Search: 1000 results found for "Other Cytokines"

Description:

Interleukin-36 Receptor Antagonist Human Recombinant, His Tag

Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.

Product # :

CYT-844

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Description

IL36RN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-155 a.a) and having a molecular mass of 19.1kDa.IL36RN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL36RN protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.
Synonyms
Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.
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 MVLSGALCFR MKDSALKVLY LHNNQLLAGG LHAGKVIKGE EISVVPNRWL DASLSPVILG VQGGSQCLSC GVGQEPTLTL EPVNIMELYL GAKESKSFTF YRRDMGLTSS FESAAYPGWF LCTVPEADQP VRLTQLPENG GWNAPITDFY FQQCD.

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:

sFas Receptor Human Recombinant, Sf9

Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.

Product # :

CYT-1153

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Description

FAS Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 156 amino acids (26-173 aa) and having a molecular mass of 17.7KDa.FAS is fused to a 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FAS protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
FAS or tumor necrosis factor receptor superfamily member 6 or TNFRSF6, is part of the death receptor family, which is part of the TNF receptor protein family. TNFRSF6 has a crucial part in regulating viral infections. FAS protein can be found in almost all cell types, when its cognate ligand (FasL) can be found in activated T cells, NK cells & dendritic cells. The regulating protein of FasL & TRAIL on HCMV-infected dendritic enhances direct destruction of activated T lymphocytes. furthermore, subvertneutrophil function in HCMV retinitis can occur when FasL is activated in HCMV infected retinal pigment epithelial cells.
Synonyms
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
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
QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRSNLE HHHHHH
Background
What is the molecular weight/Mw of FAS Protein?
FAS Protein has a total Mw of 17.7kDa.

What is the source or expression system of FAS Protein?
Sf9, Baculovirus cells

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

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

What is the amino acid sequence of FAS Protein?
QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRSNLE HHHHHH

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

What is the endotoxin level for FAS Protein?
The endotoxin level is minimal, FAS 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-13 Human Recombinant, His Tag

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

Product # :

CYT-489

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Description

Interleukin-13 His Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (21-132) having a molecular weight of 12.84kDa with a 4kDa amino-terminal hexahistidine tag (total weight of 16.84kDa). The IL-13 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin -13 His-Tag protein is supplied in 25mM Na-Acetate (pH 4.8) and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin-13 is a pleiotropic regulatory cytokine, which shares many of the properties of Interleukin-4. IL-13 is produced primarily by activated T lymphocytes and acts via specific cell surface receptor complexes. Its biological activities include the stimulation of B-cell proliferation and differentiation and the regulation of inflammatory and immune responses.
Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
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 IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein has a total Mw of 12.8kDa.

What is the source or expression system of IL13 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 HUMAN, HIS Protein?
The biological functionality of IL13 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is composed from 112 amino acids.

What applications can IL13 HUMAN, HIS Protein be used in?
IL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 HUMAN, HIS Protein?
The endotoxin level is minimal, IL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 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 IL13 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-4 Human Recombinant, His Tag

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

Product # :

CYT-483

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Description

Interleukin-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-4 His-Tag is supplied in 20mM Tris-HCl and10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

SDS-PAGE

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Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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 MHKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Recombinant IL-4 (Interleukin-4) is a bioengineered version of a naturally occurring cytokine, which plays a crucial role in the immune system. IL-4 is primarily produced by activated T cells, mast cells, and basophils, and it is involved in the regulation of immune responses, including the differentiation of T helper cells, B cell activation, and the production of immunoglobulins.Recombinant IL-4 is synthesized using recombinant DNA technology, which involves inserting the gene encoding IL-4 into a suitable expression system, such as bacteria, yeast, or mammalian cells. The host cells are then cultured, allowing them to produce the desired protein, which can be purified and used for various applications.One of the main functions of IL-4 is to promote the differentiation of naïve CD4+ T cells into T helper 2 (Th2) cells. Th2 cells are essential for coordinating immune responses against extracellular pathogens, such as parasites and allergens. They achieve this by secreting cytokines, including IL-4 itself, IL-5, and IL-13, which stimulate B cells to produce specific antibodies, eosinophils to combat parasites, and mast cells to release histamine and other inflammatory mediators.Recombinant IL-4 has been extensively studied for its potential therapeutic applications. It has been shown to have anti-inflammatory properties, making it a potential candidate for the treatment of autoimmune and inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and inflammatory bowel disease. Additionally, IL-4 has been found to inhibit the growth of certain cancer cells, suggesting that it may have potential as an anti-cancer agent.However, the use of recombinant IL-4 as a therapeutic agent is not without challenges. One of the main concerns is the potential for adverse effects due to its immunomodulatory properties. For example, excessive IL-4 activity can lead to the development of allergies and asthma, as it promotes the production

