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Name :
IFN b Mouse, HisDescription:
IFN Beta Mouse Recombinant, His Tag
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
Product # :
CYT-651Price :
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Shipped with Ice Packs
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Description
IFN beta Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (22-182 a.a.) and having a molecular mass of 22 kDa. Mouse IFN beta is fused to 21 amino acid at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IFN-Beta (0.25mg/ml) contains 20mM HEPES (pH6.0), 0.5M NaCl, 10% glycerol.
Purity
Greater than 95% as determined by Analysis by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
IFN-beta 1b has antiviral, antibacterial and anticancer activities.
Influenza A viruses not only inhibit IFN-beta gene induction but also supress Type-I IFN signaling via mechanism involving induction of the SOCS-3 protein.
Intracellular bacteria and cytosolic poly (dA-dT) trigger IFN-beta responses in different human cells without requiring human ZBP1. -
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
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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 MINYKQLQLQ ERTNIRKCQE LLEQLNGKIN LTYRADFKIP MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI VVRLLDELHQ QTVFLKTVLE EKQEERLTWE MSSTALHLKS YYWRVQRYLK LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF QN.
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Background
What is the molecular weight/Mw of IFN B MOUSE, HIS Protein?
IFN B MOUSE, HIS Protein has a total Mw of 22kDa.
What is the source or expression system of IFN B MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of IFN B MOUSE, HIS Protein?
IFN B MOUSE, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN B MOUSE, HIS Protein?
The biological functionality of IFN B MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of IFN B MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MINYKQLQLQ ERTNIRKCQE LLEQLNGKIN LTYRADFKIP MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI VVRLLDELHQ QTVFLKTVLE EKQEERLTWE MSSTALHLKS YYWRVQRYLK LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF QN.
What applications can IFN B MOUSE, HIS Protein be used in?
IFN B MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN B MOUSE, HIS Protein?
The endotoxin level is minimal, IFN B MOUSE, HIS 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 :
IRF3 HumanDescription:
IFN Regulatory Factor-3 Human Recombinant
IRF-3, IRF3, IFN Regulatory Factor 3.
Product # :
CYT-292Price :
Quantity :
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Shipped with Ice Packs
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Description
IRF-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (1-112) and having a molecular mass of 13 kDa.The IRF3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml in phosphate-buffered saline (PBS), pH 7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Members of the IFN regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates IFN-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn-alpha and ifn-beta promoters respectively. IRF-3 does not have any transcription activation domains.
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Synonyms
IRF-3, IRF3, IFN Regulatory Factor 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid IRF3 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.
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Background
What is the molecular weight/Mw of IRF3 HUMAN Protein?
IRF3 HUMAN Protein has a total Mw of 13kDa.
What is the source or expression system of IRF3 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF3 HUMAN Protein?
IRF3 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF3 HUMAN Protein?
The biological functionality of IRF3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF3 HUMAN Protein?
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.
What applications can IRF3 HUMAN Protein be used in?
IRF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF3 HUMAN Protein?
The endotoxin level is minimal, IRF3 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 :
LECT1 HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1846Price :
Quantity :
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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 144 amino acids (214-334) and having a molecular mass of 16.3kDa. 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 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1, 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 PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.
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 :
CTF1 Human, HisDescription:
Cardiotrophin-1 Human Recombinant, His Tag
CTF1, CT1, CT-1, Cardiophin 1.
Product # :
CYT-436Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Cardiotrophin His-Tagged Fusion Protein Human, produced in E. coli, is 22.5 kDa protein containing 200 amino acid residues of the human Cardiotrophin and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
CTF1 was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Purity of CTF1 Human Recombinant is greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
CTF1, CT1, CT-1, Cardiophin 1.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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. Protein 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
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 22.5kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The biological functionality of CTF1 Protein will be determined in the future.
What is the amino acid sequence of CTF1 Protein?
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
AITRL Human, T7Description:
AITRL Human Recombinant, T7 Tag
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
Product # :
CYT-807Price :
Quantity :
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Shipped with Ice Packs
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Description
AITRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (81-199 a.a) and having a molecular mass of 15kDa.AITRL is fused to a 15 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AITRL protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology. -
Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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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
MASMTGGQQM GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.
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Background
What is the molecular weight/Mw of AITRL Protein?
AITRL Protein has a total Mw of 15kDa.
What is the source or expression system of AITRL Protein?
Escherichia Coli.
What is the Purity of AITRL Protein?
AITRL Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of AITRL Protein?
The biological functionality of AITRL Protein will be determined in the future.
What is the amino acid sequence of AITRL Protein?
