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1000 results found for “Allergy”
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Name :
C1QTNF2 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 2 Human Recombinant
Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.
Product # :
PRO-133Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C1QTNF2 Protein is a 29,640 Da protein containing 280 aa fused to a 10 aa N-Terminal His-tag.
Source
E. coli
Formulation
C1QTNF2 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.03M Acetate buffer, pH 4.
Citations
More Info
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Introduction
C1QTNF2 can be found in many different organism parts such as the testis, cervix. C1QTNF2 is located in the extracellular space and has various roles such as activation of MAPK activity, positive regulation of fatty acid oxidation, positive regulation of glycogen biosynthetic process, and positive regulation of glucose import.
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Synonyms
Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.
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Stability
Store lyophilized C1QTNF2 uman at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF2 an 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
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10?g/ml. In higher concentrations the solubility of this antigen is limited. 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
MKHHHHHHAS DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG RTGNRGKPGP KGKAGAIGRA GPRGPKGVNG TPGKHGTPGK KGPKGKKGEP GLPGPCSCGS GHTKSAFSVA VTKSYPRERL PIKFDKILMN EGGHYNASSG KFVCGVPGIY YFTYDITLAN KHLAIGLVHN GQYRIRTFDA NTGNHDVASG STILALKQGD EVWLQIFYSE QNGLFYDPYW TDSLFTGFLI YADQDDPNEV.
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 :
PI16 HumanDescription:
Peptidase Inhibitor 16 Human Recombinant
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Product # :
ENZ-113Price :
Quantity :
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Shipped at Room temp
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Description
The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
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Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PI16 Human recombinant 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 0.5mg/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
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.
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 :
PTX3 Human, HEKDescription:
Pentraxin-3 Human Recombinant, HEK
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
Product # :
PRO-2041Price :
Quantity :
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Shipped at Room temp
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Description
Pentraxin-3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Glu18-Ser381) containing a total of 370 amino acids, having a calculated molecular mass of 41kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
PTX3 was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
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Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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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. PTX3 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
ENSDDYDLMY VNLDNEIDNG LHPTEDPTPC DCGQEHSEWD KLFIMLENSQ MRERMLLQAT DDVLRGELQR LREELGRLAE SLARPCAPGA PAEARLTSAL DELLQATRDA GRRLARMEGA EAQRPEEAGR ALAAVLEELR QTRADLHAVQ GWAARSWLPA GCETAILFPM RSKKIFGSVH PVRPMRLESF SACIWVKATD VLNKTILFSY GTKRNPYEIQ LYLSYQSIVF VVGGEENKLV AEAMVSLGRW THLCGTWNSE EGLTSLWVNG ELAATTVEMA TGHIVPEGGI LQIGQEKNGC CVGGGFDETL AFSGRLTGFN IWDSVLSNEE IRETGGAESC HIRGNIVGWG VTEIQPHGGA QYVSHHHHHH.
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 :
Resistin Human, HEKDescription:
Resistin Human Recombinant, HEK
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
Product # :
CYT-1183Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.
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Synonyms
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
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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
KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP 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 :
EGFR Antibody (PAT2H8AT)Description:
Epidermal Growth Factor Receptor Clone PAT2H8AT, Mouse Anti Human
ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.
Product # :
ANT-751Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
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Introduction
Epidermal growth factor receptor or EGFR or Erb-1 is a membranal protein that acts as a receptor for the extracellular EGF proteins family. This protein is a part of a family of receptors called ErbB family which are all tyrosine kinases receptors. Mutations in the gene of this receptors can cause cancer.
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Synonyms
ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human EGFR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EGFR amino acids 424-605 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PAT2H8AT.
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Applications
EGFR antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
EGFR antibody was purified from mouse ascitic fluids by protein-G 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.
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Name :
CXCL11 Human (63-87 a.a.)Description:
ITAC (63-87 a.a.) Human Recombinant
ITAC, I-TAC, CXCL-11, CXCL11.
Product # :
CHM-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
ITAC, I-TAC, CXCL-11, CXCL11.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized I-TAC 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.
What is the molecular weight/Mw of CXCL11 HUMAN (63-87 A.A.) Protein?
CXCL11 HUMAN (63-87 A.A.) Protein has a total Mw of 9kDa.
What is the source or expression system of CXCL11 HUMAN (63-87 A.A.) Protein?
Escherichia Coli.
What is the Purity of CXCL11 HUMAN (63-87 A.A.) Protein?
CXCL11 HUMAN (63-87 A.A.) Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL11 HUMAN (63-87 A.A.) Protein?
The biological functionality of CXCL11 HUMAN (63-87 A.A.) Protein will be determined in the future.
