Search: 1000 results found for "Interferon"

Description:

Interleukin-7 Human Recombinant, Yeast

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-298

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Description

Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 10⁶units/mg.

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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 -7 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 Asp-Cys-Asp-Ile-Glu.
Background
What is the molecular weight/Mw of IL7 HUMAN, YEAST Protein?
IL7 HUMAN, YEAST Protein has a total Mw of 17.4kDa.

What is the source or expression system of IL7 HUMAN, YEAST Protein?
Saccharomyces cerevisiae.

What is the Purity of IL7 HUMAN, YEAST Protein?
IL7 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN, YEAST Protein?
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

What is the amino acid sequence of IL7 HUMAN, YEAST Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

What applications can IL7 HUMAN, YEAST Protein be used in?
IL7 HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7 HUMAN, YEAST Protein?
The endotoxin level is minimal, IL7 HUMAN, YEAST Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7 HUMAN, YEAST 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 IL7 HUMAN, YEAST?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 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-7 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-2 Receptor Beta Human Recombinant

Interleukin 2 receptor subunit beta, IL2RB, CD122, IL15RB, P70-75, IL-2R subunit beta.

Product # :

CYT-1086

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Shipped with Ice Packs

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Description

IL2RB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-240 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 220 amino acids and having a molecular mass of 25.5kDa.IL2RB shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RB protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin 2 receptor is a protein that involves immune responses that are mediated through T cells. The IL2 receptor exists in three ways in which it can bind to IL2. CD25 is the lowest affinity (a monomer of the alpha subunit), therefore, it is not part of the signal transduction process. The highest affinity has three heterotrimer subunits (alpha/beta/gamma), the intermediate affinity is found to have gamma/beta subunit heterodimer. Both forms are part of the receptor mediated endocytosis and mitogenic signals transduction from IL2.
Synonyms
Interleukin 2 receptor subunit beta, IL2RB, CD122, IL15RB, P70-75, IL-2R subunit 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
AVNGTSQFTC FYNSRANISC VWSQDGALQD TSCQVHAWPD RRRWNQTCEL LPVSQASWAC NLILGAPDSQ KLTTVDIVTL RVLCREGVRW RVMAIQDFKP FENLRLMAPI SLQVVHVETH RCNISWEISQ ASHYFERHLE FEARTLSPGH TWEEAPLLTL KQKQEWICLE TLTPDTQYEF QVRVKPLQGE FTTWSPWSQP LAFRTKPAAL GKDTHHHHHH.
Background
What is the molecular weight/Mw of CD122 HUMAN Protein?
CD122 HUMAN Protein has a total Mw of 25.5kDa.
What is the source or expression system of CD122 HUMAN Protein?
Sf9, Baculovirus cells.
What is the Purity of CD122 HUMAN Protein?
CD122 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD122 HUMAN Protein?
The biological functionality of CD122 HUMAN Protein will be determined in the future.

What is the amino acid sequence of CD122 HUMAN Protein?
AVNGTSQFTC FYNSRANISC VWSQDGALQD TSCQVHAWPD RRRWNQTCEL LPVSQASWAC NLILGAPDSQ KLTTVDIVTL RVLCREGVRW RVMAIQDFKP FENLRLMAPI SLQVVHVETH RCNISWEISQ ASHYFERHLE FEARTLSPGH TWEEAPLLTL KQKQEWICLE TLTPDTQYEF QVRVKPLQGE FTTWSPWSQP LAFRTKPAAL GKDTHHHHHH.

What applications can CD122 HUMAN Protein be used in?
CD122 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD122 HUMAN Protein?
The endotoxin level is minimal, CD122 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CD122 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 CD122 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-12 Human Recombinant, Sf9

23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-1111

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Shipped at Room temp

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Description

Interleukin 12 Human Recombinant is a glycosylated heterodimer containing 503 amino acids (306 amino acid rHuIL-12 p40 and the 197 amino acid rHuIL-12 p35 subunits) and having a molecular mass of 60kDa. IL12 is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

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Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is an essential part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
Synonyms
23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Interleukin 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
>IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
>IL-12B
IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.
Background
What is the molecular weight/Mw of IL12 HUMAN, SF9 Protein?
IL12 HUMAN, SF9 Protein has a total Mw of 60kDa.

