Search: 1000 results found for "Interleukin"

Description:

Interleukin-17D Human Recombinant

Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

Product # :

CYT-876

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Description

Interleukin-17D Human Recombinant (18-202) produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 polypeptide chains of 185 amino acids each and having a molecular mass of 40kDa.The IL-17D is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Immobilized rHuIL-17D binds to rHuIL-17BR with EC₅₀ less than 2µg/ml.

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Introduction
IL17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines, as well as suppressing the proliferation of myeloid progenitors. IL17D is expressed in the skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Among IL-17 family members, IL17D is most closely related to IL17B, sharing 27% aa sequence identity. The treatment of endothelial cells with IL17D cytokine stimulates the production of other cytokines including IL6, IL8 and CSF2/ GM-CSF. The increased expression of IL8 induced by IL17D cytokine is NF-kappa B-dependent.
Synonyms
Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL17D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-17D 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-17D in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APRAGRRPAR PRGCADRPEE LLEQLYGRLA AGVLSAFHHT LQLGPREQAR NASCPAGGRP ADRRFRPPTN LRSVSPWAYR ISYDPARYPR YLPEAYCLCR GCLTGLFGEE DVRFRSAPVY MPTVVLRRTP ACAGGRSVYT EAYVTIPVGC TCVPEPEKDA DSINSSIDKQ GAKLLLGPND APAGP.

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 Rat Recombinant

Interleukin 9, Protein Il9, Il9.

Product # :

CYT-748

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Description

Interleukin-9 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa.The IL-9 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL9 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 a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 10⁵ IU/mg.

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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
Interleukin 9, Protein Il9, Il9.
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
MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.
Background
What is the molecular weight/Mw of IL9 RAT Protein?
IL9 RAT Protein has a total Mw of 14.3kDa.

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

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

What is the Biological Activity of IL9 RAT Protein?
The ED50 as determined by a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

What is the amino acid sequence of IL9 RAT Protein?
MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.

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

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

Who supplies recombinant IL9 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 IL9 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-5 Receptor Alpha Human Recombinant

Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.

Product # :

cyt-1067

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Description

IL5RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-342a.a.) and having a molecular mass of 37.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL5RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL5RA protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.
Synonyms
Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.
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
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
Background
What is the molecular weight/Mw of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein has a total Mw of 37.8kDa.

What is the source or expression system of IL 5 RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 RA HUMAN Protein?
The biological functionality of IL 5 RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 5 RA HUMAN Protein?
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
What applications can IL 5 RA HUMAN Protein be used in?
IL 5 RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 RA HUMAN Protein?
The endotoxin level is minimal, IL 5 RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 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 5 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-16 Rhesus Macaque Recombinant

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

Product # :

CYT-153

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Description

IL 16 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 12.5kDa.The IL 16 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2?m filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by 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 50.0-100.0ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

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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 IL-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-16 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-16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAASASAASD VSVESSAEAT VYTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETIQPG DEILQLAGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QPKETTAAAD 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-32 alpha Human Recombinant

NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

Product # :

CYT-584

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Description

Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids and having a molecular mass of 14.9 kDa.

Source

Escherichia Coli.

Formulation

IL-32 was lyophilized from a concentrated (1mg/ml) solution in water containing 50mM sodium Phosphate buffer pH=7.5.

Purity

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

Biological Activity

Human IL-32 alpha activity is measured via the dose-dependent induction of TNF-alpha in the human THP-1 monocytic cell line.

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Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of IFNgamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases.
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL32 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL32 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-32 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCFPKVLSDD MKKLKARMHQ AIERFYDKMQ NAESGRGQVM SSLAELEDDF KEGYLETVAA YYEEQHPELT PLLEKERDGL RCRGNRSPVP DVEDPATEEP GESFCDKSYG APRGDKEELT PQKCSEPQSS K.

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

Description:

Interleukin-18 Human Recombinant, His Tag

Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.

Product # :

CYT-663

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Description

Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 157 amino acids fragment (37-193) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-18 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin -18 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

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

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 1 Family, Member 10 Human Recombinant, His Tag

Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.