MASMTGGQQM GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.
What applications can AITRL Protein be used in?
AITRL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AITRL Protein?
The endotoxin level is minimal, AITRL 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 :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
Quantity :
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Shipped with Ice Packs
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
Citations
More Info
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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
IL 10 Anti-HumanDescription:
Interleukin-10, Mouse Anti-Human
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Product # :
ANT-112Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Formulation
1mg/ml in PBS (after reconstitution).
Citations
More Info
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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
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Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human IL-10.
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Ig Subclass
Mouse IgG1.
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Clone
NYR-HIL10.
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Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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Purification Method
Ion excahnge.
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 :
CTGF AntibodyDescription:
Mouse Anti Human Connective Tissue Growth Factor
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Product # :
ANT-699Price :
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
-
Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia. -
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CTGF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTGF protein 27-349 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
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Clone
PAT18E7AT.
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Applications
CTGF 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
CTGF antibody was purified by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SF20 HumanDescription:
MYDGF Human Recombinant
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.
Product # :
CYT-622Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
- Citations
Description
SF20 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 162 amino acids fragment (33-173) and having a total molecular mass of 18 kDa. C9orf10 is fused to 20 amino acids His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C9orf10 is supplied in 20mM Tris HCL pH-8 and 20% glycerol.
Purity
Greater than 95.0% by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
SF20 plays a role in proliferation of lymphoid cells and is considered an interleukin. SF20 was initially identified as a product of bone marrow-derived stromal cells.
-
Synonyms
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid 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.
- View Data Sheet
Name :
KRT8 Human, GSTDescription:
Cytokeratin 8 Human Recombinant, GST Tag
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Product # :
PRO-298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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Description
Cytokeratin 8 Human Recombinant full length protein expressed in E.coli, shows a 78 kDa SDS-PAGE.The Cytokeratin 8 is fused to GST-Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cytokeratin-8 in 50mM Tris-HCl pH-7.5, 10mM L-glutathione (reduced).
Citations
More Info
-
Introduction
Cytokeratin 8 belongs to the type B (basic) subfamily of high molecular weight keratins and exists in combination with keratin 18. Cytokeratin 8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin polypeptides 8 and 18.
-
Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent 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.
- View Data Sheet
Name :
SDF2 HumanDescription:
Stromal Cell-Derived Factor 2 Human Recombinant
Stromal cell-derived factor 2, SDF-2.
Product # :
CHM-028Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SDF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (19-211 a.a) and having a molecular mass of 23.7kDa. SDF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDF2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2is a protein-coding gene whose alternative splicing results in coding and non-coding variants.
-
Synonyms
Stromal cell-derived factor 2, SDF-2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.
-
Background
What is the molecular weight/Mw of SDF2 HUMAN Protein?
SDF2 HUMAN Protein has a total Mw of 23.7kDa.
What is the source or expression system of SDF2 HUMAN Protein?
Escherichia Coli.
What is the Purity of SDF2 HUMAN Protein?
SDF2 HUMAN Protein is > 85% pure as determined by SDS-PAGE.
What is the Biological Activity of SDF2 HUMAN Protein?
The biological functionality of SDF2 HUMAN Protein will be determined in the future.
What is the amino acid sequence of SDF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.
What applications can SDF2 HUMAN Protein be used in?
SDF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for SDF2 HUMAN Protein?
The endotoxin level is minimal, SDF2 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant SDF2 HUMAN 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 SDF2 HUMAN?
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 :
DYNLL2 HumanDescription:
Dynein Light Chain LC8 Type-2 Human Recombinant
Dynein light chain LC8-type 2, DNCL1B, Dlc2, MGC17810, RSPH22, 8kDa dynein light chain b, DLC8b, dynein light chain 2 cytoplasmic, radial spoke 22 homolog.
Product # :
PRO-235Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DYNLL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.5kDa.DYNLL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DYNLL2 protein solution (1 mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Dyneins are multi-subunit, high molecular weight ATPases which cooperate with microtubules to create energy by altering the chemical energy of ATP into the mechanical energy of movement. DYNLL2 is a large protein complex made up of six different subunits and is in charge of a large number of intracellular movements to the minus ends of microtubules. DYNLL2 is an extremely conserved eukaryotic hub protein with dozens of binding partners and numerous roles other than being a subunit of dynein and myosin Va motor proteins.