What is the molecular weight/Mw of IL 4 HUMAN, HIS Protein?
IL 4 HUMAN, HIS Protein has a total Mw of 17.2kDa.

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

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

What is the Biological Activity of IL 4 HUMAN, HIS Protein?
The ED50 for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

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

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

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

Who supplies recombinant IL 4 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 4 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:

Trefoil Factor-1 Human Recombinant

TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

Product # :

CYT-586

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Shipped at Room temp

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Description

TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.

Purity

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

Biological Activity

The ED₅₀ as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

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Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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 TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
PNTIDVPPEEECEF.

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:

Thrombopoietin Human Recombinant, CHO

MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.

Product # :

CYT-1070

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Shipped with Ice Packs

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Description

Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation. The TPO is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells.

Formulation

TPO protein solution contains phosphate buffered saline (pH7.4) and 2% albumin.

Purity

Greater than 98% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of MO7e cells corresponding to a specific activity of 3x10⁵ units/mg.

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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.
Synonyms
MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.
Physical Appearance
Sterile Filtered clear solution.
Stability
Thrombopoietin although stable at room temperature for 1 week, should be stored between 2-8°C.

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 Receptor Human Recombinant

Interleukin 4 Receptor, IL-4 Receptor Subunit Alpha, Interleukin 13 Receptor, IL-4RA, IL4RA, Interleukin-4 Receptor Subunit Alpha, Interleukin-4 Receptor Alpha Chain, IL4R Nirs Variant 1, IL-4R Subunit Alpha, CD124 Antigen, IL-4R-Alpha, CD124, IL4R.

Product # :

CYT-1047

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Description

IL4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (26-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 215 amino acids and having a molecular mass of 24.7kDa.IL4R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL4R protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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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
Interleukin 4 Receptor, IL-4 Receptor Subunit Alpha, Interleukin 13 Receptor, IL-4RA, IL4RA, Interleukin-4 Receptor Subunit Alpha, Interleukin-4 Receptor Alpha Chain, IL4R Nirs Variant 1, IL-4R Subunit Alpha, CD124 Antigen, IL-4R-Alpha, CD124, IL4R.
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
MKVLQEPTCV SDYMSISTCE WKMNGPTNCS TELRLLYQLV FLLSEAHTCI PENNGGAGCV CHLLMDDVVS ADNYTLDLWA GQQLLWKGSF KPSEHVKPRA PGNLTVHTNV SDTLLLTWSN PYPPDNYLYN HLTYAVNIWS ENDPADFRIY NVTYLEPSLR IAASTLKSGI SYRARVRAWA
QCYNTTWSEW SPSTKWHNSY REPFEQHLEH HHHHH
Background
What is the molecular weight/Mw of IL 4R HUMAN Protein?
IL 4R HUMAN Protein has a total Mw of 24.7kDa.

What is the source or expression system of IL 4R HUMAN Protein?
Sf9, Baculovirus cells.

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

What is the Biological Activity of IL 4R HUMAN Protein?
The biological functionality of IL 4R HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 4R HUMAN Protein?
MKVLQEPTCV SDYMSISTCE WKMNGPTNCS TELRLLYQLV FLLSEAHTCI PENNGGAGCV CHLLMDDVVS ADNYTLDLWA GQQLLWKGSF KPSEHVKPRA PGNLTVHTNV SDTLLLTWSN PYPPDNYLYN HLTYAVNIWS ENDPADFRIY NVTYLEPSLR IAASTLKSGI SYRARVRAWA
QCYNTTWSEW SPSTKWHNSY REPFEQHLEH HHHHH.

