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Description:

Cytokine-Like 1 Human Recombinant

Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

Product # :

CYT-775

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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.

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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.
Synonyms
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
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 0.5 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.
Amino Acid Sequence
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
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.

Description:

Neurotrophin-1 Human Recombinant, His Tag

Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

Product # :

CYT-071

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Description

CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.
Synonyms
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
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 MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
Background
Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation
Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death1.
CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation2.
Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation3.
In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 24.6kDa.

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

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

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

What is the amino acid sequence of CLCF Protein?
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

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

What is the endotoxin level for CLCF Protein?
The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu

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

Description:

Platelet Endothelial Cell Adhesion Molecule 1 MouseRecombinant

Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.

Product # :

CYT-1211

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Description

PECAM1 Mouse Recombinant produced in HEK293 is a single, non-glycosylated polypeptide chain containing 579 amino acids (18-590 a.a.) and having a molecular mass of 65.3 kDa. PECAM1 Mouse is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PECAM1 Mouse protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.
Synonyms
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.
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
EENSFTINSI HMESLPSWEV MNGQQLTLEC LVDISTTSKS RSQHRVLFYK DDAMVYNVTS REHTESYVIP QARVFHSGKY KCTVMLNNKE KTTIEYEVKV HGVSKPKVTL DKKEVTEGGV VTVNCSLQEE KPPIFFKIEK LEVGTKFVKR RIDKTSNENF VLMEFPIEAQ DHVLVFRCQA GILSGFKLQE SEPIRSEYVT VQESFSTPKF EIKPPGMIIE GDQLHIRCIV QVTHLVQEFT EIIIQKDKAI VATSKQSSEA VYSVMAMVEY SGHYTCKVES NRISKASSIM VNITELFPKP KLEFSSSRLD QGELLDLSCS VSGTPVANFT IQKEETVLSQ YQNFSKIAEE SDSGEYSCTA GIGKVVKRSG LVPIQVCEML SKPSIFHDAK SEIIKGHAIG ISCQSENGTA PITYHLMKAK SDFQTLEVTS NDPATFTDKP TRDMEYQCRA DNCHSHPAVF SEILRVRVIA PVDEVVISIL SSNEVQSGSE MVLRCSVKEG TSPITFQFYK EKEDRPFHQA VVNDTQAFWH NKQASKKQEG QYYCTASNRA SSMRTSPRSS TLAVRVFLAP WKK HHHHH

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

Description:

Interleukin-6 Signal Transducer Human Recombinant

Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta

Product # :