-
Synonyms
Dynein light chain LC8-type 2, DNCL1B, Dlc2, MGC17810, RSPH22, 8kDa dynein light chain b, DLC8b, dynein light chain 2 cytoplasmic, radial spoke 22 homolog.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
DYNLL2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
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 :
CCL6 MouseDescription:
C-10 Mouse Recombinant (CCL6)
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
Product # :
CHM-307Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- biological activity
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Description
C-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.7kDa.The CCL6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCL6 Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.
Citations
More Info
-
Introduction
Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1. -
Synonyms
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized C10 protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL6 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized C10 protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.
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Background
What is the molecular weight/Mw of CCL6 MOUSE Protein?
CCL6 MOUSE Protein has a total Mw of 10.7kDa.
What is the source or expression system of CCL6 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL6 MOUSE Protein?
CCL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL6 MOUSE Protein?
The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.
What is the amino acid sequence of CCL6 MOUSE Protein?
GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.
What applications can CCL6 MOUSE Protein be used in?
CCL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL6 MOUSE Protein?
The endotoxin level is minimal, CCL6 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL6 MOUSE 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 CCL6 MOUSE?
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 :
RAB8 HumanDescription:
RAB8, Member RAS Oncogene Family Human Recombinant
Ras-related protein Rab-8B, RAB8B.
Product # :
PRO-1528Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RAB8 Human Recombinant produced in E. coli is a single polypeptide chain containing 227 amino acids (1-204) and having a molecular mass of 25.7kDa. RAB8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAB8 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
-
Introduction
RAB8, Member RAS Oncogene Family (RAB8B), is a low molecular mass monomeric GTPases which localize on the cytoplasmic surfaces of distinct membrane-bound organelles. RAB8 takes part in polarized vesicular trafficking and neurotransmitter release and also in cell junction dynamics in Sertoli cells. RAB proteins function in intracellular vesicle transport by aiding in the docking or fusion of vesicles with their target membranes.
-
Synonyms
Ras-related protein Rab-8B, RAB8B.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKTYDY LFKLLLIGDS GVGKTCLLFR FSEDAFNTTF ISTIGIDFKI RTIELDGKKI KLQIWDTAGQ ERFRTITTAY YRGAMGIMLV YDITNEKSFD NIKNWIRNIE EHASSDVERM ILGNKCDMND KRQVSKERGE KLAIDYGIKF LETSAKSSAN VEEAFFTLAR DIMTKLNRKM NDSNSAGAGG PVKITENRSK KTSFFRC.
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 :
RELM g Mouse, HisDescription:
RELM-Gamma Mouse Recombinant, His Tag
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-455Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
-
Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
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.The lyophilized protein remains stable until the expiry date when stored at -20°C.
-
Solubility
It is recommended to 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 10µg/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.
-
Amino Acid Sequence
MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.
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 :
DCN HumanDescription:
Decorin Human Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
Product # :
PRO-1583Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
-
Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.
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 :
IFNA14 HumanDescription:
Interferon-alpha 14 Human Recombinant
Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.
Product # :
CYT-135Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- Citations
Description
IFNA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a.) and having a molecular mass of 22.4kDa.IFNA14 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNA14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
Interferon alpha-14 (IFNA14) is a member of the alpha/beta interferon family. IFNA14 is produced by macrophages (IFN-alpha have antiviral activities). The interferon stimulates the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
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Synonyms
Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.
-
Background
What is the molecular weight/Mw of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein has a total Mw of 22.4kDa.
What is the source or expression system of IFNA14 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNA14 HUMAN Protein?
The biological functionality of IFNA14 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFNA14 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.
What applications can IFNA14 HUMAN Protein be used in?
IFNA14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNA14 HUMAN Protein?
The endotoxin level is minimal, IFNA14 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 :
LECT2 HumanDescription:
Leukocyte Cell-Derived Chemotaxin 2 Human Recombinant
Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.
Product # :
PRO-2037Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- purity
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Description
LECT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gly19-Leu151) containing 143 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16kDa.
Source
Escherichia Coli.
Formulation
LECT2 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl & pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Leukocyte Cell-Derived Chemotaxin 2 (LECT2) functions as a chemotactic factor to neutrophils. LECT2 stimulates the proliferation of chondrocytes and osteoblasts. LECT2 is strongly expressed in the liver and weakly in the testis. LECT2 is a secreted, 16kDa protein which serves as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. LECT2 protein has a high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in the LECT2 gene is linked with rheumatoid arthritis.
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Synonyms
Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
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.
-
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. LECT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHASGPWANICAGK SSNEIRTCDR HGCGQYSAQR SQRPHQGVDI LCSAGSTVYA PFTGMIVGQE KPYQNKNAIN NGVRISGRGF CVKMFYIKPI KYKGPIKKGE KLGTLLPLQK VYPGIQSHVH IENCDSSDPT AYL.