What is the source or expression system of IL12 HUMAN, SF9 Protein?
Baculovirus.

What is the Purity of IL12 HUMAN, SF9 Protein?
IL12 HUMAN, SF9 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 HUMAN, SF9 Protein?
Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

What is the amino acid sequence of IL12 HUMAN, SF9 Protein?
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
>IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
>IL-12B
IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.

What applications can IL12 HUMAN, SF9 Protein be used in?
IL12 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL12 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 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 IL12 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-17 Rat Recombinant

CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, Interleukin-17A.

Product # :

CYT-542

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Description

Interleukin-17A Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain having a molecular mass of 30 kDa. The IL-17A Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 10mM NaCitrate, pH-3.0.

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 dose-dependent induction of IL-6 by mouse NIH 3T3 fibroblasts is 0.44-0.66ng/ml.

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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, Interleukin-17A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin Rat 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL17 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 Rat 17A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.

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-12 Mouse Recombinant

NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-144

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Quantity :

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Shipped at Room temp

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Description

Interleukin-12 Mouse Recombinant produced in HEK 293 cells is a glycosylated disulfide linked heterodimeric polypeptide containing 506 amino acids and having a molecular weight of 75 kDa comprised of disulfide-bonded 35 kDa (p35) and 40 kDa (p40) subunits.The IL-12 is purified by proprietary chromatographic techniques.

Source

HEK-293 Cells.

Formulation

The protein was lyophilized from 0.5xPBS, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

IL-12 Mouse has full biological activity when compared to standards. The ED₅₀ is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x10⁵ units/mg.

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 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 murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.
Background
What is the molecular weight/Mw of IL12 MOUSE Protein?
IL12 MOUSE Protein has a total Mw of 75kDa.

What is the source or expression system of IL12 MOUSE Protein?
HEK-293 Cells.

What is the Purity of IL12 MOUSE Protein?
IL12 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 MOUSE Protein?
IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

What is the amino acid sequence of IL12 MOUSE Protein?
p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.
p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

What applications can IL12 MOUSE Protein be used in?
IL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 MOUSE Protein?
The endotoxin level is minimal, IL12 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 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 IL12 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-17A/F Heterodimer Rat Recombinant

IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

Product # :

CYT-677

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Shipped at Room temp

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Description

IL-17A/F Rat Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide chain containing 1 monomeric subunit of each IL-17A & IL-17F. The dimer contains 269 amino acids and having a total molecular mass of 30.7 kDa. The IL-17A/F Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 98.0% as determined by HPLC and SDS-PAGE.

Biological Activity

The ED₅₀ as determined by its ability to induce of IL-6 production from NIH-3T3 cells, is 15.3-23 ng/ml.

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Introduction
Rat IL-17A/F is a glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Rat IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Rat IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat IL-17A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL-17A/F 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 IL-17A/F in sterile water not more than 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IL-17A: MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.
IL-17F: 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-8, Mouse Anti-Human

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

Product # :

ANT-111

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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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 phagocytosethe particle. Upon processing, they release chemokinesto 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 neutrophilsat the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-8.
Ig Subclass
Mouse IgG1.
Clone
NYR-HIL8.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Immunohistochemistry.
Cross reactivity
No cross reactivity with murine IL-8 was detected.
Note
This antibody was produced in BALB/c mice.
Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
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.
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.

Description:

Interleukin-1 beta Porcine Recombinant

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

CYT-400

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Description

Recombinant IL 1 beta Porcine produced in E.coli cells is a non-glycosylated, homodimeric protein containing 153 amino acid chain and having a molecular mass of 17.6kDa. The IL 1 beta is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL 1 beta was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4, containing 3 % trehalose.

