Search: 1000 results found for "Other Cytokines"

Description:

Interleukin-7 Human Recombinant

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

Product # :

CYT-254

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Shipped at Room temp

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Description

Interleukin-7 Human Recombinant produced in E.Coli is a single, non-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

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 1x 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-dependant stimulation of murine 2E8 cells is < 0.5ng/ml, corresponding to a Specific Activity of 2,000,000 IU/mg.

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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DCDIEGKDG KQYESVLMVS IDQLLDSMKE IGSNCLNNEF NFFKRHICDA NKEGMFLFRA ARKLRQFLKM NSTGDFDLHL LKVSEGTTIL LNCTGQVKGR KPAALGEAQP TKSLEENKSL KEQKKLNDLC FLKRLLQEIK TCWNKILMGT KEH.
Background
What is the molecular weight/Mw of IL7 HUMAN Protein?
IL7 HUMAN Protein has a total Mw of 17.4kDa.

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

What is the Purity of IL7 HUMAN Protein?
IL7 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of murine 2E8 cells is < 0.5ng/ml, corresponding to a Specific Activity of 2,000,000 IU/mg.

What is the amino acid sequence of IL7 HUMAN Protein?
DCDIEGKDG KQYESVLMVS IDQLLDSMKE IGSNCLNNEF NFFKRHICDA NKEGMFLFRA ARKLRQFLKM NSTGDFDLHL LKVSEGTTIL LNCTGQVKGR KPAALGEAQP TKSLEENKSL KEQKKLNDLC FLKRLLQEIK TCWNKILMGT KEH.

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

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

Who supplies recombinant IL7 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 IL7 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-23 Human Recombinant, His Tag

Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.

Product # :

CYT-067

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Shipped with Ice Packs

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Description

Recombinant Human Interleukin-23 produced in Sf9 Baculovirus cells is a glycosylated heterodimer composed of 2 disulfide-linked subunits. A p19 subunit which is unique to IL23 and a p40 subunit which is shared with IL12. The p19 subunit/IL23A (20-189aa, total of 176 aa, MW 19.5kDa) and p40 subunit /IL12B (23-328aa, total of 306 aa, MW 34.6kDa), the total predicted molecular mass of 54.1kDa (Molecular weight on SDS-PAGE will appear higher). IL23 is fused to a 6 aa His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL23 protein solution (1mg/ml) contains PBS (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
IL23 is composed of a subunit of the heterodimeric cytokine IL23 and the p40 subunit of interleukin 12 (IL12B). Interleukin-23 (IL-23) belongs to the IL-12 family and is produced by antigen presenting cells. IL-23 using IL12RB1 and IL-23R (specific for IL-23) can activate STAT and NF-kB pathways and stimulate the production of interferon-gamma. ). IL-23 is known to take a vital part in the inflammation process and is associated with auto immune diseases. However, unlike IL12, which acts primarily on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.
Synonyms
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
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
IL12B: 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.
IL23A: RAVPGGSSPA WTQCQQLSQK LCTLAWSAHP LVGHMDLREE GDEETTNDVP HIQCGDGCDP QGLRDNSQFC LQRIHQGLIF YEKLLGSDIF TGEPSLLPDS PVGQLHASLL GLSQLLQPEG HHWETQQIPS LSPSQPWQRL LLRFKILRSL QAFVAVAARV FAHGAATLSP HHHHHH.

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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Shipping Method :

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-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

Price :

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Shipping Method :

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.

More Info

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:

Interferon Alpha And Beta Receptor Subunit 2 Human Recombinant

Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.

Product # :

CYT-1167

Price :

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Shipped with Ice Packs

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SDS-PAGE
Citations

Description

IFNAR2 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 456 amino acids (27-243 a.a.) and having a molecular mass of 51.7kDa. IFNAR2 is fused to an 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IFNAR2 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.

