Search: 1000 results found for "Other Cytokines"

Description:

Interleukin-1 alpha Human Recombinant

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-253

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Description

Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM Tris-HCl, pH 8.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 10⁹ IU/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 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 Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.
Background
What is the molecular weight/Mw of IL1A HUMAN Protein?
IL1A HUMAN Protein has a total Mw of 18kDa.

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

What is the Purity of IL1A HUMAN Protein?
IL1A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

What is the amino acid sequence of IL1A HUMAN Protein?
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

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

What is the endotoxin level for IL1A HUMAN Protein?
The endotoxin level is minimal, IL1A 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 1.13 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-1 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-31 Canine Recombinant, His Tag

IL-31, Interleukin 31, IL31.

Product # :

CYT-1016

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Description

IL31 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (24-159a.a.) and having a molecular mass of 16.1kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL31 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL31 Canine protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.
Synonyms
IL-31, Interleukin 31, IL31.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQHHHH 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:

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

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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:

Wingless-Type MMTV Integration Site Family, Member 3A Human Recombinant

Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.

Product # :

CYT-861

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Description

WNT3A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 335 amino acids (19-352 a.a.) and having a molecular mass of 37.5kDa. The WNT3A Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The WNT3A Human protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins are implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. WNT3A is a member of the WNT gene family. WNT3A is a protein which shows 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. The WNT3A gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region.
Synonyms
Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.
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
MSYPIWWSLA VGPQYSSLGS QPILCASIPG LVPKQLRFCR NYVEIMPSVA EGIKIGIQEC QHQFRGRRWN CTTVHDSLAI FGPVLDKATR ESAFVHAIAS AGVAFAVTRS CAEGTAAICG CSSRHQGSPG KGWKWGGCSE DIEFGGMVSR EFADARENRP DARSAMNRHN NEAGRQAIAS HMHLKCKCHG LSGSCEVKTC WWSQPDFRAI GDFLKDKYDS ASEMVVEKHR ESRGWVETLR PRYTYFKVPT ERDLVYYEAS PNFCEPNPET GSFGTRDRTC NVSSHGIDGC DLLCCGRGHN ARAERRREKC RCVFHWCCYV SCQECTRVYD VHTCK.

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, Sf9

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

Product # :

CYT-878

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Description

IL18BP Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 406 amino acids (31-194a.a) and having a molecular mass of 44.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). IL18BP is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL18BP protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% 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, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.
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
ADPTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQGLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

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

Description:

Bone Marrow Stromal Cell Antigen 2 Human Recombinant

Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.

Product # :

CYT-059

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Description

BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.
Synonyms
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
NPC-A-7.
Physical Appearance
BST2 is supplied as a 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 MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
Background
The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine
Introduction
As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.
BST-2: The Cellular Virtuoso
BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.
Engineering a Cellular Maestro
Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.
Stepping into the Biological Arena
Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.
A Standing Ovation for Results
Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.
Conclusion
The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST2 Protein?
BST2 Protein has a total Mw of 14.8kDa.

What is the source or expression system of BST2 Protein?
Escherichia Coli.

What is the Purity of BST2 Protein?
BST2 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BST2 Protein?
The biological functionality of BST2 Protein will be determined in the future.

What is the amino acid sequence of BST2 Protein?
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

What applications can BST2 Protein be used in?
BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST2 Protein?
The endotoxin level is minimal, BST2 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-Beta Human Recombinant, His Tag

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

Product # :

CYT-495

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Description

TNF-b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (35-205 a.a.) and having a molecular mass of 20.9kDa. TNF-b is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-b protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect is <0.3 ng/ml.

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Introduction
TNF-b is a potent multifunctional cytokine produced mainly by activated T and B lymphocytes. The protein has been shown to have a specific potent cytotoxic activity on tumor cells and a variety of other target cells as well as being a mediator of inflammation and immune function.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
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 MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.

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 Like-1 Human Recombinant, Sf9 Active

Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.

Product # :

CYT-1052

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SDS-PAGE
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Description

IL1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 318 amino acids (19-328a.a.) and having a molecular mass of 36.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1RL1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1RL1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

SDS-PAGE

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Introduction
The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.
Synonyms
Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.
Background
What is the molecular weight/Mw of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein has a total Mw of 36kDa.

What is the source or expression system of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

What is the amino acid sequence of IL1RL1 HUMAN, SF9 ACTIVE Protein?
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

What applications can IL1RL1 HUMAN, SF9 ACTIVE Protein be used in?
IL1RL1 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RL1 HUMAN, SF9 ACTIVE Protein?
The endotoxin level is minimal, IL1RL1 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RL1 HUMAN, SF9 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 IL1RL1 HUMAN, SF9 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:

Follistatin Mouse Recombinant

Follistatin, FST, FS, Activin-binding protein, AL033346.

Product # :

CYT-124

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Shipped at Room temp

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Description

Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse Follistatin is lyophilized from 10mM Na2PO4 and 50mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
Background
What is the molecular weight/Mw of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein has a total Mw of 31.6kDa.