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 :
APRIL MouseDescription:
APRIL Mouse Recombinant
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.
Product # :
CYT-803Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
APRIL Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa. The APRIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4, with 0.02 % Tween-20.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
Determined by a cell proliferation assay using activated T cells.Citations
More Info
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Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines. APRIL stimulates proliferation of tumor cell lines and intensifies tumorigenicity in nude mice.
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Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized APRIL although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APRIL 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 APRIL 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
AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.
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Background
What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 16.4kDa.
What is the source or expression system of APRIL Protein?
Escherichia Coli.
What is the Purity of APRIL Protein?
APRIL Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of APRIL Protein?
Determined by a cell proliferation assay using activated T cells.
What is the amino acid sequence of APRIL Protein?
AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.
What applications can APRIL Protein be used in?
APRIL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APRIL Protein?
The endotoxin level is minimal, APRIL 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 :
Y.Enterocolitica (O:8) YopMDescription:
Yersinia Enterocolitica (O:8) YopM Recombinant
Product # :
PRO-2272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Yersinia Enterocolitica (O:8) YopM produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 60,898 Dalton. Y.Enterocolitica (O:8) YopM is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica(O:8) YopM 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
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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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- and IgA-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 :
CCL19 HumanDescription:
Macrophage Inflammatory Protein-3 Beta Human Recombinant (CCL19)
Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.
Product # :
CHM-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-3 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.8kDa. The MIP-3b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized without any additives.
Purity
Greater than 98.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity of CCL19 is calculated by the ability to chemoattract Human T cells using a concentration of 7-40ng/ml corresponding to a Specific Activity of 25,000-143,000IU/mg.Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.
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Synonyms
Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-3b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL19 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 Macrophage Inflammatory Protein-3b 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
GTNDAEDCCL SVTQKPIPGY IVRNFHYLLI KDGCRVPAVV FTTLRGRQLC APPDQPWVER IIQRLQRTSA KMKRRSS.
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Background
What is the molecular weight/Mw of CCL19 HUMAN Protein?
CCL19 HUMAN Protein has a total Mw of 8.8kDa.
What is the source or expression system of CCL19 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL19 HUMAN Protein?
CCL19 HUMAN Protein is > 98% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL19 HUMAN Protein?
The Activity of CCL19 is calculated by the ability to chemoattract Human T cells using a concentration of 7-40ng/ml corresponding to a Specific Activity of 25,000-143,000IU/mg.
What is the amino acid sequence of CCL19 HUMAN Protein?
GTNDAEDCCL SVTQKPIPGY IVRNFHYLLI KDGCRVPAVV FTTLRGRQLC APPDQPWVER IIQRLQRTSA KMKRRSS.
What applications can CCL19 HUMAN Protein be used in?
CCL19 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL19 HUMAN Protein?
The endotoxin level is minimal, CCL19 HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant CCL19 HUMAN 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 CCL19 HUMAN?
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 :
IGF1 N15 HumanDescription:
Insulin Like Growth Factor-1 N15 Labeled Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Product # :
CYT-128Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
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Description
IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
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 cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.sds-page
Citations
More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 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
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
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Background
What is the molecular weight/Mw of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein has a total Mw of 7.74kDa.
What is the source or expression system of IGF1 N15 HUMAN Protein?
Escherichia Coli.
What is the Purity of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 N15 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
What is the amino acid sequence of IGF1 N15 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
What applications can IGF1 N15 HUMAN Protein be used in?
IGF1 N15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 N15 HUMAN Protein?
The endotoxin level is minimal, IGF1 N15 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 :
TNFSF14 MouseDescription:
LIGHT Mouse Recombinant
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.
Product # :
CYT-826Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.
Source
Escherichia Coli.
Formulation
TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.
Purity
Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.Citations
More Info
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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
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Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.
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 :
Flt3 Ligand MouseDescription:
Flt3 Ligand Mouse Recombinant
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-340Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Flt3-Ligand Mouse Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 163 amino acids and having a molecular mass of 18.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FLT3L Mouse protein was lyophilized from sterile filtered solution containing 10mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.
Citations
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt-3 Ligand 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 Flt3l Mouse recombinant in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
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Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein has a total Mw of 18.6kDa.
What is the source or expression system of FLT3 LIGAND MOUSE Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND MOUSE Protein?
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.
What is the amino acid sequence of FLT3 LIGAND MOUSE Protein?
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
What applications can FLT3 LIGAND MOUSE Protein be used in?
FLT3 LIGAND MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND MOUSE Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE 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.