Product # :

CYT-783

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Shipped with Ice Packs

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Description

IL1F10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152) and having a molecular mass of 19.1kDa.IL1F10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL1F10 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
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 MCSLPMARYY IIKYADQKAL YTRDGQLLVG DPVADNCCAE KICTLPNRGL DRTKVPIFLG IQGGSRCLAC VETEEGPSLQ LEDVNIEELY KGGEEATRFT FFQSSSGSAF RLEAAAWPGW FLCGPAEPQQ PVQLTKESEP SARTKFYFEQ SW

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 Mouse Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-371

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.
Background
What is the molecular weight/Mw of IL3 MOUSE Protein?
IL3 MOUSE Protein has a total Mw of 15.1kDa.

What is the source or expression system of IL3 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL3 MOUSE Protein?
IL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

What is the amino acid sequence of IL3 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

What applications can IL3 MOUSE Protein be used in?
IL3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 MOUSE Protein?
The endotoxin level is minimal, IL3 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 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 IL3 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL3 as a Reference Standard.

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

Description:

Interleukin-7 Human Recombinant, Yeast

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

Product # :

CYT-298

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Quantity :

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Shipped at Room temp

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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.

More Info

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 Feline Recombinant

Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.

Product # :

CYT-1018

Price :

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Description

IL2 Feline Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids (21-154 a.a) and having a molecular mass of 17.8kDa. IL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL2 protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is less or equal to 0.3ng/ml.

SDS-PAGE

More Info

Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.
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 MGSAPASSST KETQQQLEQL LLDLRLLLNG VNNPENPKLS RMLTFKFYVP KKATELTHLQ CLVEELKPLE EVLYLAQSKN FHLNHIKELM SNINVTVLKL KGSETRFTCN YDDETATIVE FLNKWITFCQ SIFSTLT.
Background
What is the molecular weight/Mw of IL 2 FELINE Protein?
L 2 FELINE Protein has a total Mw of 17.8kDa.

What is the source or expression system of IL 2 FELINE Protein?
Escherichia Coli.

What is the Purity of IL 2 FELINE Protein?
IL 2 FELINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 FELINE Protein?
Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is less or equal to 0.3ng/ml.

What is the amino acid sequence of IL 2 FELINE Protein?
MGSSHHHHHH SSGLVPRGSH MGSAPASSST KETQQQLEQL LLDLRLLLNG VNNPENPKLS RMLTFKFYVP KKATELTHLQ CLVEELKPLE EVLYLAQSKN FHLNHIKELM SNINVTVLKL KGSETRFTCN YDDETATIVE FLNKWITFCQ SIFSTLT.

What applications can IL 2 FELINE Protein be used in?
IL 2 FELINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 FELINE Protein?
The endotoxin level is minimal, IL 2 FELINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 FELINE 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 2 FELINE?
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-18 Mouse Recombinant

Interleukin-18, IL-18, IFN gamma-inducing factor, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma.

Product # :

CYT-882

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL 18 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (36-192 a.a.) and having a molecular mass of 18.2kDa. The IL 18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL 18 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
Synonyms
Interleukin-18, IL-18, IFN gamma-inducing factor, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma.
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
MNFGRLHCTT AVIRNINDQV LFVDKRQPVF EDMTDIDQSA SEPQTRLIIY MYKDSEVRGL AVTLSVKDSK MSTLSCKNKI ISFEEMDPPE NIDDIQSDLI FFQKRVPGHN KMEFESSLYE GHFLACQKED DAFKLILKKK DENGDKSVMF TLTNLHQS.

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 Receptor Type 2 Human Recombinant

IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB, IL-1 type II receptor, Interleukin-1 receptor beta, CD121 antigen-like family member B.

Product # :

CYT-1056

Price :

Quantity :

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Shipped with Ice Packs

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Description

IL1R2 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 338 amino acids (14-343a.a.) and having a molecular mass of 38.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1R2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL1R2 protein solution (0.5mg/ml) contains PBS (pH7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ to 400 ng/ml with IL-1beta.