What is the amino acid sequence of CXCL11 HUMAN (63-87 A.A.) Protein?
CXCL11 HUMAN (63-87 A.A.) Protein is composed from 25 amino acids.
What applications can CXCL11 HUMAN (63-87 A.A.) Protein be used in?
CXCL11 HUMAN (63-87 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL11 HUMAN (63-87 A.A.) Protein?
The endotoxin level is minimal, CXCL11 HUMAN (63-87 A.A.) Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL11 HUMAN (63-87 A.A.) that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL11 HUMAN (63-87 A.A.)?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CHIKV E1Description:
Chikungunya E1 Recombinant
Product # :
CHI-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Chikungunya E1 produced in E.coli having a molecular weight of 42kDa.
Source
Escherichia Coli.
Formulation
Sterile Filtered solution containing PBS and 25mM K2CO3.
Purity
Protein is >90% pure as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chikungunya is an infection caused by the chikungunya virus which is passed to humans by two species of mosquito of the genus Aedes: A. albopictus and A. aegypti. Animal reservoirs of the virus include monkeys, birds, cattle, and rodents. The features of the disease are a sudden onset of fever 2-4 days after exposure. The fever typically lasts 2-7 days, while the associated joint pains usually last weeks or months but sometimes years. The mortality rate is a little less than 1 in 1,000. The disease has occurred in outbreaks in Asia, Europe and the Americas since 2004. CHIKV is a single-stranded positive-sense RNA genome, 11,800 nts long which encodes 2 open reading frames. The nucleocapsid is tightly enveloped by a host-derived lipid bilayer (envelope) supporting the virus-encoded envelope proteins. 80 glycoprotein spikes are C- terminally anchored within the viral envelope. The structural polyprotein is translated from a viral sub genomic mRNA, while as the 5 structural proteins (capsid, E3, E2, 6K, E1) are translated as a single polyprotein, from which capsid (C) is cleaved off to encapsidate. The envelope polyprotein precursor E3-E2-6K-E1 is translocated to the endoplasmatic reticulum. Polyprotein is processed by host signalases, resulting in E3, E2 & E1 forming viral hetero-trimeric spikes. The viral spikes majorly contains E2 and E1 facilitate cell receptor recognition, cell entry thru pH-dependent endocytosis and support viral budding.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CHIKV E1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
PNTVGVPYKTLVNRPGYSPMVLEMELLSVTLEPTLSLDYITCEYKTVIPSPYVKCCGTAECKDKSLPDYSC
KVFTGVYPFMWGGAYCFCDTENTQLSEAHVEKSESCKTEFASAYRAHTASASAKLRVLYQGNNVTVSAY
ANGDHAVTVKDAKFIVGPMSSAWTPFDNKIVVYKGDVYNMDYPPFGAGRPGQFGDIQSRTPESEDVYAN
TQLVLQRPSAGTVHVPYSQAPSGFKYWLKERGASLQHTAPFGCQIATNPVRAMNCAVGNMPISIDIPDAAF
TRVVDAPSLTDMSCEVPACTHSSDFGGVAIIKYAASKKGKCAVHSMTNAVTIREAEIEVEGNSQLQISFSTAL
ASAEFRVQVCSTQVHCAAECHPPKDHIVNYPASHTTLGVQDISVTAMSWVQKITG
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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.
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Name :
CHIKV E2Description:
Chikungunya E2 Recombinant
Product # :
CHI-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Chikungunya E2 produced in E.coli having a molecular weight of 38kDa (migrates at 38-40kDa on 10% SDS-PAGE).
Source
Escherichia Coli.
Formulation
Sterile Filtered solution containing PBS and 25mM K2CO3.
Purity
Protein is >95% pure as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chikungunya is an infection caused by the chikungunya virus which is passed to humans by two species of mosquito of the genus Aedes: A. albopictus and A. aegypti. Animal reservoirs of the virus include monkeys, birds, cattle, and rodents. The features of the disease are a sudden onset of fever 2-4 days after exposure. The fever typically lasts 2-7 days, while the associated joint pains usually last weeks or months but sometimes years. The mortality rate is a little less than 1 in 1,000. The disease has occurred in outbreaks in Asia, Europe and the Americas since 2004. CHIKV is a single-stranded positive-sense RNA genome, 11,800 nts long which encodes 2 open reading frames. The nucleocapsid is tightly enveloped by a host-derived lipid bilayer (envelope) supporting the virus-encoded envelope proteins. 80 glycoprotein spikes are C- terminally anchored within the viral envelope. The structural polyprotein is translated from a viral sub genomic mRNA, while as the 5 structural proteins (capsid, E3, E2, 6K, E1) are translated as a single polyprotein, from which capsid (C) is cleaved off to encapsidate. The envelope polyprotein precursor E3-E2-6K-E1 is translocated to the endoplasmatic reticulum. Polyprotein is processed by host signalases, resulting in E3, E2 & E1 forming viral hetero-trimeric spikes. The viral spikes majorly contains E2 and E1 facilitate cell receptor recognition, cell entry thru pH-dependent endocytosis and support viral budding.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CHIKV E2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Rapid test and Immunoassay.