Purity

Greater than 95.0% 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 D10S cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 10⁵ IU/mg.

More Info

Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL 1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1 beta 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 1 beta in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ANVQSMECKL QDKDHKSLVL AGPHMLKALH LLTGDLKREV VFCMSFVQGD DSNNKIPVTL GIKGKNLYLS CVMKDNTPTL QLEDIDPKRY PKRDMEKRFV FYKTEIKNRV EFESALYPNW YISTSQAEQK PVFLGNSKGR QDITDFTMEV LSP
Background
What is the molecular weight/Mw of IL1B PORCINE Protein?
IL1B PORCINE Protein has a total Mw of 17.6kDa.

What is the source or expression system of IL1B PORCINE Protein?
Escherichia Coli.

What is the Purity of IL1B PORCINE Protein?
IL1B PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B PORCINE Protein?
The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

What is the amino acid sequence of IL1B PORCINE Protein?
ANVQSMECKL QDKDHKSLVL AGPHMLKALH LLTGDLKREV VFCMSFVQGD DSNNKIPVTL GIKGKNLYLS CVMKDNTPTL QLEDIDPKRY PKRDMEKRFV FYKTEIKNRV EFESALYPNW YISTSQAEQK PVFLGNSKGR QDITDFTMEV LSP.

What applications can IL1B PORCINE Protein be used in?
IL1B PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B PORCINE Protein?
The endotoxin level is minimal, IL1B PORCINE 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-9 Human Recombinant

P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

Product # :

CYT-348

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

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Description

Interleukin-9 Human Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14,004 Dalton. The IL-9 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-9 protein 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 by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of human MO7e cells is less than 0.2 ng/ml, corresponding to a Specific Activity of >5.0×10⁶ IU/mg.

More Info

Introduction
Factor that 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
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQGCPTLAGI LDINFLINKM QEDPASKCHC SANVTSCLCL GIPSDNCTRP CFSERLSQMT NTTMQTRYPL IFSRVKKSVE VLKNNKCPYF SCEQPCNQTT AGNALTFLKS LLEIFQKEKM RGMRGKI.
Background
What is the molecular weight/Mw of IL9 HUMAN Protein?
IL9 HUMAN Protein has a total Mw of 14kDa.

What is the source or expression system of IL9 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL9 HUMAN Protein?
IL9 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of human MO7e cells is less than 0.2 ng/ml, corresponding to a Specific Activity of >5.0×106 IU/mg.

What is the amino acid sequence of IL9 HUMAN Protein?
MQGCPTLAGI LDINFLINKM QEDPASKCHC SANVTSCLCL GIPSDNCTRP CFSERLSQMT NTTMQTRYPL IFSRVKKSVE VLKNNKCPYF SCEQPCNQTT AGNALTFLKS LLEIFQKEKM RGMRGKI.

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

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

Who supplies recombinant IL9 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 IL9 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 17A Human Recombinant, Sf9

Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.

Product # :

CYT-895

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL17A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-155 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 138 amino acids and having a molecular mass of 15.9kDa.IL17A shows multiple bands between 13.5-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17A protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM EDTA and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 7 ng/ml. The activity is determined by the IL-6 ELISA in a using NIH/3T3 mouse embryonic fibroblast cells.

More Info

Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Synonyms
Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.
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
GITIPRNPGC PNSEDKNFPR TVMVNLNIHN RNTNTNPKRS SDYYNRSTSP WNLHRNEDPE RYPSVIWEAK CRHLGCINAD GNVDYHMNSV PIQQEILVLR REPPHCPNSF RLEKILVSVG CTCVTPIVHH VAHHHHHH

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

Description:

Interleukin-36 Gamma Human Recombinant

Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.