More Info

Introduction
IL1R2 is a cytokine receptor which is a part of the interleukin-1 receptor family. IL1R2 is expressed mainly by T cells, endothelial cells and fibroblasts. IL1R2 binds IL1A, IL1B and IL1RN preventing them from binding to their regular receptors and thus inhibiting the transduction of their signaling. Also, Interleukin-4 antagonizes the activity of interleukin-1 by inducing the expression and release of this protein.
Synonyms
IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB, IL-1 type II receptor, Interleukin-1 receptor beta, CD121 antigen-like family member B.
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
FTLQPAAHTG AARSCRFRGR HYKREFRLEG EPVALRCPQV PYWLWASVSP RINLTWHKND SARTVPGEEE TRMWAQDGAL WLLPALQEDS GTYVCTTRNA SYCDKMSIEL RVFENTDAFL PFISYPQILT LSTSGVLVCP DLSEFTRDKT DVKIQWYKDS LLLDKDNEKF LSVRGTTHLL
VHDVALEDAG YYRCVLTFAH EGQQYNITRS IELRIKKKKE ETIPVIISPL KTISASLGSR LTIPCKVFLG TGTPLTTMLW WTANDTHIES AYPGGRVTEG PRQEYSENNE NYIEVPLIFD PVTREDLHMD FKCVVHNTLS FQTLRTTVKE LEHHHHHH.
Background
What is the molecular weight/Mw of IL1R2 HUMAN Protein?
IL1R2 HUMAN Protein has a total Mw of 38.8kDa.

What is the source or expression system of IL1R2 HUMAN Protein?
Sf9, Insect cells.

What is the Purity of IL1R2 HUMAN Protein?
IL1R2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1R2 HUMAN Protein?
Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ to 400 ng/ml with IL-1beta.

What is the amino acid sequence of IL1R2 HUMAN Protein?
FTLQPAAHTG AARSCRFRGR HYKREFRLEG EPVALRCPQV PYWLWASVSP RINLTWHKND SARTVPGEEE TRMWAQDGAL WLLPALQEDS GTYVCTTRNA SYCDKMSIEL RVFENTDAFL PFISYPQILT LSTSGVLVCP DLSEFTRDKT DVKIQWYKDS LLLDKDNEKF LSVRGTTHLL
VHDVALEDAG YYRCVLTFAH EGQQYNITRS IELRIKKKKE ETIPVIISPL KTISASLGSR LTIPCKVFLG TGTPLTTMLW WTANDTHIES AYPGGRVTEG PRQEYSENNE NYIEVPLIFD PVTREDLHMD FKCVVHNTLS FQTLRTTVKE LEHHHHHH.

What applications can IL1R2 HUMAN Protein be used in?
IL1R2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1R2 HUMAN Protein?
The endotoxin level is minimal, IL1R2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1R2 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 IL1R2 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 His Tag Human Recombinant

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-846

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Quantity :

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Shipped with Ice Packs

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Description

IL12 Human Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-219aa, total of 203 aa, MW 23.3kDa) and IL12B (23-328aa, total of 306 aa, MW 34.6kDa), having a total predicted molecular mass of 57.9kDa (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

Baculovirus.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED₅₀ for this effect is less than or equal to 0.03 ng/ml.

SDS-PAGE

More Info

Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.
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 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
IL12A(p35):
RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.

IL12B(p40):
IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.
Background
What is the molecular weight/Mw of IL12 HUMAN, HIS Protein?
IL12 HUMAN, HIS Protein has a total Mw of 57.9kDa.

What is the source or expression system of IL12 HUMAN, HIS Protein?
Baculovirus.
What is the Purity of IL12 HUMAN, HIS Protein?
IL12 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 HUMAN, HIS Protein?
The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

What is the amino acid sequence of IL12 HUMAN, HIS Protein?
IL12A(p35):
RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.
IL12B(p40):
IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

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

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

Who supplies recombinant IL12 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 IL12 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-36 Receptor Antagonist Human Recombinant

Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

Product # :

CYT-009

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

Purity

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

Biological Activity

As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

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Introduction
Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.
Synonyms
Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/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-Val-Leu-Ser-Gly.

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 Receptor Alpha Human Recombinant, BioActive

Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

Product # :

CYT-1142

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL10RA Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 220 amino acids (22-235 aa) and having a molecular mass of 25.2kDa.IL10RA is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL10RA solution (0.2mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

More Info

Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein has a total Mw of 25.2kDa.

