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Name :
ANGPTL4 HumanDescription:
Angiopoietin-like Protein 4 Human Recombinant
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Product # :
CYT-249Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
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Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 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
Add 0.1M Acetate buffer pH4 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.
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Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
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Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:
Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.Introduction:
Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.Mechanisms of ANGPTL4 Action:
ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.Role of ANGPTL4 in Metabolic Regulation:
ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.Therapeutic Potential of ANGPTL4 Human Recombinant Protein:
The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.Conclusion:
ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.
What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.
What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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 :
ARF1 HumanDescription:
ADP-Ribosylation Factor 1 Human Recombinant
ARF-1, ADP-ribosylation factor 1.
Product # :
PRO-867Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.
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Synonyms
ARF-1, ADP-ribosylation factor 1.
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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 MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.
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 :
KLK10 HumanDescription:
Kallikrein-10 Human Recombinant
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
Product # :
ENZ-795Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (34-276) and having a molecular mass of 29.1kDa.KLK10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.
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Synonyms
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
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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 MGSALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN.
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 :
SARS Envelope, HisDescription:
SARS-Associated Coronavirus Envelope Recombinant, His Tag
Product # :
SARS-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.coli derived recombinant protein contains the Envelope protein 1-76 amino acids immunodominant regions fused to 6xHis tag at C-terminal.
Source
Escherichia Coli.
Formulation
SARS Envelope protein solution is supplied in PBS.
Purity
Protein is >90% pure as determined SDS-PAGE.
More Info
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Introduction
SARS Associated Coronavirus Envelope is a small membrane protein that takes major part in the life cycle of the virus. This protein is needed for the assembly, budding, creation of the envelope and pathogenesis. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to assure viral entry thetarget cells. Accordingly, S-protein has a major part in virus infection cycle and is the mainly target of neutralizing antibodies.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Specificity
Immunoreactive with sera of SARS-infected individuals.
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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 :
ANGPTL4 Human, HEKDescription:
Angiopoietin-like Protein 4 Human Recombinant, HEK
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Product # :
CYT-698Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ANGPTL4 Human Recombinant is manufactured with C-terminal fusion of 11 amino acid FLAG Tag. The ANGPTL4 Flag -Tagged Fusion Protein is a 44.2kDa protein containing 392 amino acid residues of the Angiopoietin-like Protein 4 and 11 additional amino acid residues - Flag Tag (underlined).
Source
HEK293.
Formulation
Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
The fasting-induced adipose factor (FIAF, ANGPTL4, PGAR, HFARP) was identified as an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. At the protein level, in human and mouse blood plasma, FIAF was found to be present both as a native protein and in a truncated form. Differentiation of mouse 3T3-L1 adipocytes was associated with the production of truncated FIAF, whereas in human white adipose tissue and SGBS adipocytes, only the native FIAF could be detected. Interestingly, the truncated FIAF was produced by human liver.
Experimental data suggest that FIAF is mainly presented in human blood plasma in a truncated form (FIAF-S2), whose level is increased by fenofibrate treatment. Levels of both truncated and native FIAF showed marked inter individual variation but were not associated with body mass index and were not influenced by prolonged semistarvation. -
Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Angiopoietin-like Protein 4 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
Add pyrogen free water to a working concentration 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
GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.
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Applications
Western blotting.
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Background
What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 44.2kDa.
What is the source or expression system of ANGPTL4 Protein?
HEK293.
What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL4 Protein?
GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.
What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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 :
IFNG FelineDescription:
Interferon-gamma Feline Recombinant
Interferon gamma, IFN-gamma, IFNG.
Product # :
CYT-998Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- SDS-PAGE
Description
IFNG Feline Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (24-167 a.a) and having a molecular mass of 19.3kDa.IFNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (1mg/ml) containing PBS buffer (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Interferon gamma, IFN-gamma, IFNG.
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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 MGSQAMFFKE IEELKGYFNA SNPDVADGGS LFVDILKNWK EESDKTIIQS QIVSFYLKMF ENLKDDDQRI QRSMDTIKED MLDKLLNTSS SKRDDFLKLI QIPVNDLQVQ RKAINELFKV MNDLSPRSNL RKRKRSQNLF RGRRASK.
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Background
What is the molecular weight/Mw of IFNG FELINE Protein?
IFNG FELINE Protein has a total Mw of 19.3kDa.
What is the source or expression system of IFNG FELINE Protein?
Escherichia Coli.
What is the Purity of IFNG FELINE Protein?
IFNG FELINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG FELINE Protein?
The biological functionality of IFNG FELINE Protein will be determined in the future.