Product # :

CYT-160

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL36G Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 169 amino acids and having a molecular mass of 18.7kDa.The IL36G is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

Measured by its binding ability in a functional ELISA to bind recombinant human IL-1 Rrp2 Fc Chimera.

More Info

Introduction
IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and IL-1F10. ). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.
Synonyms
Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36g Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g 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 IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRGTPGDADG GGRAVYQSMC KPITGTINDL NQQVWTLQGQ NLVAVPRSDS VTPVTVAVIT CKYPEALEQG RGDPIYLGIQ NPEMCLYCEK VGEQPTLQLK EQKIMDLYGQ PEPVKPFLFY RAKTGRTSTL ESVAFPDWFI ASSKRDQPII LTSELGKSYN TAFELNIND

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 Human Recombinant

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

Product # :

CYT-583

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-17E Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2x145 amino acids (with an N-terminal Methionine for each chain total aa for each chain 146) and having a total predicted molecular mass of 33.7kDa. The IL-25 Human 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 SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent production of IL-8 by Human PBMCs is 26-40ng/ml, corresponding to a specific activity of 3.8x10⁴ units/mg.

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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, Interleukin-17E.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin Human IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-25 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 IL25 in sterile 10mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MYSHWPSCCP SKGQDTSEEL LRWSTVPVPP LEPARPNRHP ESCRASEDGP LNSRAISPWR YELDRDLNRL PQDLYHARCL CPHCVSLQTG SHMDPRGNSE LLYHNQTVFY RRPCHGEKGT HKGYCLERRL YRVSLACVCV RPRVMG.

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-4 Human Recombinant

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-211

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15kDa. The IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 98% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

More Info

Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-4 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-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Everything You Should Know About IL-4 Human Recombinant
Interleukin-4 (IL-4) is an important type-2 cytokine with multiple effects on numerous cells and tissues in the body. As such, it's crucial for the immune system's maintenance and function.
Recent advancements have led to the development of interleukin-4 (rhIL-4) human recombinant in laboratories. As a result, experts have started studying its potential uses and therapeutic applications.
If you're interested in learning more about IL-4 human recombinant, check out the information below!
How Does Interleukin-4 (IL-4) Work?
Interleukin-4 (IL-4) acts as a signaling molecule, specifically a protein. It communicates with various immune cells by binding to specific receptors on their surface.
This process triggers responses against common threats, such as allergens, contaminants, and infections.
IL-4 is produced by T helper 2 (Th2) cells (a type of white blood cells), mast cells, eosinophils, and basophils.
What Interleukin-4 (IL-4) Does
As mentioned, this type-2 cytokine has multiple effects on various cells and tissues, so it fulfills several functions. Below are the most important ones:
- Th2 cell differentiation: IL-4 promotes the differentiation of T cells, triggering the response of Th2 cells, which fight parasites and regulate allergic responses.
- B cell activation and antibody production: IL-4 stimulates B cells, helping them proliferate and produce antibodies, particularly immunoglobulin E (IgE), which is involved in allergic reactions.
- Inflammation reduction: IL-4 can promote inflammation to address threats, such as allergens or parasites, and suppress it when necessary, depending on the context.
- Tissue repair and remodeling: IL-4 is key for tissue repair and remodeling processes, such as wound healing and fibrosis.
What Is IL-4 Human Recombinant?
IL-4 human recombinant is a version produced in a laboratory using DNA technology. The cytokine is inserted into a host organism, commonly E. Coli bacteria, for mass production.
This method allows experts to obtain pure and contaminant-free rhIL-4 with uniform biological activity and in large quantities.
What Can IL-4 Human Recombinant Be Used For?
Since this cytokine plays a key role in different processes, it may have multiple therapeutic applications for numerous diseases. These are the most common:
- Allergic diseases, such as asthma, rhinitis, and eczema
- Autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis
- Infectious diseases, including those caused by parasites and viruses
- Cancer, as research suggests IL-4 could enhance the immune system's ability to fight cancer cells
Final Thoughts
The future of IL-4 human recombinant seems promising. This laboratory-produced version of an essential type-2 cytokine may be key to developing innovative therapies. However, more research is needed on potential applications to determine if it's safe and effectiv.
What is the molecular weight/Mw of IL 4 HUMAN Protein?
IL 4 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IL 4 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL 4 HUMAN Protein?
IL 4 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

What is the amino acid sequence of IL 4 HUMAN Protein?
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.