CYT-1156

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Description

IL6ST Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 605 amino acids (23-619 a.a) and having a molecular mass of 68.9kDa.IL6ST is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL6ST solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.
Synonyms
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
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
ELLDPCGYIS PESPVVQLHS NFTAVCVLKE KCMDYFHVNA NYIVWKTNHF TIPKEQYTII NRTASSVTFT DIASLNIQLT CNILTFGQLE QNVYGITIIS GLPPEKPKNL SCIVNEGKKM RCEWDRGRET HLETNFTLKS EWATHKFADC KAKRDTPTSC TVDYSTVYFV NIEVWVEAEN ALGKVTSDHI NFDPVYKVKP NPPHNLSVIN SEELSSILKL TWTNPSIKSV IILKYNIQYR TKDASTWSQI PPEDTASTRS SFTVQDLKPF TEYVFRIRCM KEDGKGYWSD WSEEASGITY EDRPSKAPSF WYKIDPSHTQ GYRTVQLVWK TLPPFEANGK ILDYEVTLTR WKSHLQNYTV NATKLTVNLT NDRYVATLTV RNLVGKSDAA VLTIPACDFQ ATHPVMDLKA FPKDNMLWVE WTTPRESVKK YILEWCVLSD KAPCITDWQQ EDGTVHRTYL RGNLAESKCY LITVTPVYAD GPGSPESIKA YLKQAPPSKG PTVRTKKVGK NEAVLEWDQL PVDVQNGFIR NYTIFYRTII GNETAVNVDS SHTEYTLSSL TSDTLYMVRM AAYTDEGGKD GPEFTFTTPK FAQGEIELEH HHHHH
Background
Significance of Human Recombinant Interleukin-6 Signal Transducer: Insights and Implications
Abstract:
The Interleukin-6 (IL-6) signal transducer holds a pivotal role in the complex IL-6 signaling pathway, orchestrating crucial cellular responses. This paper delves into the significance of Human Recombinant IL-6 Signal Transducer in unraveling IL-6-mediated cellular communication and highlights its potential applications in research and therapeutic development. The review sheds light on the methodology of producing this transducer and its relevance in advancing our understanding of cytokine signaling.
Introduction:
IL-6, a pleiotropic cytokine, is known to exert its diverse effects through a complex signaling cascade, wherein the signal transducer plays a crucial role. The availability of Human Recombinant IL-6 Signal Transducer enables the investigation of its role in health and disease. This transducer is vital for transmitting IL-6 signals, influencing processes like immune response, inflammation, and cell differentiation.
IL-6 Signal Transduction Pathway:
The IL-6 signal transduction pathway involves binding of IL-6 to its receptor, leading to the recruitment of the signal transducer and subsequent activation of downstream signaling molecules such as JAK/STAT pathway. This orchestrated response modulates gene expression, thereby impacting cellular behavior.
Methods of Production:
Human Recombinant IL-6 Signal Transducer is produced by expressing the corresponding gene in a suitable expression system, often utilizing bacterial or mammalian cells. Proper post-translational modifications are necessary to ensure its biological activity and appropriate functioning within the signaling cascade.
Applications in Research:
Human Recombinant IL-6 Signal Transducer serves as a fundamental tool in elucidating IL-6-mediated signaling mechanisms. Its availability facilitates the exploration of how aberrant signaling contributes to diseases such as autoimmune disorders, inflammatory conditions, and certain cancers. The transducer's interaction with other signaling pathways is also of interest for comprehensive pathway analysis.
Therapeutic Implications:
Understanding the IL-6 signal transduction pathway has led to the development of targeted therapies for IL-6-related diseases. Modulation of this pathway presents potential opportunities for novel therapeutic interventions, thereby offering a new dimension in precision medicine.
Challenges and Future Directions:
While the availability of Human Recombinant IL-6 Signal Transducer has significantly advanced our knowledge, challenges remain in deciphering the intricate nuances of IL-6 signaling. Developing strategies to selectively intervene in this pathway without disturbing physiological homeostasis presents an ongoing challenge.
Conclusion:
The Human Recombinant IL-6 Signal Transducer serves as a cornerstone in unraveling the complexities of IL-6 signaling, shedding light on its roles in health and disease. Its applications span from fundamental research to therapeutic development, showcasing its potential to shape the future of precision medicine.
What is the molecular weight/Mw of IL6ST HUMAN Protein?
IL6ST HUMAN Protein has a total Mw of 68.9kDa.

What is the source or expression system of IL6ST HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL6ST HUMAN Protein?
IL6ST HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6ST HUMAN Protein?
The biological functionality of IL6ST HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL6ST HUMAN Protein?
ELLDPCGYIS PESPVVQLHS NFTAVCVLKE KCMDYFHVNA NYIVWKTNHF TIPKEQYTII NRTASSVTFT DIASLNIQLT CNILTFGQLE QNVYGITIIS GLPPEKPKNL SCIVNEGKKM RCEWDRGRET HLETNFTLKS EWATHKFADC KAKRDTPTSC TVDYSTVYFV NIEVWVEAEN ALGKVTSDHI NFDPVYKVKP NPPHNLSVIN SEELSSILKL TWTNPSIKSV IILKYNIQYR TKDASTWSQI PPEDTASTRS SFTVQDLKPF TEYVFRIRCM KEDGKGYWSD WSEEASGITY EDRPSKAPSF WYKIDPSHTQ GYRTVQLVWK TLPPFEANGK ILDYEVTLTR WKSHLQNYTV NATKLTVNLT NDRYVATLTV RNLVGKSDAA VLTIPACDFQ ATHPVMDLKA FPKDNMLWVE WTTPRESVKK YILEWCVLSD KAPCITDWQQ EDGTVHRTYL RGNLAESKCY LITVTPVYAD GPGSPESIKA YLKQAPPSKG PTVRTKKVGK NEAVLEWDQL PVDVQNGFIR NYTIFYRTII GNETAVNVDS SHTEYTLSSL TSDTLYMVRM AAYTDEGGKD GPEFTFTTPK FAQGEIELEH HHHHH.