What is the source or expression system of IL10RA HUMAN, ACTIVE Protein?
Sf9, Baculovirus cells.
What is the Purity of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RA HUMAN, ACTIVE Protein?
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

What is the amino acid sequence of IL10RA HUMAN, ACTIVE Protein?
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH.

What applications can IL10RA HUMAN, ACTIVE Protein be used in?
IL10RA HUMAN, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10RA HUMAN, ACTIVE Protein?
The endotoxin level is minimal, IL10RA HUMAN, ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10RA HUMAN, ACTIVE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL10RA HUMAN, ACTIVE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-17 Mouse Recombinant

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

Product # :

CYT-378

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Quantity :

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Description

Interleukin-17 Murine Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 268 (2x134 a.a.) amino acids and having a molecular mass of 30 kDa. The IL-17 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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant induction of IL-6 production in cultured mouse NIH 3T3 fibroblasts was found to be 0.4 ng/ml, corresponding to a specific activity of 2,500,000 units/mg.

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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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 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 17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAAIIPQSSA CPNTEAKDFL QNVKVNLKVF NSLGAKVSSR RPSDYLNRST SPWTLHRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPESCPF TFRVEKMLVG VGCTCVASIV RQAA.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.942 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-17 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-6 Rat Recombinant, sf9

IL6, Ifnb2, ILg6.

Product # :

CYT-1048

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Description

IL6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (25-211 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL6 protein solution (0.5mg/ml) contains 20% glycerol & 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 M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IL6, Ifnb2, ILg6.
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
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH
Background
Production and Applications of Rat Recombinant Interleukin-6 in sf9 Cells
Abstract:
Interleukin-6 (IL-6) is a critical cytokine involved in various physiological processes, including inflammation, immune responses, and hematopoiesis. The production of recombinant IL-6 has paved the way for numerous applications in research and therapeutic development. This paper elucidates the production of Rat Recombinant IL-6 in sf9 cells using baculovirus expression system and explores its potential applications in immunology and disease research.
Introduction:
Interleukin-6 is a pleiotropic cytokine with diverse functions in immune regulation, acute phase responses, and tissue homeostasis. The ability to produce recombinant IL-6 allows researchers to investigate its role in various biological contexts and develop potential therapies. The sf9 cell line, derived from Spodoptera frugiperda insect cells, offers an efficient platform for recombinant protein expression through the baculovirus system.
Methods:
The production of Rat Recombinant IL-6 involves inserting the rat IL-6 gene into a baculovirus transfer vector. This vector is then co-transfected with a linearized baculovirus DNA into sf9 cells. The resulting recombinant baculovirus expresses the IL-6 protein, which is secreted into the culture medium. The expressed protein is subsequently purified using chromatographic techniques to ensure its quality and activity.
Applications:
Rat Recombinant IL-6 produced in sf9 cells has widespread applications. It serves as a valuable tool for investigating the mechanisms underlying IL-6-mediated immune responses, inflammation, and hematopoiesis. Furthermore, it enables the development of potential therapies targeting IL-6-related disorders, including autoimmune diseases, inflammatory conditions, and certain types of cancer.
Advantages of sf9 Expression:
The sf9 expression system offers several advantages, including high protein yields, post-translational modifications, and proper protein folding. This system is especially suitable for complex cytokines like IL-6, which require correct tertiary structure for optimal biological activity.
Challenges and Future Prospects:
While sf9-based expression of Rat Recombinant IL-6 offers numerous benefits, challenges such as optimization of expression conditions, scale-up, and quality control remain. Additionally, further research is needed to explore the therapeutic potential of Rat Recombinant IL-6 in preclinical and clinical settings.
Conclusion:
The production of Rat Recombinant IL-6 in sf9 cells using the baculovirus expression system provides a powerful tool for unraveling the roles of IL-6 in various biological processes. This platform holds promise for advancing our understanding of IL-6-related diseases and facilitating the development of targeted therapeutic interventions.
What is the molecular weight/Mw of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein has a total Mw of 22.8kDa.

