Search: 1000 results found for "other cytokines"

Description:

BD 4 Rat

Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

Product # :

CYT-066

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Shipped at Room temp

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Description

BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-4 protein was 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

Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

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Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.
Synonyms
Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BD-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-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 BD-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
Background
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 4.4kDa.

What is the source or expression system of BD4 Protein?
Escherichia Coli.

What is the Purity of BD4 Protein?
BD4 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BD4 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

What is the amino acid sequence of BD4 Protein?
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 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 Binding Protein Human Recombinant

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

Product # :

CYT-728

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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

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

Description:

Interleukin-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

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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.

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Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
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.

Description:

Interleukin-2 Human Recombinant

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

Product # :

CYT-209

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Shipped at Room temp

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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x10⁷IU/mg.

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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
T-cell growth factor (TCGF), Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
Background
IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research
IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.
By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.
Production and Characteristics
Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.
The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.
Reconstituting IL-2 Human for Laboratory Use
To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.
Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.
Storage and Stability
The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.
Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.
Purity and Biological Activity
IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.
Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.
Applications in Research
IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.
Important Considerations
It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.
Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.
What is the molecular weight/Mw of IL 2 HUMAN Protein?
IL 2 HUMAN Protein has a total Mw of 15.4kDa.

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

What is the Purity of IL 2 HUMAN Protein?
IL 2 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

What is the amino acid sequence of IL 2 HUMAN Protein?
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

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

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

Who supplies recombinant IL 2 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 2 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin 12 Receptor Beta 1 Human Recombinant

Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.

Product # :

CYT-862

Price :

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Shipping Method :

Shipped with Ice Packs

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Description

IL12RB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 568 amino acids (1-545 a.a) and having a molecular mass of 62.6kDa. IL12RB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL12RB1 protein solution (0.25mg/ml) containing 20mM TRIS 8.0 buffer and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFN gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.
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 MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.
Background
What is the molecular weight/Mw of IL12RB1 HUMAN Protein?
IL12RB1 HUMAN Protein has a total Mw of 62.6kDa.

What is the source or expression system of IL12RB1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL12RB1 HUMAN Protein?
IL12RB1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12RB1 HUMAN Protein?
The biological functionality of IL12RB1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL12RB1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.
What applications can IL12RB1 HUMAN Protein be used in?
IL12RB1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12RB1 HUMAN Protein?
The endotoxin level is minimal, IL12RB1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12RB1 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 IL12RB1 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 13 Receptor, Alpha 2 Human Recombinant

CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

Product # :

CYT-757

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

IL13RA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (27-343 a.a.) and having a molecular mass of 39.5kDa.IL13RA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL13RA2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.
Synonyms
CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.
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 MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.
Background
What is the molecular weight/Mw of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein has a total Mw of 39.5kDa.

What is the source or expression system of IL13RA2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13RA2 HUMAN Protein?
The biological functionality of IL13RA2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL13RA2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.

What applications can IL13RA2 HUMAN Protein be used in?
IL13RA2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13RA2 HUMAN Protein?
The endotoxin level is minimal, IL13RA2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13RA2 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 IL13RA2 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-2 Receptor alpha Human Recombinant, sf9

Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

Product # :

CYT-1020

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Description

IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RA 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.

More Info

Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.
Synonyms
Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.
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
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK 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 CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein has a total Mw of 52.1kDa.

What is the source or expression system of CD25 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD25 HUMAN, SF9 Protein?
The biological functionality of CD25 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CD25 HUMAN, SF9 Protein?
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK 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 CD25 HUMAN, SF9 Protein be used in?
CD25 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD25 HUMAN, SF9 Protein?
The endotoxin level is minimal, CD25 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CD25 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CD25 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Flt3 Ligand Mouse Recombinant

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

Product # :

CYT-340

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Shipped at Room temp

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biological activity
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Description

Flt3-Ligand Mouse Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 163 amino acids and having a molecular mass of 18.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FLT3L Mouse protein was lyophilized from sterile filtered solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x10⁵ units/mg.

