Search: 1000 results found for "interleukin"

Description:

Interleukin-7 Rat Recombinant

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

Product # :

CYT-163

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Shipped at Room temp

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Description

IL 7 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 15.0kDa.The IL 7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2ng/ml, corresponding to a specific activity of >5,000,000IU/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 IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-7 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-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DCHIKDKDGK AFGSVLMISI NQLDKMTGTD SDCPNNEPNF FKKHLCDDTK EAAFLNRAAR KLRQFLKMNI SEEFNDHLLR VSDGTQTLVN CTSKEEKTIK EQKKNDPCFL KRLLREIKTC WNKILKGSI
Background
What is the molecular weight/Mw of IL7 RAT Protein?
IL7 RAT Protein has a total Mw of 15kDa.

What is the source or expression system of IL7 RAT Protein?
Escherichia Coli.

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

What is the Biological Activity of IL7 RAT Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2ng/ml, corresponding to a specific activity of >5,000,000IU/mg.

What is the amino acid sequence of IL7 RAT Protein?
DCHIKDKDGK AFGSVLMISI NQLDKMTGTD SDCPNNEPNF FKKHLCDDTK EAAFLNRAAR KLRQFLKMNI SEEFNDHLLR VSDGTQTLVN CTSKEEKTIK EQKKNDPCFL KRLLREIKTC WNKILKGSI.

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

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

Who supplies recombinant IL7 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 IL7 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-10 Mouse Recombinant

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

Product # :

CYT-497

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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.

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
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-1 beta Human Recombinant, His Tag

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

Product # :

CYT-480

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Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial 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 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
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
Background
What is the molecular weight/Mw of IL1B HUMAN, HIS Protein?
IL1B HUMAN, HIS Protein has a total Mw of 21.88kDa.

What is the source or expression system of IL1B HUMAN, HIS Protein?
Escherichia Coli.

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

What is the Biological Activity of IL1B HUMAN, HIS Protein?
The biological functionality of IL1B HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1B HUMAN, HIS Protein?
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

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

What is the endotoxin level for IL1B HUMAN, HIS Protein?
The endotoxin level is minimal, IL1B HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-12 p40 Human Recombinant

NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

Product # :

CYT-488

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Shipped with Ice Packs

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Description

Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
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.
Background
What is the source or expression system of IL12P40 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL12P40 HUMAN Protein?
IL12P40 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12P40 HUMAN Protein?
The biological functionality of IL12P40 HUMAN Protein will be determined in the future.

What applications can IL12P40 HUMAN Protein be used in?
IL12P40 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12P40 HUMAN Protein?
The endotoxin level is minimal, IL12P40 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12P40 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 IL12P40 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-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

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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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-2 Feline Recombinant

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

Product # :

CYT-1018

Price :

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Shipped with Ice Packs

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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

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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-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

Price :

Quantity :

Shipping Method :

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-10 Human Recombinant

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

Product # :

CYT-500

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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biological activity
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Description

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

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

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

Biological Activity

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

More Info

Introduction
Recombinant IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL10 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN Protein?
IL10 HUMAN Protein has a total Mw of 18.6kDa.

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

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

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

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

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

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

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

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

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

Description:

Interleukin 1 Receptor Type I Human Recombinant

Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.

Product # :

CYT-923

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Description

IL1R1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 324 amino acids (21-336a.a.) and having a molecular mass of 37.4kDa(Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL1R1 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1R1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interleukin-1 receptor type 1 (IL1R1) associates with the co-receptor IL1RAP to form the high affinity interleukin-1 receptor complex, which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. IL1R1 is a central mediator involved in numerous cytokine induced immune and inflammatory responses.
Synonyms
Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.
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
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
Background
What is the molecular weight/Mw of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein has a total Mw of 37.4kDa.

What is the source or expression system of IL1R1 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1R1 HUMAN Protein?
The biological functionality of IL1R1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL1R1 HUMAN Protein?
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
What applications can IL1R1 HUMAN Protein be used in?
IL1R1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1R1 HUMAN Protein?
The endotoxin level is minimal, IL1R1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1R1 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 IL1R1 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-31 Canine Recombinant, HEK

IL-31, Interleukin 31, IL31.

Product # :

CYT-1215

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Description

IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Synonyms
IL-31, Interleukin 31, IL31.
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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.