What is the amino acid sequence of IFNG FELINE Protein?
MGSSHHHHHH SSGLVPRGSH MGSQAMFFKE IEELKGYFNA SNPDVADGGS LFVDILKNWK EESDKTIIQS QIVSFYLKMF ENLKDDDQRI QRSMDTIKED MLDKLLNTSS SKRDDFLKLI QIPVNDLQVQ RKAINELFKV MNDLSPRSNL RKRKRSQNLF RGRRASK.
What applications can IFNG FELINE Protein be used in?
IFNG FELINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG FELINE Protein?
The endotoxin level is minimal, IFNG FELINE 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 :
TNFSF7 HumanDescription:
CD70 Human Recombinant
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
Product # :
CYT-880Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFSF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (39-193 a.a) and having a molecular mass of 19.5kDa. TNFSF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFSF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
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Synonyms
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
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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 MGSQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRP.
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 :
IL 3 MouseDescription:
Interleukin-3 Mouse Recombinant
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-371Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.More Info
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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils. -
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 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 Interleukin-3 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 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 IL3 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 :
IL 4 Rhesus MacaqueDescription:
Interleukin-4 Rhesus Macaque Recombinant
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
Product # :
CYT-172Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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- biological activity
- More Info
Description
IL-4 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.The IL4 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
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 the dose-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.More Info
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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleikin-4 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
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.
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 :
IL1F10 HumanDescription:
Interleukin 1 Family, Member 10 Human Recombinant
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
Product # :
CYT-012Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL1F10 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 152 amino acids and having a molecular mass of 17kDa.The IL1F10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL1F10 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
As measured by its binding ability in a functional ELISA, immobilized IL1F10 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.
More Info
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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
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Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL1F10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F10 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 quick spin followed by reconstitution of IL1F10 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Cys-Ser-Leu-Pro.
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 :
IL31 MouseDescription:
Interleukin-31 Mouse Recombinant
Interleukin 31, IL31, IL-31.
Product # :
CYT-604Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL31 mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.7 kDa.
Source
Escherichia Coli.
Formulation
The IL31 (1mg/ml) was lyophilized from 10mM sodium Phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune re -
Synonyms
Interleukin 31, IL31, IL-31.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL31 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 IL31 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
MTCSLSFGAP ISKEDLRTTI DLLKQESQDL YNNYSIKQAS GMSADESIQL PCFSLDREAL TNISVIIAHL EKVKVLSENT VDTSWVIRWL TNISCFNPLN LNISVPGNTD ESYDCKVFVL TVLKQFSNCM AELQAKDNTT C.
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 :
RNASE2 HumanDescription:
Ribonuclease 2 Human Recombinant
EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.
Product # :
ENZ-1175Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNASE2 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 143 amino acids (28-161 a.a.) and having a molecular mass of 16.5kDa.RNASE2 is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RNASE2 Human protein (1mg/ml) is formulated in 20% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RNASE2, also known as EDN, is best-known as one of the 4 major proteins found in the large specific granules of human eosinophilic leukocytes. This protein is also expressed constitutively in human liver tissue and its expression can be induced in macrophages by proinflammatory stimuli. RNASE2 is a non-secretory ribonuclease which belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. Diseases associated with EDN include Dermatitis, Atopic, 8 and Pulmonary Eosinophilia.
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Synonyms
EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.
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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
ADPKPPQFTW AQWFETQHIN MTSQQCTNAM QVINNYQRRC KNQNTFLLTT FANVVNVCGN PNMTCPSNKT RKNCHHSGSQ VPLIHCNLTT PSPQNISNCR YAQTPANMFY IVACDNRDQR RDPPQYPVVP VHLDRIIHHH HHH
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 :
PKLR AntibodyDescription:
Pyruvate Kinase, Liver and RBC, Mouse Anti Human
PK1, PKL, RPK, pyruvate kinase isozyme R/L, Red cell/liver pyruvate kinase, PKRL.
Product # :
ANT-060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.
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Synonyms
PK1, PKL, RPK, pyruvate kinase isozyme R/L, Red cell/liver pyruvate kinase, PKRL.
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Immunogen
Anti-human PKLR mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PKLR amino acids 47-574 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and kappa light chain.
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Clone
PPKLRAT.
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Applications
PKLR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Recommended dilution range for Western blot analysis is 1:500. -
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
PKLR 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 :
LYVE1 AntibodyDescription:
Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1, Mouse Anti Human
Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, LYVE-1, Cell surface retention sequence-binding protein 1, CRSBP-1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
Product # :
ANT-322Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.02% Sodium Azide and 10% Glycerol.