What applications can IL 4 HUMAN Protein be used in?
IL 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 HUMAN Protein?
The endotoxin level is minimal, IL 4 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 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 IL 4 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.594 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-4 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-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

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-13 Rhesus Macaque Recombinant

NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

Product # :

CYT-175

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

IL 13 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids and having a molecular mass of 12.6kDa.The IL 13 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 containing 3% trehalose.

Purity

Greater than 98.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 5ng/ml, corresponding to a specific activity of > 2×10⁵IU/mg.

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Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-13 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 IL-13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN

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 Mouse Recombinant

Interleukin-19, IL-19, Il19.

Product # :

CYT-855

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Description

Interleukin-19 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.7kDa. The IL-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile filtered aqueous solution containing 5mM Na3PO4 and 150mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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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
Interleukin-19, IL-19, Il19.
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 IL-19 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRRCLISVDMRLIEKSFHEIKRAMQTKDTFKNVTILSLENLRSIKPGDVCCMTNNLL
TFYRDRVFQDHQERSLEVLRRISSIANSFLCVQKSLERCQVHRQCNCSQEATNATRII
HDNYNQLEVSSAALKSLGELNILLAWIDRNHLETPAA.

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-33 Mouse Recombinant

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

Product # :

CYT-655

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Description

Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

Source

Escherichia Coli.

Formulation

The Mouse IL-33 was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of murine D10S cells is 0.04ng/ml, corresponding to a specific activity of 2.5x10⁷units/mg.

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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-33 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI.

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-21 Receptor Mouse Recombinant

Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

Product # :

CYT-1204

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Description

IL21R Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 457amino acids (20-237 a.a) and having a molecular mass of 52 kDa.IL21R is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IL21R solution (0.25mg/1ml) contains PBS (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit IFN-g secretion using NK-92 human natural killer cells. The ED50 range ≤ 4 ug/ml with mouse IL-2.

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Introduction
IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in na?ve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (?c) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.
Synonyms
Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.
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
CLDLTCYTDY LWTITCVLET RSPNPSILSL TWQDEYEELQ DQETFCSLHR SGHNTTHIWY TCHMRLSQFL SDEVFIVNVT DQSGNNSQEC GSFVLAESIK PAPPLNVTVA FSGRYDISWD SAYDEPSNYV LRGKLQYELQ YRNLRDPYAV RPVTKLISVD SRNVSLLPEE FHKDSSYQLQ VRAAPQPGTS FRGTWSEWSD PVIFQTQAGE PEAGWDPHLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

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

Description:

Interleukin-3 Receptor Subunit Alpha Human Recombinant

Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

Product # :

CYT-1049

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Description

IL3RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-305 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 295 amino acids and having a molecular mass of 34.1kDa.IL3RA is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL3RA protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
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
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.
Background
What is the molecular weight/Mw of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein has a total Mw of 34.1kDa.

What is the source or expression system of IL 3 RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RA HUMAN Protein?
The biological functionality of IL 3 RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 3 RA HUMAN Protein?
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.

What applications can IL 3 RA HUMAN Protein be used in?
IL 3 RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RA HUMAN Protein?
The endotoxin level is minimal, IL 3 RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RA 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 IL 3 RA 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-1 alpha Mouse Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-523

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Description

Interleukin-1A Mouse Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 156 amino acids and having a molecular mass of 17.9 kDa. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 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-dependant stimulation of murine D10S cells is < 0.002 ng/ml.

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
Background
What is the molecular weight/Mw of IL1A MOUSE Protein?
IL1A MOUSE Protein has a total Mw of 17.9kDa.