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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 Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt-3 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 Flt3l Mouse recombinant in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein has a total Mw of 18.6kDa.

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

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

What is the Biological Activity of FLT3 LIGAND MOUSE Protein?
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.

What is the amino acid sequence of FLT3 LIGAND MOUSE Protein?
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.

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

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

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

Description:

Interleukin-33 Human Recombinant, His Tag

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.

Product # :

CYT-667

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Shipped with Ice Packs

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Description

Interleukin-33 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 159 amino acids C-terminal fragment (112-270) having a molecular weight of 22.49kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-33 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-33 protein solution is supplied in 10mM Tris-HCl pH 8.0, 180mM NaCl and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.
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-1 beta Mouse Recombinant, His Tag

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

Product # :

CYT-578

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Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 189 amino acids and having a molecular mass of 21 kDa. The IL-1b is fused to His-Tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL-1B protein contains 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1b is an inflammatory cytokine which modulates angiogenesis by interacting directly with vascular endothelial cells & increasing the production of proangiogenic factors through paracrine control. IL-1 beta stimulates endothelial cell migration and proliferation, adhesion-molecule expression, inflammatory mediator production, and leukocyte recruitment. IL1B is essential for tumor growth, metastasis, and angiogenesis in quite a few animal models.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta, Interleukin-1 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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.
Background
What is the molecular weight/Mw of IL1B MOUSE, HIS Protein?
IL1B MOUSE, HIS Protein has a total Mw of 21kDa.

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

What is the Purity of IL1B MOUSE, HIS Protein?
IL1B MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of IL1B MOUSE, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

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

What is the endotoxin level for IL1B MOUSE, HIS Protein?
The endotoxin level is minimal, IL1B MOUSE, 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:

Granulocyte Macrophage Colony Stimulating Factor, Mouse Anti-Human

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Product # :

ANT-129

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human GM-CSF.
Ig Subclass
Mouse IgG.
Clone
NYRhGMCSF.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange Protein concentration1mg/ml in PBS (after reconstitution).

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:

Lymphotactin Human Recombinant (XCL1), His Tag

XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

Product # :

CHM-357

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

XCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 114 amino acids (22-114 a.a.) and having a molecular mass of 12.5 kDa. The XCL1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Recombinant XCL1 contains 20mM Tris buffer pH-8, 200mM NaCl, 2mM DTT and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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 MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.
Background
What is the molecular weight/Mw of LYMPHOTACTIN HUMAN, HIS Protein?
LYMPHOTACTIN HUMAN, HIS Protein has a total Mw of 12.5kDa.

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

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

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

What is the amino acid sequence of LYMPHOTACTIN HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.

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

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

Who supplies recombinant LYMPHOTACTIN 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 LYMPHOTACTIN 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-2 alpha Soluble Receptor Human Recombinant

CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.

Product # :

CYT-285

Price :

Quantity :

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Shipped with Ice Packs

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source
formulation
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Description

Interleukin-2R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (22-213) corresponding to the mature IL2-R protein with an amino terminal hexahistidine tag.The IL-2R is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-2R His-Tag protein is supplied in 1x PBS and 50% glycerol pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.
Synonyms
CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.
Physical Appearance
Sterile colorless liquid formulation.
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 CD25 HUMAN Protein?
Escherichia Coli.

What is the Purity of CD25 HUMAN Protein?
CD25 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD25 HUMAN Protein?
The biological functionality of CD25 HUMAN Protein will be determined in the future.

What is the amino acid sequence of CD25 HUMAN Protein?
CD25 HUMAN Protein is composed from 192 amino acids.

What applications can CD25 HUMAN Protein be used in?
CD25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD25 HUMAN Protein?
The endotoxin level is minimal, CD25 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CD25 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 CD25 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 13 Receptor Alpha 1 Human Recombinant

CD213A1, IL-13Ra, NR404235, Interleukin-13 receptor subunit alpha-1,IL-13R subunit alpha-1, IL-13R-alpha-1, IL-13RA1, Cancer/testis antigen 19, Cancer/testis antigen 19.