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 p35 Human Recombinant

NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

Product # :

CYT-487

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Description

Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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.
Background
What is the source or expression system of IL12P35 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL12P35 HUMAN Protein?
IL12P35 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12P35 HUMAN Protein?
The biological functionality of IL12P35 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL12P35 HUMAN Protein?
IL12P35 HUMAN Protein is composed from 197 amino acids.

What applications can IL12P35 HUMAN Protein be used in?
IL12P35 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12P35 HUMAN Protein?
The endotoxin level is minimal, IL12P35 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12P35 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 IL12P35 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-36 Beta Mouse Recombinant

Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

Product # :

CYT-165

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Description

IL36B Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 183 amino acids and having a molecular mass of 21.0kDa.The IL36B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
Mouse IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (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. Mouse IL-36b/IL-1F8 is a 183 amino acid protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation site(s). Mouse IL-36b like its human homologue is actively secreted. Mouse IL-36?/IL-1F8 shares 61-74% aa homology with human IL-36?/IL-1F8 isoform 2 and rat IL-1F8.
Synonyms
Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36B Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36B 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 IL36B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MMAFPPQSCV HVLPPKSIQM WEPNHNTMHG SSQSPRNYRV HDSQQMVWVL TGNTLTAVPA SNNVKPVILS LIACRDTEFQ DVKKGNLVFL GIKNRNLCFC CVEMEGKPTL QLKEVDIMNL YKERKAQKAF LFYHGIEGST SVFQSVLYPG WFIATSSIER QTIILTHQRG KLVNTNFYIE SEK

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

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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

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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-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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Shipped at Room temp

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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 1 Family, Member 10 Human Recombinant

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

Product # :

CYT-012

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL1F10 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 152 amino acids and having a molecular mass of 17kDa.The IL1F10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL1F10 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

Purity

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

Biological Activity

As measured by its binding ability in a functional ELISA, immobilized IL1F10 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

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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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1F10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F10 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to quick spin followed by reconstitution of IL1F10 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Cys-Ser-Leu-Pro.

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

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

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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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-36 Gamma Mouse Recombinant

Interleukin-36 gamma, Interleukin-1 family member 9, IL-1F9, Il36g, Il1f9.

Product # :

CYT-745

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Description

IL36G Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.3kDa.The IL36G is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1M MOPS, 10 mM NaAC, pH7.6, 5 % Trehalose, 2 mM EDTA and 0.02 % Tween-20.

Purity

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

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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, Interleukin-1 family member 9, IL-1F9, Il36g, Il1f9.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36g Mouse 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
GRETPDFGEV FDLDQQVWIF RNQALVTVPR SHRVTPVSVT ILPCKYPESL EQDKGIAIYL GIQNPDKCLF CKEVNGHPTL LLKEEKILDL YHHPEPMKPF LFYHTRTGGT STFESVAFPG HYIASSKTGN PIFLTSKKGE YYNINFNLDI KS.

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 Rat Recombinant

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

Product # :

CYT-385

Price :

Quantity :

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Shipped at Room temp

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Description

Interleukin-4 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids and having a molecular mass of 14kDa. The IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 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

The ED₅₀ as determined in a cell proliferation assay using rat splenocytes is less than 2ng/ml corresponding to a specific activity of 500,000IU/mg.

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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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 IL4 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 4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.
Background
What is the molecular weight/Mw of IL 4 RAT Protein?
IL 4 RAT Protein has a total Mw of 14kDa.

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

What is the Purity of IL 4 RAT Protein?
IL 4 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 RAT Protein?
The ED50 as determined in a cell proliferation assay using rat splenocytes is less than 2ng/ml corresponding to a specific activity of 500,000IU/mg.

What is the amino acid sequence of IL 4 RAT Protein?
HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.

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

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

Who supplies recombinant IL 4 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 IL 4 RAT?
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 0.2 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 Human Recombinant, His

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

Product # :

CYT-486

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% by SDS-PAGE.

More Info

Introduction
Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN, HIS Protein?
IL10 HUMAN, HIS Protein has a total Mw of 20.94kDa.

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

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

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

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

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

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

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

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

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

Description:

Interleukin-3 Mouse Recombinant

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

Product # :

CYT-371

Price :

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.

More Info

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-18 Binding Protein Human Recombinant

Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.

Product # :

CYT-728

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Shipped with Ice Packs

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Description

IL18BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (31-194 a.a) and having a molecular mass of 20kDa. IL18BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL18BP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQG.

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

Description:

Interleukin-16 Human Recombinant, His Tag

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

Product # :

CYT-562

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Shipped with Ice Packs

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Description

Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

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 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
MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.

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.

More Info

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.

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