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

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

Who supplies recombinant IL 4R HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 4R HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-1 alpha Human Recombinant, His Tag

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

Product # :

CYT-479

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Quantity :

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Shipped with Ice Packs

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Description

IL-1A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids fragment (113-271) with an amino-terminal hexahistidine tag and having a total molecular mass of 22.5kDa. The Interleukin-1 alpha His-tag is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1 alpha His-tag protein is supplied in 1x PBS and 50% glycerol.

Purity

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

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced by inflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered 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 IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein has a total Mw of 22.5kDa.

What is the source or expression system of IL1A HUMAN, HIS Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein is composed from 159 amino acids.

What applications can IL1A HUMAN, HIS Protein be used in?
IL1A HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A HUMAN, HIS Protein?
The endotoxin level is minimal, IL1A 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:

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag

Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

Product # :

CYT-900

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Shipped with Ice Packs

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Description

TNF a Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235a.a.) and having a molecular mass of 19.9kDa.TNF a is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF a protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

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

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

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

Description:

Interleukin-1 alpha Human Recombinant, HEK

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

Product # :

CYT-964

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Description

Interleukin-1 alpha Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 18kDa due to glycosylation.The IL1A is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The IL-1A protein was lyophilized from a 0.2µm filtered solution of PBS pH 7.4 with 10% trehalose as protectant.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x10⁹ unit/mg.

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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL1A in deionized water to a stock solution of 0.5mg/ml.
Background
What is the molecular weight/Mw of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein has a total Mw of 18kDa.

What is the source or expression system of IL1A HUMAN, HEK Protein?
HEK.
What is the Purity of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN, HEK Protein?
Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.

What applications can IL1A HUMAN, HEK Protein be used in?
IL1A HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A HUMAN, HEK Protein?
The endotoxin level is minimal, IL1A HUMAN, HEK 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-15 Human Recombinant, His Tag

IL-15, MGC9721.

Product # :

CYT-490

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Description

Interleukin-15 His Human Recombinant ?produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 123 amino acids fragment (49-162) having a total molecular weight of 13.9 kDa with an C-terminal hexahistidine tag. The IL-15 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-15 His is supplied in 20mM Tris-HCl buffer (pH 8.0) 0.2mM PMSF and 10% glycerol.

Purity

Greater than 95.0% 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 < 2.5ng/ml, corresponding to a Specific Activity of 400,000units/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 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
MNWVNVISDL KKIEDLIQSM HIDATLYTES DVHPSCKVTA MKCFLLELQV ISLESGDASI HDTVENLIIL ANNSLSSNGN VTESGCKECE ELEEKNIKEF LQSFVHIVQM FINTSLEHHH HHH.

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:

Resistin Mutant Human Recombinant

Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Product # :

CYT-585

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Description

9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

Source

Escherichia Coli.

Formulation

Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

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, His Tag

9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.

Product # :

CYT-847

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Description

IL33 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (109-266 a.a) and having a molecular mass of 18.1kDa.IL33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL33 protein solution (0.5mg/ml) containing Phosphate buffered saline,10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED₅₀ for this effect is ≤ 0.1ng/ml.

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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
9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.
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 MGSSIQGTSL LTQSPASLST YNDQSVSFVL ENGCYVINVD DSGKDQEQDQ VLLRYYESPC PASQSGDGVD GKKLMVNMSP IKDTDIWLHA NDKDYSVELQ RGDVSPPEQA FFVLHKKSSD FVSFECKNLP GTYIGVKDNQ LALVEEKDES CNNIMFKLSK I.

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:

Bone Morphogenetic protein-8b, Mouse Anti Human

Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

Product # :

ANT-558

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human BMP8B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human BMP8B protein 264-402 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT13E6AT.
Applications
BMP8B antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
BMP8B antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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:

Clusterin, Mouse Anti Human

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

Product # :

ANT-314

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol & 0.02% Sodium Azide.