What is the source or expression system of IL1A MOUSE Protein?
Escherichia Coli.

What is the Purity of IL1A MOUSE Protein?
IL1A MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE Protein?
The biological functionality of IL1A MOUSE Protein will be determined in the future.

What is the amino acid sequence of IL1A MOUSE Protein?
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
What applications can IL1A MOUSE Protein be used in?
IL1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE Protein?
The endotoxin level is minimal, IL1A MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-24 Human Recombinant

C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.

Product # :

CYT-515

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Description

Interleukin 24 human recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18 kDa. As a result of glycosylation, the protein migrates at 19.5 kDa on SDS-PAGE.

Source

Sacharomyces cerevisiae.

Formulation

Lyophilized from a 0.2µm filtered solution in PBS with BSA as a carrier.

Purity

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

Biological Activity

Measured by its ability to bind to the cell receptor of Capan-1 cells line resulted in Stat-3 activation. The ED₅₀ for this effect is typically 1.0 ng/ml, corresponding to a Specific Activity of 1x10⁶ units/mg.

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Introduction
IL24 is a member of the IL10 family of cytokines. It was identified as a gene induced during terminal differentiation in melanoma cells. IL-10B encoded can induce apoptosis selectively in various cancer cells. Overexpression IL-24 leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Alternatively spliced transcript variants encoding distinct isoforms have been reported. The glycosylation is essential for activity of IL-24. Functionally, IL-24 has diverse activities. At low concentrations, it induces type I proinflammatory cytokines such as IFN-g, IL-1b, IL-12 and TNF-a. At high concentration, it is a strong inducer of apoptosis in tumor cells, but not normal cells. mda-7/IL-24 is being hailed as a ‘magic bullet’ for cancer gene therapy.
Synonyms
C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MDA7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MDA-7 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-24 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Interleukin-22 Mouse Recombinant, Pegylated

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-701

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Shipped at Room temp

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Description

Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Interleukin 12, Sf9 Human Recombinant

Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.

Product # :

CYT-1058

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Description

IL12 Mouse Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-335aa, total of 319 aa, MW 35.7kDa) and IL12B (23-215aa, total of 199 aa, MW 22.5kDa), having a total predicted molecular mass of 58.3kDa (Molecular weight on SDS-PAGE will appear higher). IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL12 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

SDS-PAGE

More Info

Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is a crucial part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
Synonyms
Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
IL12B(p40)
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
IL12A(p35)
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
VTINRVMGYL SSAHHHHHH.
Background
What is the molecular weight/Mw of IL12 MOUSE, SF9 Protein?
IL12 MOUSE, SF9 Protein has a total Mw of 58.3kDa.

What is the source or expression system of IL12 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of IL12 MOUSE, SF9 Protein?
IL12 MOUSE, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 MOUSE, SF9 Protein?
The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

What is the amino acid sequence of IL12 MOUSE, SF9 Protein?
IL12B(p40)
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
IL12A(p35)
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
VTINRVMGYL SSAHHHHHH.
What applications can IL12 MOUSE, SF9 Protein be used in?
IL12 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL12 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 MOUSE, 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 IL12 MOUSE, 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-17B Human Recombinant, Sf9

Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.

Product # :

CYT-1004

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Shipping Method :

Shipped with Ice Packs

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Citations

Description

IL17B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 169 amino acids (21-180a.a.) and having a molecular mass of 19.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL17B is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17B protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.
Synonyms
Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.
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
ADPQPRSPKS KRKGQGRPGP LAPGPHQVPL DLVSRMKPYA RMEEYERNIE EMVAQLRNSS ELAQRKCEVN LQLWMSNKRS LSPWGYSINH DPSRIPVDLP EARCLCLGCV NPFTMQEDRS MVSVPVFSQV PVRRRLCPPP PRTGPCRQRA VMETIAVGCT CIFHHHHHH.

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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