What applications can IL6ST HUMAN Protein be used in?
IL6ST HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6ST HUMAN Protein?
The endotoxin level is minimal, IL6ST HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6ST 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 IL6ST 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.

Description:

Endothelial-Monocyte Activating Polypeptide II Human Recombinant

AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

Product # :

CYT-607

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Description

EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

Purity

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

Biological Activity

Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized EMAP-II in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.

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

What is the Purity of EMAP II HUMAN Protein?
EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

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

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

Description:

Interleukin-19 Human Recombinant

Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.

Product # :

CYT-363

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Shipped at Room temp

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Description

Interleukin-19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17913 Dalton. The IL-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM sodium citrate pH-5.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by it's ability to activate STAT following receptor-ligand interaction.

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Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. It can bind the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.
Synonyms
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL19 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 Interleukin -19 in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml or less.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Cys.

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

Description:

Interleukin-16 Human Recombinant, (121 a.a.)

IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

Product # :

CYT-142

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids and having a molecular mass of 12.4 kDa. The IL-16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-16 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

Fully biologically active when compared to standard. Determined by its ability to chemoattract human CD4+ T-Lymphocytes using a concentration range of 50.0-100.0 ng/ml.

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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL16 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 Interleukin-16 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAASASAASD VSVESTAEAT VCTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETVQPG DEILQLGGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QSKETTAAGD S

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

Description:

Interleukin 17F Human Recombinant

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-587

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Citations

Description

Interleukin-17F Human Recombinant produced in E.Coli is a homodimeric, cysteine linked, non-glycosylated polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 30.1 kDa.The IL-17F Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium citrate buffer pH-3.

Purity

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

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin Human IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-17F 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 Interleukin Human IL17F in sterile water not more than 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ.

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

Description:

Interleukin-17F Mouse Recombinant

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-642

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
More Info
Citations

Description

IL17F Mouse Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 266 amino acids and having a molecular mass of 29.8 kDa. The Mouse IL-17F is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17F was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

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

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Murine IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17F 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 Mouse IL17F in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSP
WDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRR
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAA.

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

Description:

Interleukin-10 Rat Recombinant

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-465

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

IL-10 Recombinant Rat produced in E.coli is a single, glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 18.6 kDa. The Interleukin-10 Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized containing 20mM Tris-HCl pH-8.0 and 100mM NaCl.

Purity

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

Biological Activity

The ED50 as determined by the dose dependent inhibition of MC/9 proliferation is less than 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

More Info

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.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-10 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin10 Rat recombinant 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 IL-10 Rat Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKGHSIRGDN NCTHFPVSQT HMLRELRAAF SQVKTFFQKK DQLDNILLTD SLLQDFKGYL GCQALSEMIK FYLVEVMPQA ENHGPEIKEH LNSLGEKLKT LWIQLRRCHR FLPCENKSKA VEQVKNDFNK LQDKGVYKAM NEFDIFINCI EAYVTLKMKN.
Background
What is the molecular weight/Mw of IL10 RAT Protein?
IL10 RAT Protein has a total Mw of 18.6kDa.

What is the source or expression system of IL10 RAT Protein?
Escherichia Coli.

What is the Purity of IL10 RAT Protein?
IL10 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 RAT Protein?
The ED50 as determined by the dose dependent inhibition of MC/9 proliferation is less than 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of IL10 RAT Protein?
SKGHSIRGDN NCTHFPVSQT HMLRELRAAF SQVKTFFQKK DQLDNILLTD SLLQDFKGYL GCQALSEMIK FYLVEVMPQA ENHGPEIKEH LNSLGEKLKT LWIQLRRCHR FLPCENKSKA VEQVKNDFNK LQDKGVYKAM NEFDIFINCI EAYVTLKMKN.