More Info
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Introduction
LYVE-1 has been identified as a major receptor for HA (extracellular matrix glycosaminoglycan hyaluronan) on the lymph vessel wall. The deduced amino acid sequence of LYVE-1 predicts a 322-residue type I integral membrane polypeptide 41% similar to the CD44 HA receptor with a 212-residue extracellular domain containing a single Link module the prototypic HA binding domain of the Link protein superfamily. Like CD44, the LYVE-1 molecule binds both soluble and immobilized HA. However, unlike CD44, the LYVE-1 molecule colocalizes with HA on the luminal face of the lymph vessel wall and is completely absent from blood vessels. Hence, LYVE-1 is the first lymph-specific HA receptor to be characterized and is a uniquely powerful marker for lymph vessels themselves.
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Synonyms
Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, LYVE-1, Cell surface retention sequence-binding protein 1, CRSBP-1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
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Immunogen
Anti-human LYVE1 mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LYVE1 amino acids 25-235 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
P4G1AT.
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Applications
LYVE1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:1,000.
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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
LYVE1 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 :
GH AntibodyDescription:
Growth Hormone, Mouse Anti Human
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
ANT-197Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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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 Growth Hormone.
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Ig Subclass
Mouse IgG1.
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Clone
NYRhGH.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation.
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Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 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 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
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Purification Method
Ion exchange.
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 :
C3b RatDescription:
Complement C3b Rat
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Product # :
PRO-2708Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Rat Complement C3b produced in Rat plasma having a molecular weight of 175kDa.
Source
Rat Plasma.
Formulation
C3b solution contains contains phosphate Buffered Saline, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C3b is derived from native C3 upon cleavage with the alternative pathway C3 convertase and release of C3a. C3b is essential to the function of all 3complement pathways. Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3b created during complement activation. Surface-bound C3b is needed in all 3 pathways for effective activation of C5 and formation of C5b-9 complexes which lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are identifyid by various receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. It results in an expansion of target-specific B-cell and T-cell populations.
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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
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Physical Appearance
Sterile filtered solution.
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Stability
C3b Rat 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.
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 :
CXCL8 Human, GSTDescription:
Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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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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Applications
Immunoassay.
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Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.
What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST 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 :
HIV-2 gp36, 17kDaDescription:
HIV-2 gp36 Recombinant
Product # :
HIV-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant HIV-2 gp36 produced in E.coli is a non-glycosylated polypeptide chain contains HIV2 subtype A gp 36 sequence and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
HIV-2 gp36 contains PBS, 25mM K2CO3 and 0.025% NaN3.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids. Immunodeficiency develops more slowly with HIV-2.
HIV-2 is less infectious in the early stages of the virus than with HIV-1.
The infectiousness of HIV-2 increases as the virus progresses.
Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.
HIV-1 gp41 helical regions can form more stable 6-helix bundles than HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition. -
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.
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Applications
ELISA, lateral flow assay.
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 :
CYTL1 HumanDescription:
Cytokine-Like 1 Human Recombinant
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
Product # :
CYT-775Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).
Source
Escherichia Coli.
Formulation
CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.
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Synonyms
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
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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. CYTL1 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
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
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Background
Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential
Abstract:
Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.Production and Characterization:
Recombinant CYTL1 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 bioactivity of the recombinant CYTL1.Role in Immune Regulation:
CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.Therapeutic Implications:
The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.Conclusion:
Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.What is the molecular weight/Mw of CYTL1 Protein?
CYTL1 Protein has a total Mw of 14.6kDa.
What is the source or expression system of CYTL1 Protein?
Escherichia Coli.
What is the Purity of CYTL1 Protein?
CYTL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CYTL1 Protein?
The biological functionality of CYTL1 Protein will be determined in the future.
What is the amino acid sequence of CYTL1 Protein?
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
What applications can CYTL1 Protein be used in?
CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CYTL1 Protein?
The endotoxin level is minimal, CYTL1 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 :
NTRK2 HumanDescription:
Neurotrophic Receptor Tyrosine Kinase 2 Human Recombinant
GP145-TrkB, trk-B, TRKB, NTRK2
Product # :
CYT-1159Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTRK2 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 407 amino acids (32-430a.a) and having a molecular mass of 45.2kDa.NTRK2 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NTRK2 solution (0. 5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Neurotrophic Receptor Tyrosine Kinase 2, also referred to NTRK2, is a tyrosine-protein kinase receptor which takes part in the development & the maturation of the central and the peripheral nervous systems through regulation of neuron survival, migration, proliferation, differentiation and synapse formation & plasticity. NTRK2 acts in learning and memory by regulating both short term synaptic function and long-term potentiation. The substrates that are known for the TRK family receptors are: SHC1, PI-3 kinase and PLC-gamma-1.