Product # :

CYT-829

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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SDS-PAGE
Citations

Description

IL13RA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (22-343 a.a) and having a molecular mass of 37.7kDa (Migrates at 40-57kDa on SDS–PAGE under reducing conditions).IL13RA1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL13RA1 protein solution (0.5mg/ml) in Phosphate buffer saline (pH 7.4).

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interleukin-13 receptor subunit alpha-1 (IL13RA1) is a subunit of the interleukin 13 receptor. The IL13RA1 subunit forms a receptor complex with IL4 receptor alpha, which is a subunit shared by IL13 and IL4 receptors. IL13RA1 binds tyrosine kinase TYK2, and thus may mediate the signaling processes which leads to the activation of JAK1, STAT3 and STAT6 induced by IL13 and IL4. IL13RA1 is vital for allergen-induced airway hyperactivity and mucus hypersecretion.
Synonyms
CD213A1, IL-13Ra, NR404235, Interleukin-13 receptor subunit alpha-1,IL-13R subunit alpha-1, IL-13R-alpha-1, IL-13RA1, Cancer/testis antigen 19, Cancer/testis antigen 19.
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
GGGGAAPTET QPPVTNLSVS VENLCTVIWT WNPPEGASSN CSLWYFSHFG DKQDKKIAPE TRRSIEVPLN ERICLQVGSQ CSTNESEKPS ILVEKCISPP EGDPESAVTE LQCIWHNLSY MKCSWLPGRN TSPDTNYTLY YWHRSLEKIH QCENIFREGQ YFGCSFDLTK VKDSSFEQHS VQIMVKDNAG KIKPSFNIVP LTSRVKPDPP HIKNLSFHND DLYVQWENPQ NFISRCLFYE VEVNNSQTET HNVFYVQEAK CENPEFERNV ENTSCFMVPG VLPDTLNTVR IRVKTNKLCY EDDKLWSNWS QEMSIGKKRN STHHHHHH.
Background
What is the molecular weight/Mw of IL13RA1 HUMAN Protein?
IL13RA1 HUMAN Protein has a total Mw of 37.7kDa.

What is the source or expression system of IL13RA1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL13RA1 HUMAN Protein?
IL13RA1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13RA1 HUMAN Protein?
The biological functionality of IL13RA1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL13RA1 HUMAN Protein?
GGGGAAPTET QPPVTNLSVS VENLCTVIWT WNPPEGASSN CSLWYFSHFG DKQDKKIAPE TRRSIEVPLN ERICLQVGSQ CSTNESEKPS ILVEKCISPP EGDPESAVTE LQCIWHNLSY MKCSWLPGRN TSPDTNYTLY YWHRSLEKIH QCENIFREGQ YFGCSFDLTK VKDSSFEQHS VQIMVKDNAG KIKPSFNIVP LTSRVKPDPP HIKNLSFHND DLYVQWENPQ NFISRCLFYE VEVNNSQTET HNVFYVQEAK CENPEFERNV ENTSCFMVPG VLPDTLNTVR IRVKTNKLCY EDDKLWSNWS QEMSIGKKRN STHHHHHH.

What applications can IL13RA1 HUMAN Protein be used in?
IL13RA1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13RA1 HUMAN Protein?
The endotoxin level is minimal, IL13RA1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13RA1 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 IL13RA1 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 10 Receptor Alpha Human Recombinant, BioActive

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

Product # :

CYT-1142

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Quantity :

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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein has a total Mw of 25.2kDa.

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

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

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

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

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

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

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

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

Description:

RELM-Gamma Mouse Recombinant, His Tag

Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

Product # :

CYT-455

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) 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-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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.The lyophilized protein remains stable until the expiry date when stored at -20°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.