SDS-PAGE

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Introduction
Interferon Alpha and Beta Receptor Subunit 2 or IFNAR2 is a protein, part of the class II cytokine receptor family. When different innate immune signaling transduction are activated, there is a rapid induction of type I IFNs because it has an intronless gene source. IFNAR2 is the main ligand and binds to the receptor. Once bind, stabilization occurs and a signaling compelx recptor is formed. IFNAR2 also takes part in the activation process of STAT proteins.
Synonyms
Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.
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
ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
Background
What is the molecular weight/Mw of IFNAR2 HUMAN Protein?
IFNAR2 HUMAN Protein has a total Mw of 51.7kDa.

What is the source or expression system of IFNAR2 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IFNAR2 HUMAN Protein?
IFNAR2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNAR2 HUMAN Protein?
The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.

What is the amino acid sequence of IFNAR2 HUMAN Protein?
ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
What applications can IFNAR2 HUMAN Protein be used in?
IFNAR2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNAR2 HUMAN Protein?
The endotoxin level is minimal, IFNAR2 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-2 Receptor Beta Human Recombinant

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

Product # :

CYT-1086

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Shipped with Ice Packs

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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin 2 receptor is a protein that involves immune responses that are mediated through T cells. The IL2 receptor exists in three ways in which it can bind to IL2. CD25 is the lowest affinity (a monomer of the alpha subunit), therefore, it is not part of the signal transduction process. The highest affinity has three heterotrimer subunits (alpha/beta/gamma), the intermediate affinity is found to have gamma/beta subunit heterodimer. Both forms are part of the receptor mediated endocytosis and mitogenic signals transduction from IL2.
Synonyms
Interleukin 2 receptor subunit beta, IL2RB, CD122, IL15RB, P70-75, IL-2R subunit beta.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
AVNGTSQFTC FYNSRANISC VWSQDGALQD TSCQVHAWPD RRRWNQTCEL LPVSQASWAC NLILGAPDSQ KLTTVDIVTL RVLCREGVRW RVMAIQDFKP FENLRLMAPI SLQVVHVETH RCNISWEISQ ASHYFERHLE FEARTLSPGH TWEEAPLLTL KQKQEWICLE TLTPDTQYEF QVRVKPLQGE FTTWSPWSQP LAFRTKPAAL GKDTHHHHHH.
Background
What is the molecular weight/Mw of CD122 HUMAN Protein?
CD122 HUMAN Protein has a total Mw of 25.5kDa.
What is the source or expression system of CD122 HUMAN Protein?
Sf9, Baculovirus cells.
What is the Purity of CD122 HUMAN Protein?
CD122 HUMAN Protein is >95% pure as determined by SDS-PAGE.

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

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

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

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

Who supplies recombinant CD122 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CD122 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-6 Mouse Recombinant

IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

Product # :

CYT-350

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

Interleukin-6 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21709 Dalton. The IL-6 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 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

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
IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Mouse Il-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.
Background
Research Paper on Interleukin-6 Mouse Recombinant
Abstract:
Interleukin-6 (IL-6) Mouse Recombinant stands at the forefront of immunological exploration, unraveling the intricacies of immune modulation. This research paper delves into its molecular attributes and implications within the realm of immunological studies. By examining its functions, synonyms like DIF, TNFA, and TNFSF2, and potential applications, we gain insights into its pivotal role in shaping immune responses.
Introduction:
IL-6 Mouse Recombinant has emerged as a linchpin in immunological research. This paper seeks to comprehensively elucidate its molecular characteristics and the impact it bears on immune mechanisms.
Molecular Architecture and Insights:
Delving into the molecular makeup of IL-6 Mouse Recombinant, we unveil its crucial role in immune signaling. Its interactions and functions contribute significantly to orchestrating immune responses.
Navigating Immune Dynamics:
The well-established influence of IL-6 on immune cell activation and inflammation is a cornerstone. IL-6 Mouse Recombinant allows for a more intricate exploration of these immune processes, augmenting our understanding of cytokine-mediated functions.
Synonyms and Network Connections:
Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, amplifies our grasp of immune signaling networks. IL-6 Mouse Recombinant aids in unraveling the complexity of these interconnected pathways.
Potential Applications in Research and Beyond:
Beyond the confines of research, IL-6 Mouse Recombinant holds promise in deciphering immune-related diseases. Its significance extends to potential therapeutic interventions and diagnostic applications.
Clinical Implications and Future Prospects:
The clinical relevance of IL-6 Mouse Recombinant is underscored by its role in diseases characterized by altered IL-6 signaling. Unearthing its therapeutic potential paves the way for innovative strategies in disease management.
Conclusion:
Within the realm of immunology, IL-6 Mouse Recombinant assumes a pivotal role. Its molecular insights, fundamental functions, and potential applications position it as a cornerstone in advancing our comprehension of immune regulation.
What is the molecular weight/Mw of IL6 MOUSE Protein?
IL6 MOUSE Protein has a total Mw of 21.7kDa.