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Synonyms
GP145-TrkB, trk-B, TRKB, NTRK2
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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
CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREHL EHHHHHH
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 :
IL 31 HumanDescription:
Interleukin-31 Human Recombinant
Interleukin 31, IL31, IL-31.
Product # :
CYT-625Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.
Source
Escherichia Coli.
Formulation
The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.More Info
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Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis. -
Synonyms
Interleukin 31, IL31, IL-31.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 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 IL-31 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
SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.
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 :
IL 6 RatDescription:
Interleukin-6 Rat Recombinant
IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.
Product # :
CYT-388Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-6 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21732 Dalton. The IL6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 0.02% TFA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is less than 0.01 ng/ml as determined by dose-dependent stimulation of mouse 7TD1 cells.More Info
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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
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Synonyms
IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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 Interleukin-6 with 10mM HCl at a concentration of 0.1 mg/ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Phe-Pro-Thr-Ser.
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Background
Research Paper on Interleukin-6 Rat Recombinant
Abstract:
Exploring Interleukin-6 Rat Recombinant: This research paper provides an extensive description of Interleukin-6 (IL-6) Rat Recombinant, a vital cytokine in immunological studies. We delve into its molecular properties, significance in immune responses, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 Rat Recombinant in advancing our understanding of immune regulation.
Introduction:
Unraveling IL-6 Rat Recombinant: This paper introduces IL-6 Rat Recombinant, a valuable tool for investigating immune responses. As researchers, we are intrigued by its diverse functions and potential therapeutic implications.
An Extensive Description of IL-6 Rat Recombinant:
We present a comprehensive overview of IL-6 Rat Recombinant, focusing on its structural characteristics and involvement in immune signaling. This recombinant cytokine allows us to explore the complexities of IL-6 biology and its impact on immune system homeostasis.
Significance in Immune Responses:
Marvel at IL-6's pivotal role in orchestrating immune responses! As a crucial mediator between immune cells, IL-6 plays a critical role in regulating inflammation and immune cell activation. It also contributes to tissue repair and antibody production.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our comprehension of the interconnected cytokine network, contributing to a broader understanding of immune signaling.
Potential Applications in Immunological Research:
Explore the diverse applications of IL-6 Rat Recombinant in immunological research. From deciphering cellular responses to developing potential therapeutics, this recombinant cytokine serves as an indispensable tool for advancing our knowledge of the immune system. Researchers use it for in vitro studies, functional assays, and investigating disease pathogenesis.
Novel Insights and Therapeutic Implications:
Gain novel insights into the therapeutic implications of IL-6 Rat Recombinant. Understanding its role in disease pathogenesis may lead to the development of targeted therapies for various immune-related disorders. Clinical trials targeting IL-6 have shown promise in treating certain inflammatory conditions.
Conclusion:
Concluding our exploration of IL-6 Rat Recombinant, we recognize its significance in immunological research. The extensive description of this recombinant cytokine broadens our understanding of IL-6 biology and its potential applications in various fields. By utilizing this powerful tool, we strive to make significant advancements in immunology research for improved health outcomes.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.55 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 IL-6 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TECK HumanDescription:
Thymus Expressed Chemokine Human Recombinant (CCL25)
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-364Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK 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
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
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 :
IL5RA MouseDescription:
Interleukin-5 Receptor Alpha Mouse Recombinant
Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA, CD125.
Product # :
CYT-955Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
IL5RA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (18-339a.a.) and having a molecular mass of 37.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). IL5RA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL5RA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.
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Synonyms
Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA, CD125.
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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
DLLNHKKFLL LPPVNFTIKA TGLAQVLLHW DPNPDQEQRH VDLEYHVKIN APQEDEYDTR KTESKCVTPL HEGFAASVRT ILKSSHTTLA SSWVSAELKA PPGSPGTSVT NLTCTTHTVV SSHTHLRPYQ VSLRCTWLVG KDAPEDTQYF LYYRFGVLTE KCQEYSRDAL NRNTACWFPR TFINSKGFEQ LAVHINGSSK RAAIKPFDQL FSPLAIDQVN PPRNVTVEIE SNSLYIQWEK PLSAFPDHCF NYELKIYNTK NGHIQKEKLI ANKFISKIDD VSTYSIQVRA AVSSPCRMPG RWGEWSQPIY VGKERKSLVE WHLEHHHHHH.
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.