What is the source or expression system of IL6 RAT, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 RAT, SF9 Protein?
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

What is the amino acid sequence of IL6 RAT, SF9 Protein?
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH.

What applications can IL6 RAT, SF9 Protein be used in?
IL6 RAT, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6 RAT, SF9 Protein?
The endotoxin level is minimal, IL6 RAT, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6 RAT, 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 IL6 RAT, 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-36 Gamma Human Recombinant, His Tag

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-782

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Quantity :

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Shipped with Ice Packs

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Description

IL36G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-169) and having a molecular mass of 21.1kDa.IL36G is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL36G solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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 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 MGSMRGTPGD ADGGGRAVYQ SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND

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-15 Human Recombinant, HEK

IL-15, IL15, Interleukin-15, MGC9721.

Product # :

CYT-967

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-15 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 12.8kDa.The IL15 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The IL-15 protein was lyophilized from 1842µl filtered (0.2µm) solution in PBS, pH 7.4 and 10% Trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity was determined by the dose dependent stimulation of the proliferation of CTLL-2 cells, the ED₅₀ is typically less than 0.5ng/ml, corresponding to a specific activity of >2 x 10⁶ Unit/mg.

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Introduction
The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.
Synonyms
IL-15, IL15, Interleukin-15, MGC9721.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 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 IL15 with 2500µl PBS to a stock solution of 400µg/ml.

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 Receptor Antagonist Mouse Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

Product # :

CYT-658

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL1 ra Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.4kDa. The IL1ra is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution in water containing NaHCO3.

Purity

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

Biological Activity

The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1ra 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 six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.
Background
What is the molecular weight/Mw of IL1RA MOUSE Protein?
IL1RA MOUSE Protein has a total Mw of 17.4kDa.

What is the source or expression system of IL1RA MOUSE Protein?
Escherichia Coli.

What is the Purity of IL1RA MOUSE Protein?
IL1RA MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RA MOUSE Protein?
The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

What is the amino acid sequence of IL1RA MOUSE Protein?
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.

What applications can IL1RA MOUSE Protein be used in?
IL1RA MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RA MOUSE Protein?
The endotoxin level is minimal, IL1RA MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RA 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 IL1RA MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.91 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).

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 Receptor Antagonist (Y51A), PEG Mouse Recombinant

Product # :

CYT-1248

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Shipped at Room temp

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Description

Interleukin 22 Y51A mutan Mouse Recombinant is a single non-glycosilated polypeptide chain containing 147 amino acids and additional Ala at N-terminus. The iL22RA is bound to 20 kDa PEG molecule at N-terminus, resulting in 36.0 kDa. The Mouse iL22RA (Y51A) Pegylated runs as a 50 kDa due to enlarged hydrodymanic volume. iL22RA Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse iL22RA (Y51A) was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Mouse iL22RA inhibits mouse IL-22 induced STAT3 phosphorylation in HepG cells. Its inhibitory acrtivity in vitro is ~ 10-20% compared to the non-pegylated mIL22 (Y51A) mutant.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized iL22RA (Y51A) Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization iL22RA mutant can be stored at 4°C or even room temperature 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 iL22RA (Y51A) Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
IL-22 is a part of the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes part in wound healing and in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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-29 Human Recombinant, His Tag

Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.

Product # :

CYT-864

Price :

Quantity :

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Description

IL 29 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (20-200 a.a) and having a molecular mass of 22.7kDa.IL 29 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 29 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
IL-29 is distantly related to type I interferons 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 Interferon-Lambda 2 receptor tyrosine residues.
Synonyms
Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.
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 MGSHMGPVPT SKPTTTGKGC HIGRFKSLSP QELASFKKAR DALEESLKLK NWSCSSPVFP GNWDLRLLQV RERPVALEAE LALTLKVLEA AAGPALEDVL DQPLHTLHHI LSQLQACIQP QPTAGPRPRG RLHHWLHRLQ EAPKKESAGC LEASVTFNLF RLLTRDLKYV ADGNLCLRTS THPEST.

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 Mouse Recombinant

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

Product # :

CYT-373

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.

Purity

Greater than 95% as determined by RP-HPLC and SDS-PAGE analysis.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

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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
MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-9 as a Reference Standard.

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

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Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info