What is the source or expression system of IL6 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL6 MOUSE Protein?
IL6 MOUSE Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

What is the amino acid sequence of IL6 MOUSE Protein?
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

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

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

Who supplies recombinant IL6 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 IL6 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-27 Human Recombinant

Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.

Product # :

CYT-048

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Description

IL-27 Human Recombinant produced in HEK cells is a glycosylated non-covalently heterodimer that consists of 2 chains, IL27A (IL27p28) having a Mw of 25kDa and IL27B (EBI3) having a Mw of 30kDa. Each chain migrates separately on SDS-PAGE. The IL-27 protein is purified by proprietary chromatographic techniques

Source

HEK.

Formulation

The IL-27 was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 90% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose dependent inhibition of HIV replication in human CD4+ T cells and in human monocyte-derived macrophages and is typically 4-12ng/ml.

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Introduction
Interleukin-27 protein is related to IL-12A & is one of the subunits of a heterodimeric cytokine complex. IL-27 interacts with EBV induced gene 3 also called EBI3, and forms a complex that drives rapid expansion of CD4 (+) T cells. IL-27 complex is synergizes with IL-12 in order to trigger the cytokine production of IFN-Gamma of CD4 (+) T cells. The biological effect of IL-27 is mediated by class-I cytokine receptor (WSX1/TCRR). The pro-inflammatory activity of IL-27 is mediated through the growing expression of key molecules involved in the MHC class-I & MHC class-II pathways. Both MHC class-I and MHC-class-II expression are increased in endothelial cells after Interleukin-27 stimulation which suggests that it may play an important role in conferring the immune function on vascular endothelium IL-27p28 subunit can be induced by IFN-beta and during LPS-induced maturation of dendritic cells in type-I IFN-dependent manner through IFN regulatory factor-1 activation. Interleukin-27 regulates Interleukin-12 responsiveness of CD4+ T cells through Stat1-dependent and -independent mechanisms. IL-17 & IL-23 play an important IL-17 role in inflammation. Interleukin-27 possesses potent anti-angiogenic activity that plays an important role in its antitumor and antimetastatic activities. EBV induced gene 3 plays a role, independently from IL-27, in regulating anti-viral or anti-tumoral immune responses. Interleukin-27 is a potent inhibitor of HIV-1 replication in macrophages, CD4+ T cells, peripheral blood mononuclear cells. Interleukin-27 triggers STAT activation and gene transcription.
Synonyms
Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL27 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-27 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
IL-27A (215aa):
FPRPPGRPQL SLQELRREFT VSLHLARKLL AEVRGQAHRF AESHLPGVNL YLLPLGEQLP DVSLTFQAWR RLSDPERLCF ISTTLQPFHA LLGGLGTQGR WTNMERMQLW AMRLDLRDLQ RHLRFQVLAA GFNLPEEEEE EEEEEEEERK GLLPGALGSA LQGPAQVSWP QLLSTYRLLH SLELVLSRAV RELLLLSKAG HSVWPLGFPT LSPQP.

IL-27B (209aa):
RKGPPAALTL PRVQCRASRY PIAVDCSWTL PPAPNSTSPV SFIATYRLGM AARGHSWPCL QQTPTSTSCT ITDVQLFSMA PYVLNVTAVH PWGSSSSFVP FITEHIIKPD PPEGVRLSPL AERQLQVQWE PPGSWPFPEI FSLKYWIRYK RQGAARFHRV GPIEATSFIL RAVRPRARYY VQVAAQDLTD YGELSDWSLP ATATMSLGK.