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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified. The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the ? and ? chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil ? -helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen. It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, b
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human Clusterin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Clusterin amino acids 1-333 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P1A11AT.
Applications
Clusterin antibody has been tested by ELISA, Western blot, ICC/IF, IHC and FACS analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Clusterin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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:

Tumor Necrosis Factor-Beta Human Recombinant

Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

Product # :

CYT-224

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Description

Tumor Necrosis Factor-b Human Recombinant (Lymphotoxin) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 18645 Dalton. The TNF-b is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized protein with no additives.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-b 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 Tumor Necrosis Factor-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.082 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 calibrated solution of TNF-b 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:

RELM-Beta Human Recombinant, His Tag

Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

Product # :

CYT-454

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Description

RELM-beta Human Recombinant is a His-Tagged Fusion Protein which is 11 kDa protein containing 90 amino acid residues of the RELM-beta human and 12 additional amino acid residues - HisTag (underlined).

Source

Escherichia Coli.

Formulation

Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MGSTQCSLDS VMDKKIKDVL NSLEYSPSPI SKKLSCASVK SQGRPSSCPA GMAVTGCACG YGCGSWDVQLETTCHCQCSV VDWTTARCCH LTKLRSHHHH HH.

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

Description:

Interleukin 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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SDS-PAGE
Citations

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-4 Human Recombinant

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

Product # :

CYT-211

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Shipping Method :

Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Everything You Should Know About IL-4 Human Recombinant
Interleukin-4 (IL-4) is an important type-2 cytokine with multiple effects on numerous cells and tissues in the body. As such, it's crucial for the immune system's maintenance and function.
Recent advancements have led to the development of interleukin-4 (rhIL-4) human recombinant in laboratories. As a result, experts have started studying its potential uses and therapeutic applications.
If you're interested in learning more about IL-4 human recombinant, check out the information below!
How Does Interleukin-4 (IL-4) Work?
Interleukin-4 (IL-4) acts as a signaling molecule, specifically a protein. It communicates with various immune cells by binding to specific receptors on their surface.
This process triggers responses against common threats, such as allergens, contaminants, and infections.
IL-4 is produced by T helper 2 (Th2) cells (a type of white blood cells), mast cells, eosinophils, and basophils.
What Interleukin-4 (IL-4) Does
As mentioned, this type-2 cytokine has multiple effects on various cells and tissues, so it fulfills several functions. Below are the most important ones:
- Th2 cell differentiation: IL-4 promotes the differentiation of T cells, triggering the response of Th2 cells, which fight parasites and regulate allergic responses.
- B cell activation and antibody production: IL-4 stimulates B cells, helping them proliferate and produce antibodies, particularly immunoglobulin E (IgE), which is involved in allergic reactions.
- Inflammation reduction: IL-4 can promote inflammation to address threats, such as allergens or parasites, and suppress it when necessary, depending on the context.
- Tissue repair and remodeling: IL-4 is key for tissue repair and remodeling processes, such as wound healing and fibrosis.
What Is IL-4 Human Recombinant?
IL-4 human recombinant is a version produced in a laboratory using DNA technology. The cytokine is inserted into a host organism, commonly E. Coli bacteria, for mass production.
This method allows experts to obtain pure and contaminant-free rhIL-4 with uniform biological activity and in large quantities.
What Can IL-4 Human Recombinant Be Used For?
Since this cytokine plays a key role in different processes, it may have multiple therapeutic applications for numerous diseases. These are the most common:
- Allergic diseases, such as asthma, rhinitis, and eczema
- Autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis
- Infectious diseases, including those caused by parasites and viruses
- Cancer, as research suggests IL-4 could enhance the immune system's ability to fight cancer cells
Final Thoughts
The future of IL-4 human recombinant seems promising. This laboratory-produced version of an essential type-2 cytokine may be key to developing innovative therapies. However, more research is needed on potential applications to determine if it's safe and effectiv.
What is the molecular weight/Mw of IL 4 HUMAN Protein?
IL 4 HUMAN Protein has a total Mw of 15kDa.

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

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

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

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

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

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

Who supplies recombinant IL 4 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 4 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.594 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-4 as a Reference Standard.