What applications can IL10 RAT Protein be used in?
IL10 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 RAT Protein?
The endotoxin level is minimal, IL10 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 RAT 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 IL10 RAT?
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.

Description:

Interleukin-17F Rat Recombinant

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-643

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Citations

Description

IL17F Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 270 amino acids and having a molecular mass of 30 kDa. The Rat IL-17F is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17F Rat was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

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

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL17F 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 Rat IL17F in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARRNPKVGL SALQKAGNCP PLEDNSVRVD IRIFNQNQGI SVPRDFQNRS SSPWDYNITR DPDRFPSEIA EAQCRHSGCI NAQGQEDGSM NSVPIQQEIL VLRREPQGCS NSFRLEKMLI KVGCTCVTPI VHHAA.

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

Description:

Interleukin-10 Human Recombinant, His

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-486

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.

Purity

Greater than 95.0% by SDS-PAGE.

More Info

Introduction
Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN, HIS Protein?
IL10 HUMAN, HIS Protein has a total Mw of 20.94kDa.

What is the source or expression system of IL10 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL10 HUMAN, HIS Protein?
IL10 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN, HIS Protein?
The biological functionality of IL10 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL10 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

What applications can IL10 HUMAN, HIS Protein be used in?
IL10 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN, HIS Protein?
The endotoxin level is minimal, IL10 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL10 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin 28B Human Recombinant

Lambda 3, IL28B, Interleukin 28B (IFN, Lambda 3), Cytokine Zcyto22, Interleukin-28B, Interleukin-28C, IFN-Lambda-3, IL-28B, IL-28C, IL28C, Lambda 4, Interleukin 28B, Interleukin 28C, IFN-Lambda-4, ZCYTO22, IFNL3.

Product # :

CYT-893

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Citations

Description

IL 28B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (22-196 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 181 amino acids and having a molecular mass of 20.4kDa.IL 28B shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL 28B protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM EDTA and 0.1mM PMSF.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
IL-28B is a cytokine remotely related to type I IFNs and the IL-10 family. Interleukin-28B, interleukin 28A (IL28A), and interleukin 29 (IL29) are 3 closely related cytokine genes which form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by these 3 genes can be induced by viral infection. All 3 cytokines interact with a heterodimeric class II cytokine receptor which consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha (IL28RA).
Synonyms
Lambda 3, IL28B, Interleukin 28B (IFN, Lambda 3), Cytokine Zcyto22, Interleukin-28B, Interleukin-28C, IFN-Lambda-3, IL-28B, IL-28C, IL28C, Lambda 4, Interleukin 28B, Interleukin 28C, IFN-Lambda-4, ZCYTO22, IFNL3.
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
VPVARLRGAL PDARGCHIAQ FKSLSPQELQ AFKRAKDALE ESLLLKDCKC RSRLFPRTWD LRQLQVRERP VALEAELALT LKVLEATADT DPALGDVLDQ PLHTLHHILS QLRACIQPQP TAGPRTRGRL HHWLHRLQEA PKKESPGCLE ASVTFNLFRL LTRDLNCVAS GDLCVHHHHHH.

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

Description:

Interleukin-10 Mouse Recombinant

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-497

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

IL-10 Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 18.7kDa.
The Interleukin-10 Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-10 Mouse lyophilized from a 0.2μm filtered solution in PBS, 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 a cell proliferation assay using murine MC/9-2 cells is less than 1ng/ml, corresponding to a specific activity of > 1.0 ×106 IU/mg.