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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.
- View Data Sheet
Name :
LLODescription:
Listeriolysin-O Recombinant
Listeriolysin-O, LLO, hlyA.
Product # :
PRO-320Price :
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Shipped with Ice Packs
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Description
LLO is a single, non-glycosylated polypeptide chain containing 529 amino acids and having a molecular mass of 58kDa. (accession number: AAF64524).
Source
Escherichia Coli.
Formulation
The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, pH 6.4, 1mM DTT, 5% (v/v) glycerol and 0.5M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Hemolytic activity is 8,27E+05 HU/mg of protein where HU means hemolytic activity unit that is the amount of toxin needed to release half the hemoglobin (50% lysis) of the erythrocytes as determined by hemolysin assay.
Citations
More Info
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Introduction
Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.
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Synonyms
Listeriolysin-O, LLO, hlyA.
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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.
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 :
CCL15 68 a.a HumanDescription:
Macrophage Inflammatory Protein-5 (68 a.a) Human Recombinant (CCL15)
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Product # :
CHM-011Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.4kDa. The MIP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP5 was lyophilized from a 0.2µm filtered concentrated solution containing PBS, pH-7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.Citations
More Info
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Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
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Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 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
SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.
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Background
What is the molecular weight/Mw of CCL15 68 A.A HUMAN Protein?
CCL15 68 A.A HUMAN Protein has a total Mw of 7.4kDa.
What is the source or expression system of CCL15 68 A.A HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL15 68 A.A HUMAN Protein?
CCL15 68 A.A HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL15 68 A.A HUMAN Protein?
Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.
What is the amino acid sequence of CCL15 68 A.A HUMAN Protein?
SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.
What applications can CCL15 68 A.A HUMAN Protein be used in?
CCL15 68 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL15 68 A.A HUMAN Protein?
The endotoxin level is minimal, CCL15 68 A.A 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.
- View Data Sheet
Name :
TOR1A HumanDescription:
Torsin Family 1 Member A Human Recombinant
DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.
Product # :
PRO-1430Price :
Quantity :
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Shipped with Ice Packs
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Description
TOR1A Human Recombinant produced in E. coli is a single polypeptide chain containing 333 amino acids (21-332) and having a molecular mass of 38kDa. TOR1A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TOR1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.
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Synonyms
DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.
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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 MVEPISLGLA LAGVLTGYIY PRLYCLFAEC CGQKRSLSRE ALQKDLDDNL FGQHLAKKII LNAVFGFINN PKPKKPLTLS LHGWTGTGKN FVSKIIAENI YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA GAERITDVAL DFWRSGKQRE DIKLKDIEHA LSVSVFNNKN SGFWHSSLIH RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEIDEDIVSR VAEEMTFFPK EERVFSDKGC KTVFTKLDYY YDD.
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 :
HEV ORF2 (452-617 a.a.)Description:
Hepatitis E Virus ORF2 (452-617 a.a.) Recombinant
Product # :
HEV-236Price :
Quantity :
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Description
The E.Coli derived HEV protein contains the HEV immunodominant regions from ORF2 452-617 a.a. having a Mw. of 44.3 kDa. HEV ORF2 protein is fused to a 26kDa GST tag and purified by standard chromatography techniques.
Formulation
25mM Tris-HCl, 1mM EDTA, 0.5M urea and 50% glycerol.
Purity
HEV ORF2 protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF2 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HEV ORF2 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HEV with minimal specificity problems.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF2 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.
- View Data Sheet
Name :
IL10RA Human, ActiveDescription:
Interleukin 10 Receptor Alpha Human Recombinant, BioActive
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
Product # :
CYT-1142Price :
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Description
IL10RA Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 220 amino acids (22-235 aa) and having a molecular mass of 25.2kDa.IL10RA is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL10RA solution (0.2mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.
Citations
More Info
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Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
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Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
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Background
What is the molecular weight/Mw of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein has a total Mw of 25.2kDa.
What is the source or expression system of IL10RA HUMAN, ACTIVE Protein?
Sf9, Baculovirus cells.