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-11 Mouse Recombinant

AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

Product # :

CYT-646

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Description

Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was 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-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

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Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
Synonyms
AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.
Background
What is the molecular weight/Mw of IL11 MOUSE Protein?
IL11 MOUSE Protein has a total Mw of 19.1kDa.

What is the source or expression system of IL11 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL11 MOUSE Protein?
IL11 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL11 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

What is the amino acid sequence of IL11 MOUSE Protein?
MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.
What applications can IL11 MOUSE Protein be used in?
IL11 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL11 MOUSE Protein?
The endotoxin level is minimal, IL11 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL11 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 IL11 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-15 Rat Recombinant

IL-15, MGC9721.

Product # :

CYT-345

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Description

Interleukin-15 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 13533 Dalton. The IL-15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 10mM Tris, pH-8.5.

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 stimulation of the proliferation of CTLL-2 was found to be < 10 ng/ml, corresponding to a Specific Activity of 100,000IU/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, MGC9721.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-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 Interleukin-15 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-Asn-Trp-Ile-Asp.

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

Description:

Interleukin-12 Mouse Recombinant

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

Product # :

CYT-144

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Description

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

Source

HEK-293 Cells.

Formulation

The protein was lyophilized from 0.5xPBS, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

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

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

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

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

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

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

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

Who supplies recombinant IL12 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL12 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-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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Shipped with Ice Packs

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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 Human 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-159

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Description

IL36B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.7kDa.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 human IL-1 Rrp2 Fc Chimera.

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Introduction
Human 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. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner.
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 Human 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
MNPQREAAPK SYAIRDSRQM VWVLSGNSLI AAPLSRSIKP VTLHLIACRD TEFSDKEKGN MVYLGIKGKD LCLFCAEIQG KPTLQLKEKN IMDLYVEKKA QKPFLFFHNK EGSTSVFQSV SYPGWFIATS TTSGQPIFLT KERGITNNTN FYLDSVE

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

Description:

Interleukin-17A/F Heterodimer Rat Recombinant

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

Product # :

CYT-677

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Quantity :

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
Rat IL-17A/F is a glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Rat IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Rat IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat IL-17A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL-17A/F should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Rat IL-17A/F in sterile water not more than 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IL-17A: MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.
IL-17F: MARRNPKVGL SALQKAGNCP PLEDNSVRVD IRIFNQNQGI SVPRDFQNRS SSPWDYNITR DPDRFPSEIA EAQCRHSGCI NAQGQEDGSM NSVPIQQEIL VLRREPQGCS NSFRLEKMLI KVGCTCVTPI VHHAA.

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

Description:

Interleukin-36 Gamma Human Recombinant

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

Product # :

CYT-160

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Quantity :

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and IL-1F10. ). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.
Synonyms
Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36g Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRGTPGDADG GGRAVYQSMC KPITGTINDL NQQVWTLQGQ NLVAVPRSDS VTPVTVAVIT CKYPEALEQG RGDPIYLGIQ NPEMCLYCEK VGEQPTLQLK EQKIMDLYGQ PEPVKPFLFY RAKTGRTSTL ESVAFPDWFI ASSKRDQPII LTSELGKSYN TAFELNIND

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

Description:

Interleukin-3 Rhesus Macaque Recombinant

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

Product # :

CYT-156

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL 3 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a molecular mass of 14.0kDa.The IL 3 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human
TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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 IL-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.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ
Background
What is the molecular weight/Mw of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein has a total Mw of 14kDa.

What is the source or expression system of IL 3 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of IL 3 RHESUS MACAQUE Protein?
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ.

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

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

Who supplies recombinant IL 3 RHESUS MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 RHESUS MACAQUE?
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 Rat Recombinant

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

Product # :

CYT-383

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-3 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids and having a molecular mass of 16.3kDa. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-3 Rat was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 10⁵ units/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 IL3 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
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.
Background
What is the molecular weight/Mw of IL 3 RAT Protein?
IL 3 RAT Protein has a total Mw of 16.3kDa.

