQ NLKLFRHPHI IKLYQVISTP SDIFMVMEYV SGGELFDYIC KNGRLDEKES RRLFQQILSG VDYCHRHMVV HRDLKPENVL LDAHMNAKIA DFGLSNMMSD GEFLRTSCGS PNYAAPEVIS GRLYAGPEVD IWSSGVILYA LLCGTLPFDD DHVPTLFKKI CDGIFYTPQY LNPSVISLLK HMLQVDPMKR ATIKDIREHE WF.
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.