More Info

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.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-10 Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin10 Mouse recombinant 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 IL-10 Mouse Recombinant in sterile 10mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SRGQYSREDN NCTHFPVGQS HMLLELRTAF SQVKTFFQTK DQLDNILLTD SLMQDFKGYL
GCQALSEMIQ FYLVEVMPQA EKHGPEIKEH LNSLGEKLKT LRMRLRRCHR FLPCENKSKA
VEQVKSDFNK LQDQGVYKAM NEFDIFINCI EAYMMIKMKS.
Background
What is the molecular weight/Mw of IL10 MOUSE Protein?
IL10 MOUSE Protein has a total Mw of 18.7kDa.

What is the source or expression system of IL10 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL10 MOUSE Protein?
IL10 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 MOUSE Protein?
The ED50 as determined by a cell proliferation assay using murine MC/9-2 cells is less than 1ng/ml, corresponding to a specific activity of > 1.0 ×106 IU/mg.

What is the amino acid sequence of IL10 MOUSE Protein?
SRGQYSREDN NCTHFPVGQS HMLLELRTAF SQVKTFFQTK DQLDNILLTD SLMQDFKGYL
GCQALSEMIQ FYLVEVMPQA EKHGPEIKEH LNSLGEKLKT LRMRLRRCHR FLPCENKSKA
VEQVKSDFNK LQDQGVYKAM NEFDIFINCI EAYMMIKMKS.

What applications can IL10 MOUSE Protein be used in?
IL10 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 MOUSE Protein?
The endotoxin level is minimal, IL10 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 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 IL10 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.

Description:

Interleukin 10 Human Recombinant, Sf9, Active

Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.

Product # :

CYT-1147

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
biological activity
More Info
sds-page
Citations

Description

IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

sds-page

More Info

Introduction
Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.
Synonyms
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
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
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.
Background
What is the molecular weight/Mw of IL10 HUMAN, SF9 Protein?
IL10 HUMAN, SF9 Protein has a total Mw of 19.4kDa.

What is the source or expression system of IL10 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL10 HUMAN, SF9 Protein?
IL10 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN, SF9 Protein?
Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

What is the amino acid sequence of IL10 HUMAN, SF9 Protein?
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.

What applications can IL10 HUMAN, SF9 Protein be used in?
IL10 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL10 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 HUMAN, SF9 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 IL10 HUMAN, SF9?
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.

Description:

Interleukin 17F Human Recombinant, sf9

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-1017

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL17F produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (31-163 a.a.) and having a molecular mass of 16kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa). IL17F is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17F protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
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
ADPRKIPKVG HTFFQKPESC PPVPGGSMKL DIGIINENQR VSMSRNIESR STSPWNYTVT WDPNRYPSEV VQAQCRNLGC INAQGKEDIS MNSVPIQQET LVVRRKHQGC SVSFQLEKVL VTVGCTCVTP VIHHVQHHHH HH.

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

Description:

Interleukin-28A Human Recombinant, His Tag

Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

Product # :

CYT-813

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 28A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
IL-28A is distantly related to type I interferons and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
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 MGSVPVARLH GALPDARGCH IAQFKSLSPQ ELQAFKRAKD ALEESLLLKD CRCHSRLFPR TWDLRQLQVR ERPMALEAEL ALTLKVLEAT ADTDPALVDV LDQPLHTLHH ILSQFRACIQ PQPTAGPRTR GRLHHWLYRL QEAPKKESPG CLEASVTFNL FRLLTRDLNC VASGDLCV .

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

Description:

Flt3 Ligand Human Recombinant

Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.

Product # :

CYT-331

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
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biological activity
More Info
sds-page
Citations

Description

Flt3-Ligand Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

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

Biological Activity

The ED₅₀ as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×10⁶ IU/mg.

sds-page

More Info

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.
Synonyms
Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-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.
Solubility
It is recommended to reconstitute the lyophilized Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.
Background

What is the molecular weight/Mw of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein has a total Mw of 17.6kDa.

What is the source or expression system of FLT3 LIGAND HUMAN Protein?
Escherichia Coli.

What is the Purity of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND HUMAN Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.

What is the amino acid sequence of FLT3 LIGAND HUMAN Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.