What is the Purity of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IL10RA HUMAN, ACTIVE Protein?
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.
What is the amino acid sequence of IL10RA HUMAN, ACTIVE Protein?
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH.
What applications can IL10RA HUMAN, ACTIVE Protein be used in?
IL10RA HUMAN, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL10RA HUMAN, ACTIVE Protein?
The endotoxin level is minimal, IL10RA HUMAN, ACTIVE Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL10RA HUMAN, ACTIVE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL10RA HUMAN, ACTIVE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
Protein-A/G/LDescription:
Protein A/G/L Recombinant
Product # :
PRO-1936Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.
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 :
Gliadin NativeDescription:
Gliadin Triticum Aestivum Grain Native
Product # :
PRO-2675Price :
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Description
The native Gliadin Triticum Aestivum Grain is purified from wheat by protein chemical methods.
Formulation
Gliadin is supplied in 20mM HEPES buffer pH-7.4 and 6M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Gliadin is a common substrate of transglutaminase, which generates neo-epitopes by deamidation of glutamine side chains. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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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 IgA-type human auto antibodies in sera of patients diagnosed with celiac disease.2. Immunodot analysis with positive/negative samples.
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Applications
Western blot with patient sample.
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 :
ELANE MouseDescription:
Elastase-2 Mouse Recombinant
Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.
Product # :
ENZ-1105Price :
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Description
ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.
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Synonyms
Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.
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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
SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH HHHHH
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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
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Shipping Method :
Shipped at Room temp
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Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
Citations
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 standard solution of Brain-derived Neurotrophic Factor 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.
- View Data Sheet
Name :
SPIN1 HumanDescription:
Spindlin-1 Human Recombinant
Ovarian cancer-related protein, spindlin 1, SPIN, OCR.
Product # :
PRO-1184Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPIN1 Human Recombinant produced E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 32.0kDa.SPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SPIN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SPIN1 is a member of the SPIN/STSY family. SPIN1 is localized to nucleus, and expressed in several tissues and cells. SPIN1 takes part in cell-cycle regulation in the course of the transition from gamete to embryo.
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Synonyms
Ovarian cancer-related protein, spindlin 1, SPIN, OCR.
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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 MGSMKTPFGK TPGQRSRADA GHAGVSANMM KKRTSHKKHR SSVGPSKPVS QPRRNIVGCR IQHGWKEGNG PVTQWKGTVL DQVPVNPSLY LIKYDGFDCV YGLELNKDER VSALEVLPDR VATSRISDAH LADTMIGKAV EHMFETEDGS KDEWRGMVLA RAPVMNTWFY ITYEKDPVLY MYQLLDDYKE GDLRIMPDSN DSPPAEREPG EVVDSLVGKQ VEYAKEDGSK RTGMVIHQVE AKPSVYFIKF DDDFHIYVYD LVKTS
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 :
C6 HumanDescription:
Complement C6 Human
Complement component C6, C6.
Product # :
PRO-2693Price :
Quantity :
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Description
Human Complement C6 produced in Human plasma having a molecular mass of 105 kDa.
Source
Human Plasma.
Formulation
C6 protein solution contains phosphate buffer saline, pH 7.2.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
C6 is necessary for membrane attack complex formation and is activated by binding to recently-formed C5b at the cell membrane.Each pathway of complement activation generates proteolytic enzyme complexes which are bound to the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing C5a and activating C5b. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC. The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell.
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Synonyms
Complement component C6, C6.
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Physical Appearance
Sterile filtered solution.
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Stability
C6 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.
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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 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.
- View Data Sheet
Name :
EBI3 HumanDescription:
Epstein Barr Virus Induced 3 Human Recombinant
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Product # :
CYT-367Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 23.3kDa. The EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 Human Recombinant was lyophilized from a solution containing 10mM Acetic Acid and 0.5% Mannitol.