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

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

What is the Biological Activity of FOLLISTATIN MOUSE Protein?
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

What is the amino acid sequence of FOLLISTATIN MOUSE Protein?
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.

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

What is the endotoxin level for FOLLISTATIN MOUSE Protein?
The endotoxin level is minimal, FOLLISTATIN 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-3 Mouse Recombinant, sf9

Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

Product # :

CYT-922

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Description

IL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 148 amino acids (27-166 a.a.) and having a molecular mass of 16.7kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

SDS-PAGE

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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.
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
ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.
Background
What is the molecular weight/Mw of IL3 MOUSE, SF9 Protein?
IL3 MOUSE, SF9 Protein has a total Mw of 16.7kDa.

What is the source or expression system of IL3 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL3 MOUSE, SF9 Protein?
IL3 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 MOUSE, SF9 Protein?
The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

What is the amino acid sequence of IL3 MOUSE, SF9 Protein?
ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.

What applications can IL3 MOUSE, SF9 Protein be used in?
IL3 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL3 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 MOUSE, 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 IL3 MOUSE, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-12 p75, Rat Anti-Mouse

Product # :

ANT-209

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Murine IL-12 p75.
Ig Subclass
Rat IgG2b.
Clone
NYRmIL-12p75.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Note
This antibody recognizes the entire IL-12 molecule and has no reactivity to denatured p40 or p35.
Titer
By direct ELISA, 1:5,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Rat Anti Mouse 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.

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:

Beta Defensin-3, Mouse Anti Human

HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

Product # :

ANT-050

Price :

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Shipped with Ice Packs

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human beta-defensin-3
Ig Subclass
mouse IgG2a
Clone
hb-def3
Applications
Direct ELISA, Immuneprecipitation, blotting , Immunohistochemistry.
Titer
By direct ELISA, 1:7,000 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 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange

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 Type 2 Human Recombinant, His Tag

Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-674

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Description

TNFR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 184 amino acids fragment (23-206) having a molecular weight of 24.45kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR2 protein is supplied in 20mM Tris HCl pH-8, 5mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
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
LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWV
PECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSD
VVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT.

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

Description:

Interleukin-36 Receptor Antagonist Human Recombinant

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

Product # :

CYT-009

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.
Synonyms
Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Val-Leu-Ser-Gly.

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

Description:

Mouse Anti Human Connective Tissue Growth Factor

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

ANT-699

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Formulation

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

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CTGF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTGF protein 27-349 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
PAT18E7AT.
Applications
CTGF antibody has been tested by ELISA, Western blot analysis and ICC/IF 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
CTGF antibody was purified 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:

Interleukin-1 alpha Human Recombinant, His Tag Active

Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.

Product # :

CYT-1134

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Description

IL1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (113-271 a.a) and having a molecular mass of 22.4kDa. IL1A is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL1A protein solution (1mg/ml) contains 20mM Tris-HCl (pH 7.5) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 0.04 ng/ml.

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Introduction
IL-1 alpha is derived fromactivated macrophages. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity.
Synonyms
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
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 KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.
Background
What is the molecular weight/Mw of IL1A HUMAN, HIS ACTIVE Protein?
IL1A HUMAN, HIS ACTIVE Protein has a total Mw of 22.4kDa.

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

What is the Purity of IL1A HUMAN, HIS ACTIVE Protein?
IL1A HUMAN, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN, HIS ACTIVE Protein?
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 0.04 ng/ml.

What is the amino acid sequence of IL1A HUMAN, HIS ACTIVE Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.

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

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

RANK Mouse Recombinant

Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa B.

Product # :

CYT-1161

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Description

RANK Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 426 amino acids (31-214 aa) and having a molecular mass of 47.5kDa.RANK is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

RANK protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 11A or TNFRSF11A or RANK, is a protein, part of the tumor necrosis factor receptor (TNFR) group of proteins. RANK acts as the receptor of RANK-Ligand and regulates osteoclast activation & differentiation. RANK protein has been linked to activation of NF-kappa B & c-jun N-terminal kinase, enhancement of T cell growth, bone remodeling and repair, dendritic cell function, lymph node development, immune cell function, mammary gland development & thermal regulation.
Synonyms
Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa B.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLVTPPCTQ ERHYEHLGRC CSRCEPGKYL SSKCTPTSDS VCLPCGPDEY LDTWNEEDKC LLHKVCDAGK ALVAVDPGNH TAPRRCACTA GYHWNSDCEC CRRNTECAPG FGAQHPLQLN KDTVCTPCLL GFFSDVFSST DKCKPWTNCT LLGKLEAHQG TTESDVVCSS SMTLRRPPKE AQAYLPSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI VEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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

Description:

Thymic Stromal Lymphopoietin Receptor Human Recombinant, Sf9

Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.

Product # :

CYT-995

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Description

TSLPR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 218 amino acids (23-231) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TSLPR is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TSLPR protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.
Synonyms
Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.
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
ADPQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SKHHHHHH.