What applications can FLT3 LIGAND HUMAN Protein be used in?
FLT3 LIGAND HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND HUMAN Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-10 Human Recombinant

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-500

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

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source
formulation
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biological activity
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Description

Interleukin-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.The IL-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, 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 co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×10⁵ IU/mg.

More Info

Introduction
Recombinant 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.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL10 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 Interleukin-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN Protein?
IL10 HUMAN Protein has a total Mw of 18.6kDa.

What is the source or expression system of IL10 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL10 HUMAN Protein?
IL10 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN Protein?
The ED50 as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×105 IU/mg.

What is the amino acid sequence of IL10 HUMAN Protein?
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

What applications can IL10 HUMAN Protein be used in?
IL10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN Protein?
The endotoxin level is minimal, IL10 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 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 IL10 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.

Description:

Interleukin-17F Human Recombinant, His Tag

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-762

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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purity
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Description

IL 17F His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (31-163) and having a molecular mass of 17.6kDa.IL 17F His is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL 17F His 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

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
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 MGSHMRKIPK VGHTFFQKPE SCPPVPGGSM KLDIGIINEN QRVSMSRNIE SRSTSPWNYT VTWDPNRYPS EVVQAQCRNL GCINAQGKED ISMNSVPIQQ ETLVVRRKHQ GCSVSFQLEK VLVTVGCTCV TPVIHHVQ

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

Description:

Interleukin-20 Mouse Recombinant

IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.

Product # :

CYT-379

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-20 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a total molecular mass of 17,584 Dalton. The IL-20 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing no additives.

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 measuring the dose dependent activation of STAT3 in human epidermal keratinocytes (HEK2a cells). Significant STAT3 activation is observed with >100ng/mL of Interleukin-20 recombinant mouse, corresponding to a specific activity of 10,000 units/mg of Interleukin-20 recombinant mouse.

More Info

Introduction
IL20 is a cytokine structurally related to interleukin 10 (IL10). IL20 cytokine has been shown to transduce its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. A specific receptor for this cytokine is found to be expressed in skin and upregulated dramatically in psoriatic skin, suggesting a role for this protein in epidermal function and psoriasis.
Synonyms
IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL20 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 Interleukin-20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Lys-Thr-Leu.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.552 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-20 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.

Description:

Interleukin-17E Mouse Recombinant

IL-25, IL-17E, IL17E, IL25, Interleukin-25.

Product # :

CYT-641

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Recombinant mouse IL-17E is a non-glycosylated, disulfide-linked homodimer, containing 2x145 amino acid chains, with a total molecular weight of 35.5 kDa. The Mouse IL-17E is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17E was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the dose-dependent production of IL-8 by human PBMCs and is 322-488ng/ml.

More Info

Introduction
IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.
Synonyms
IL-25, IL-17E, IL17E, IL25, Interleukin-25.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Murine IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17E 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 Mouse IL17E in sterile 10mM HCl at a concentration not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVS
PPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRD
LNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPL
YHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACV
CVRPRVMA.

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

Description:

Interleukin-9 Human Recombinant, Sf9

Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.

Product # :

CYT-866

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL-9 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IL-9 is a factor which is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
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
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein has a total Mw of 23kDa.

What is the source or expression system of IL9 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 Protein?
The biological functionality of IL9 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL9 HUMAN, SF9 Protein?
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.

What applications can IL9 HUMAN, SF9 Protein be used in?
IL9 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 HUMAN, SF9 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 IL9 HUMAN, SF9?
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Description:

Interleukin-29 Human Recombinant

Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

Product # :

CYT-603

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Shipped at Room temp

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Description

IL-29 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution containing no additives.

Purity

Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues.
Synonyms
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 1 Recombinant 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 IL-29 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPVPTSKPTTT GKGCHIGRFK SLSPQELASF KKARDALEES LKLKNWSCSS PVFPGNWDLR LLQVRERPVA LEAELALTLK VLEAAAGPAL EDVLDQPLHTLHHILSQLQA CIQPQPTAGP RPRGRLHHWL HRLQEAPKKE SAGCLEASVT FNLFRLLTRD LKYVADGNLC LRTSTHPEST.

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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