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

Description:

IFN Regulatory Factor-1 Human Recombinant

IRF-1, IRF1, MAR.

Product # :

CYT-449

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Description

IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
Synonyms
IRF-1, IRF1, MAR.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored 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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.

What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.

What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 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:

Adiponectin glycosylated Human Recombinant, HMW Rich

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-764

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

Source

HEK293.

Formulation

Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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-7 Receptor Human Recombinant

IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.

Product # :

CYT-1046

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL7R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (21-239a.a.) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IL7R is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL7R protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interleukin-7 receptor (IL7R) ,is a hematopoietin receptor superfamily member. IL7R takes a vital part in lymphocyte differentiation, proliferation, multiple sclerosis, as well as survival. IL7R protein signaling is vital for T-cell development and regulation of native and memory T-cell homeostasis. Likewise, IL7R is critically needed for the proper function & development of lymphoid cells.
Synonyms
IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.
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
ADLESGYAQN GDLEDAELDD YSFSCYSQLE VNGSQHSLTC AFEDPDVNIT NLEFEICGAL VEVKCLNFRK LQEIYFIETK KFLLIGKSNI CVKVGEKSLT CKKIDLTTIV KPEAPFDLSV VYREGANDFV VTFNTSHLQK KYVKVLMHDV AYRQEKDENK WTHVNLSSTK LTLLQRKLQP AAMYEIKVRS IPDHYFKGFW SEWSPSYYFR TPEINNSSGE MDLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H
Background
What is the molecular weight/Mw of IL7R HUMAN Protein?
IL7R HUMAN Protein has a total Mw of 52.5kDa.

What is the source or expression system of IL7R HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL7R HUMAN Protein?
IL7R HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7R HUMAN Protein?
The biological functionality of IL7R HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL7R HUMAN Protein?
ADLESGYAQN GDLEDAELDD YSFSCYSQLE VNGSQHSLTC AFEDPDVNIT NLEFEICGAL VEVKCLNFRK LQEIYFIETK KFLLIGKSNI CVKVGEKSLT CKKIDLTTIV KPEAPFDLSV VYREGANDFV VTFNTSHLQK KYVKVLMHDV AYRQEKDENK WTHVNLSSTK LTLLQRKLQP AAMYEIKVRS IPDHYFKGFW SEWSPSYYFR TPEINNSSGE MDLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

What applications can IL7R HUMAN Protein be used in?
IL7R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7R HUMAN Protein?
The endotoxin level is minimal, IL7R HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7R 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 IL7R 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:

Desert HedgeHog (C23II) Human Recombinant, His Tag

HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

Product # :

CYT-763

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Shipped with Ice Packs

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Description

DHH (C23II) His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (23-198) and having a molecular mass of 22.4kDa.DHH (C23II) His is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DHH (C23II) His solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
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 MGSMIIGPGR GPVGRRRYAR KQLVPLLYKQ FVPGVPERTL GASGPAEGRV ARGSERFRDL VPNYNPDIIF KDEENSGADR LMTERCKERV NALAIAVMNM WPGVRLRVTE GWDEDGHHAQ DSLHYEGRAL DITTSDRDRN KYGLLARLAV EAGFDWVYYE SRNHVHVSVK ADNSLAVRAG G

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

Description:

Interleukin-3 Receptor Subunit Alpha Mouse Recombinant

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

Product # :

CYT-1210

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL3RA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-331 a.a.) and fused to a 231 a.a. Human IgG His Tag at C-terminus containing a total of 554 amino acids and having a molecular mass of 61.5 kDa.

Source

Sf9, Baculovirus cells.

Formulation

IL3RA protein solution (0.25mg/ml) contains 20mM Tris-HCL, 30% glycerol & 0.1M NaCl (pH-8).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH
Background
What is the molecular weight/Mw of IL 3 RA MOUSE Protein?
IL 3 RA MOUSE Protein has a total Mw of 61.5kDa.

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

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

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

What is the amino acid sequence of IL 3 RA MOUSE Protein?
SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

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

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

Who supplies recombinant IL 3 RA 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 IL 3 RA 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.

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