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:

Neuropoietin Mouse Recombinant

Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

Product # :

CYT-1128

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Description

Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

More Info

Introduction
CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.
Synonyms
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
Background
What is the molecular weight/Mw of CTF2P Protein?
CTF2P Protein has a total Mw of 19.7kDa.

What is the source or expression system of CTF2P Protein?
Escherichia Coli.

What is the Purity of CTF2P Protein?
CTF2P Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF2P Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

What is the amino acid sequence of CTF2P Protein?
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

What applications can CTF2P Protein be used in?
CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF2P Protein?
The endotoxin level is minimal, CTF2P 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-32, Mouse Anti Human

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

Product # :

ANT-007

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function. Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine,
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human IL32 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human IL32 amino acids 1-331 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT2F9AT.
Applications
IL32 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 1:500.
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
IL32 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:

IFN Regulatory Factor-2 Human Recombinant

IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.

Product # :

CYT-534

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Description

IFN Regulatory Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 133 amino acids (1-113) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8, 1mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IFN regulatory factor 2 is a member of the IFN regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of IFNs alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4. IRF2 binds to the upstream regulatory region of type-1 IFN and IFN-inducible MHC class-1 genes (the IFN consensus sequence (ics) and represses those genes.
Synonyms
IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.
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 MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.
Background
What is the molecular weight/Mw of IRF2 HUMAN Protein?
IRF2 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IRF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF2 HUMAN Protein?
IRF2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF2 HUMAN Protein?
The biological functionality of IRF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.

What applications can IRF2 HUMAN Protein be used in?
IRF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF2 HUMAN Protein?
The endotoxin level is minimal, IRF2 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:

IL-6 Receptor Beta Mouse Recombinant

IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.

Product # :

CYT-918

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Description

IL6R produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 603 amino acids (23-617a.a.) and having a molecular mass of 67.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).IL6R is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL6R protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.
Synonyms
IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.
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
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.
Background
Research Paper on IL-6 Receptor Beta Mouse Recombinant
Abstract:
The IL-6 Receptor Beta Mouse Recombinant stands as a pivotal player in deciphering the intricate realm of immune modulation. This research paper offers an in-depth exploration of its molecular intricacies and its profound implications in immunological research. By delving into its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its role in shaping immune responses.
Introduction:
The IL-6 Receptor Beta Mouse Recombinant has emerged as a central focus in immunological investigations. This paper aims to provide a comprehensive understanding of its molecular attributes and its influence on immune mechanisms.
Molecular Insights and Signaling Proficiency:
Examining the molecular architecture of IL-6 Receptor Beta Mouse Recombinant, we uncover its critical role in transducing IL-6 signals. Its intricate interactions and signaling proficiency contribute to precise immune responses.
Influencing Immune Responses:
IL-6, a key cytokine, exerts remarkable effects on immune cell activation and inflammation. IL-6 Receptor Beta Mouse Recombinant serves as an essential component in the IL-6 signaling pathway, influencing immune outcomes.
Synonyms and Network Connections:
Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, deepens our comprehension of cytokine-mediated signaling networks. The intricate interplay between IL-6 Receptor Beta Mouse Recombinant and these molecules shapes immune dynamics.
Potential Therapeutic and Research Applications:
IL-6 Receptor Beta Mouse Recombinant transcends the boundaries of laboratory research. Its potential as a therapeutic target for immune-related disorders and its utility in deciphering immune responses offer promising avenues for clinical applications.
Clinical Relevance and Future Prospects:
The clinical relevance of IL-6 Receptor Beta Mouse Recombinant is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies to modulate immune-related conditions.
Conclusion:
In the intricate tapestry of immunology, IL-6 Receptor Beta Mouse Recombinant emerges as a central player in orchestrating immune responses. Its molecular intricacies, pivotal functions, and potential therapeutic implications position it as a cornerstone in understanding immune regulation and developing innovative interventions.
What is the molecular weight/Mw of IL6R MOUSE Protein?
IL6R MOUSE Protein has a total Mw of 67.7kDa.

What is the source or expression system of IL6R MOUSE Protein?
Sf9, Insect cells.

What is the Purity of IL6R MOUSE Protein?
IL6R MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6R MOUSE Protein?
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.

What is the amino acid sequence of IL6R MOUSE Protein?
IL6R MOUSE Protein is composed from XX amino acids.

What applications can IL6R MOUSE Protein be used in?
IL6R MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6R MOUSE Protein?
The endotoxin level is minimal, IL6R MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6R 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 IL6R MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-1 alpha Rat Recombinant, His Tag

Interleukin-1 alpha, IL-1 alpha.

Product # :

CYT-913

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Description

IL 1 alpha Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa. IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 1 alpha protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

More Info

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
Interleukin-1 alpha, IL-1 alpha.
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 MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
Background
What is the molecular weight/Mw of IL1A RAT, HIS Protein?
IL1A RAT, HIS Protein has a total Mw of 20.2kDa.

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

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

What is the Biological Activity of IL1A RAT, HIS Protein?
The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

What is the amino acid sequence of IL1A RAT, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.

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

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

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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Quantity :

Shipping Method :

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.

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