Purity
Greater than 90% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.Citations
More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 10mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK. -
Background
Title: Epstein-Barr Virus Induced 3 Human Recombinant: Unveiling its Role in Epstein-Barr Virus-Associated Diseases
Abstract:
Epstein-Barr Virus Induced 3 (EBI3) is a crucial cytokine involved in the immune response against Epstein-Barr virus (EBV) and various other pathogens. This research paper provides an extensive analysis of human recombinant EBI3, focusing on its production, characterization, and potential applications in understanding EBV-associated diseases. The paper highlights the significance of EBI3 in modulating immune responses and explores its role in the pathogenesis of EBV-related malignancies. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EBI3 in immune disorders and cancer. The information presented in this paper aims to enhance our understanding of human recombinant EBI3 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Epstein-Barr Virus Induced 3 (EBI3) is a cytokine that plays a critical role in the immune response against EBV. Human recombinant EBI3, produced through genetic engineering techniques, provides a valuable tool for studying its immunomodulatory properties and exploring its potential therapeutic applications.Production and Characterization:
Recombinant EBI3 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EBI3.Role in EBV-Associated Diseases:
EBI3 is involved in the regulation of immune responses during EBV infection. It acts as a subunit of the heterodimeric cytokine interleukin-27 (IL-27), which plays a crucial role in anti-viral immunity. Recombinant EBI3 serves as a valuable tool for investigating the mechanisms underlying EBI3-mediated immune regulation and its potential implications in EBV-associated diseases, including infectious mononucleosis, nasopharyngeal carcinoma, and EBV-related lymphomas.Therapeutic Implications:
Dysregulation of the immune response is implicated in various immune disorders and cancers. Recombinant EBI3 holds promise as a potential immunotherapeutic agent due to its immunomodulatory properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant EBI3 in conditions such as autoimmune diseases, viral infections, and cancer.Conclusion:
Human recombinant EBI3 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in understanding EBV-associated diseases contribute to our understanding of immune regulation and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EBI3 offer promising avenues for improving outcomes in immune disorders and EBV-related malignancies.What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 23.3kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.
What is the amino acid sequence of EBI3 Protein?
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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 BmpADescription:
Borrelia Afzelii Basic Membrane Protein A Recombinant
Product # :
BOR-012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Afzelii Basic Membrane Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 36,227 Dalton. Borrelia Afzelii BmpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Afzelii BmpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% 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).
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Applications
Western blot with Lyme positive plasma.
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 :
IL4 Human, HisDescription:
Interleukin-4 Human Recombinant, His Tag
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-483Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Interleukin-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-4 His-Tag is supplied in 20mM Tris-HCl and10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.
SDS-PAGE
Citations
More Info
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Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
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Background
Recombinant IL-4 (Interleukin-4) is a bioengineered version of a naturally occurring cytokine, which plays a crucial role in the immune system. IL-4 is primarily produced by activated T cells, mast cells, and basophils, and it is involved in the regulation of immune responses, including the differentiation of T helper cells, B cell activation, and the production of immunoglobulins.Recombinant IL-4 is synthesized using recombinant DNA technology, which involves inserting the gene encoding IL-4 into a suitable expression system, such as bacteria, yeast, or mammalian cells. The host cells are then cultured, allowing them to produce the desired protein, which can be purified and used for various applications.One of the main functions of IL-4 is to promote the differentiation of naïve CD4+ T cells into T helper 2 (Th2) cells. Th2 cells are essential for coordinating immune responses against extracellular pathogens, such as parasites and allergens. They achieve this by secreting cytokines, including IL-4 itself, IL-5, and IL-13, which stimulate B cells to produce specific antibodies, eosinophils to combat parasites, and mast cells to release histamine and other inflammatory mediators.Recombinant IL-4 has been extensively studied for its potential therapeutic applications. It has been shown to have anti-inflammatory properties, making it a potential candidate for the treatment of autoimmune and inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and inflammatory bowel disease. Additionally, IL-4 has been found to inhibit the growth of certain cancer cells, suggesting that it may have potential as an anti-cancer agent.However, the use of recombinant IL-4 as a therapeutic agent is not without challenges. One of the main concerns is the potential for adverse effects due to its immunomodulatory properties. For example, excessive IL-4 activity can lead to the development of allergies and asthma, as it promotes the production
What is the molecular weight/Mw of IL 4 HUMAN, HIS Protein?
IL 4 HUMAN, HIS Protein has a total Mw of 17.2kDa.
What is the source or expression system of IL 4 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of IL 4 HUMAN, HIS Protein?
IL 4 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 4 HUMAN, HIS Protein?
The ED50 for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.
What is the amino acid sequence of IL 4 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
What applications can IL 4 HUMAN, HIS Protein be used in?
IL 4 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 4 HUMAN, HIS Protein?
The endotoxin level is minimal, IL 4 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 4 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 4 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
TACI Human, Sf9Description:
Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9
Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.
Product # :
CYT-982Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
TACI a protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.
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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
ADLMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
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 :
TACI HumanDescription:
Tumor Necrosis Factor Receptor 13B Human Recombinant
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Product # :
CYT-819Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- purity
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Description
TACI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18.0kDa.
Source
Escherichia Coli.
Formulation
TACI protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/ml corresponding to a specific activity of 334-1000 IU/mg.Citations
More Info
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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
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Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TACI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TACI 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 TACI 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
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV
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.