What is the source or expression system of IL 3 RAT Protein?
Escherichia Coli.

What is the Purity of IL 3 RAT Protein?
IL 3 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RAT Protein?
The ED50 as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 105 units/mg.

What is the amino acid sequence of IL 3 RAT Protein?
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.

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

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

Who supplies recombinant IL 3 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 3 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:

Flt3 Ligand Porcine Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-1041

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
Background
What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

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

What is the Purity of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

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

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

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

Description:

Uteroglobin Human Recombinant

Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

Product # :

CYT-743

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Uteroglobin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 15.8kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

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 ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

More Info

Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

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:

Interferon-gamma Recombinant Rhesus Macaque

Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-1122

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interferon-gamma Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 142 amino acid and having a molecular mass of approximately 16.8kDa.IFNG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

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 an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

More Info

Introduction
IFN-gamma produced by lymphocytes activated by specific antigens / mitogens.
IFN-gamma, on top of having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-gamma Rhesus Macaque 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 Interferon-gamma Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
Background
What is the molecular weight/Mw of IFNG MONKEY Protein?
IFNG MONKEY Protein has a total Mw of 16.8kDa.

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

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

What is the Biological Activity of IFNG MONKEY Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

What is the amino acid sequence of IFNG MONKEY Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.

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

What is the endotoxin level for IFNG MONKEY Protein?
The endotoxin level is minimal, IFNG MONKEY 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-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.

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
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-2 Human Recombinant, His Tag

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

Product # :

CYT-666

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-2 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-2 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

Purity

Greater than 90.0% as determined by 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
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.
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 molecular weight/Mw of IL 2 HUMAN, HIS Protein?
IL 2 HUMAN, HIS Protein has a total Mw of 20kDa.

What is the source or expression system of IL 2 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL 2 HUMAN, HIS Protein?
IL 2 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN, HIS Protein?
The biological functionality of IL 2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL 2 HUMAN, HIS Protein?
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

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

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

Who supplies recombinant IL 2 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 IL 2 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:

IFN-alpha 7 Human Recombinant

IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

Product # :

CYT-196

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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SDS-PAGE
Citations

Description

IFNA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a) and having a molecular mass of 22.3kDa.IFNA7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IFNA7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IFN alpha 7 (IFNA7) is a member of the alpha/beta IFN family. IFNA7 is generated by macrophages. IFN-alpha has antiviral functions. IFN promotes the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.
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 MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
Background
What is the molecular weight/Mw of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein has a total Mw of 22.3kDa.

What is the source or expression system of IFNA7 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA7 HUMAN Protein?
The biological functionality of IFNA7 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNA7 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
What applications can IFNA7 HUMAN Protein be used in?
IFNA7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA7 HUMAN Protein?
The endotoxin level is minimal, IFNA7 HUMAN Protein was purified using conventional chromatography techniques.

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Description:

Interleukin 17B Human Recombinant

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

Product # :

CYT-771

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Shipped at Room temp

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Description

Interleukin-17B Human Recombinant produced in E.Coli is a homodimeric, non-disulfide-linked polypeptide chain containing a total of 322 amino acids (2 chains of 161aa) and having a molecular mass of 36.5kDa. The IL-17B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-17B was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 0.05% Tween-20 and 3%Trehalose.

Purity

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

Biological Activity

The ED50 as determined by inducing IL-8 secretion of human HepG2 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000 IU/mg.

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Introduction
IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.
Synonyms
Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 17B although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution IL17B should be stored at 4C between 2-7 days and for future use below -18C. 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 17B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQPRSPKSKR KGQGRPGPLA PGPHQVPLDL VSRMKPYARM EEYERNIEEM VAQLRNSSEL AQRKCEVNLQ LWMSNKRSLS PWGYSINHDP SRIPVDLPEA RCLCLGCVNP FTMQEDRSMV SVPVFSQVPV RRRLCPPPPR TGPCRQRAVM ETIAVGCTCI F.

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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