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 Receptor 2 Fusion Protein Human Recombinant

Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-422

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Description

Recombinant Human Tumor Necrosis Factor Receptor 2 Fusion Protein produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of the extracellular ligand-binding portion of the human 75 kilo Dalton (p75) tumor necrosis factor receptor 2 (TNFR2) linked to the Fc portion of human IgG1. The Fc component of TNFR2 contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. It consists of 934 amino acids and has an apparent molecular weight of approximately 150 kilo Daltons.The TNFR2 is purified by standard chromatographic techniques.

Source

Chinese Hamster Ovarian Cells (CHO).

Formulation

Each mg contains 1.6mg mannitol, 0.4 mg sucrose and 48 µg tromethamine.

Purity

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

Biological Activity

Potency is determined by its ability to neutralize TNF-alpha mediated growth inhibition of A375 cells, corresponding to a Specific Activity of 17,000,000 IU/mg.

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Introduction
TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules.
It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF? and TNF? (lymphotoxin alpha [LT?]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement.
TNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).
Synonyms
Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFR2 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 TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

IFN-Alpha 2a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.

Product # :

CYT-204

Price :

Quantity :

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Shipped at Room temp

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Description

IFN Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine.The Interferon-alpha-2a gene was obtained from human leukocytes.The IFNA2A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without additives.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

More Info

Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNA-2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha-2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein has a total Mw of 19.2kDa.

What is the source or expression system of IFN A 2A HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2A HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

What is the amino acid sequence of IFN A 2A HUMAN Protein?
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.

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

What is the endotoxin level for IFN A 2A HUMAN Protein?
The endotoxin level is minimal, IFN A 2A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 IFN-a 2a as a Reference Standard.

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

Description:

Interleukin-22 Receptor Antagonist (Y51A), PEG Mouse Recombinant

Product # :

CYT-1248

Price :

Quantity :

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Shipped at Room temp

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Description

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

Source

Escherichia coli.

Formulation

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

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

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

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

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

Description:

Rantes Human Recombinant (CCL5), His Tag

Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

Product # :

CHM-361

Price :

Quantity :

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Description

Rantes Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 68 amino acids fragment (24-91) having a total molecular mass of 17.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.The Rantes His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Rantes His-Tag protein is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.
Synonyms
Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.
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 CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein has a total Mw of 17.5kDa.

What is the source or expression system of CCL5 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL5 HUMAN, HIS Protein?
The biological functionality of CCL5 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein is composed from 68 amino acids.

What applications can CCL5 HUMAN, HIS Protein be used in?
CCL5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL5 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL5 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL5 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 CCL5 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:

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

Price :

Quantity :

Shipping Method :

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:

Cardiotrophin-1 Human Recombinant, His Tag

CTF1, CT1, CT-1, Cardiophin 1.

Product # :

CYT-436

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The Cardiotrophin His-Tagged Fusion Protein Human, produced in E. coli, is 22.5 kDa protein containing 200 amino acid residues of the human Cardiotrophin and 12 additional amino acid residues – His Tag (underlined).

Source

Escherichia Coli.

Formulation

CTF1 was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Purity of CTF1 Human Recombinant is greater than 90% as determined by SDS-PAGE.

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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
CTF1, CT1, CT-1, Cardiophin 1.
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
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10?g/ml. In higher concentrations the solubility of this antigen is limited. Protein is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.
Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 22.5kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The biological functionality of CTF1 Protein will be determined in the future.

What is the amino acid sequence of CTF1 Protein?
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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-3 Receptor Subunit Alpha Human Recombinant

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

Product # :

CYT-1049

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sds-page
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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.
Background
What is the molecular weight/Mw of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein has a total Mw of 34.1kDa.

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

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

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

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

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

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

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

Where can I order bulk mg quantities of IL 3 RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Betacellulin Human Recombinant, HEK

Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

Product # :

CYT-1188

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Description

BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

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Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.
Synonyms
Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC
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
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9.8kDa.

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

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

What is the Biological Activity of BETACELLULIN Protein?
ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

What is the amino acid sequence of BETACELLULIN Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

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

What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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.

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