Search: 1000 results found for "Anti Mouse Cytokine"

Description:

Interleukin-13 109 a.a. Rat Recombinant

NC300, ALRH, BHR1, P600, IL-13.

Product # :

CYT-182

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Description

Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 11.9 kDa. The IL-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized in PBS, pH7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

ED₅₀ range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

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Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
Synonyms
NC300, ALRH, BHR1, P600, IL-13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 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 IL-13 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:

Betacellulin Mouse Recombinant

Betacellulin, Probetacellulin.

Product # :

CYT-131

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Description

BTC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.0kDa. The BTC is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×10⁸ IU/mg.

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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 probably mediated by the egf receptor and other related receptors.
Synonyms
Betacellulin, Probetacellulin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BTC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC 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 BTC Mouse Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.

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

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?
The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.

What is the amino acid sequence of BETACELLULIN Protein?
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY

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.

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

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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:

B-cell Activating Factor, Mouse Anti Human

BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.

Product # :

ANT-367

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Formulation

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

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Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response. B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays. Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.
Physical Appearance
Sterile Filtered colorless solution.
Immunogen
Anti-human BAFF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human BAFF amino acids 134-285 purified from E. coli.
Ig Subclass
Mouse IgG3 heavy chain and κ light chain.
Clone
PH4C7AT.
Applications
BAFF antibody has been tested by ELISA and 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 dilution range for Western blot analysis is 1:500 ~ 1,000. 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
BAFF 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:

Endoglin Mouse Recombinant

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Cell surface MJ7/18 antigen, Endoglin.

Product # :

CYT-424

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Shipped at Room temp

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Description

CD105 Mouse Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 581 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 75-85 kDa under reducing conditions in SDS-PAGE. Based on N-terminal sequence analysis, the primary structure of recombinant mature Endoglin starts at Glu 26. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

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

Biological Activity

Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Cell surface MJ7/18 antigen, Endoglin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDRGVLPLPITLLFVIYSFVPTTGLAERVGCDLQPVDPTRGEVT
FTTSQVSEGCVAQAANAVREVHVLFLDFPGMLSHLELTLQASKQNGTETQEVF
LVLVSNKNVFVKFQAPEIPLHLAYDSSLVIFQGQPRVNITVLPSLTSRKQILDWA
ATKGAITSIAALDDPQSIVLQLGQDPKAPFLCLPEAHKDMGATLEWQPRAQTP
VQSCRLEGVSGHKEAYILRILPGSEAGPRTVTVMMELSCTSGDAILILHGPPYVS
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 61kDa.

What is the source or expression system of CD105 Protein?
Insect Cells.

What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

What is the amino acid sequence of CD105 Protein?
MDRGVLPLPITLLFVIYSFVPTTGLAERVGCDLQPVDPTRGEVT
FTTSQVSEGCVAQAANAVREVHVLFLDFPGMLSHLELTLQASKQNGTETQEVF
LVLVSNKNVFVKFQAPEIPLHLAYDSSLVIFQGQPRVNITVLPSLTSRKQILDWA
ATKGAITSIAALDDPQSIVLQLGQDPKAPFLCLPEAHKDMGATLEWQPRAQTP
VQSCRLEGVSGHKEAYILRILPGSEAGPRTVTVMMELSCTSGDAILILHGPPYVS

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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-1 Receptor Antagonist Rat Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

Product # :

CYT-152

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Description

IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL 1RA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ
Background
What is the molecular weight/Mw of IL1RA RAT Protein?
IL1RA RAT Protein has a total Mw of 17.5kDa.

What is the source or expression system of IL1RA RAT Protein?
Escherichia Coli.

What is the Purity of IL1RA RAT Protein?
IL1RA RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RA RAT Protein?
Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

What is the amino acid sequence of IL1RA RAT Protein?
HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ.

What applications can IL1RA RAT Protein be used in?
IL1RA RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RA RAT Protein?
The endotoxin level is minimal, IL1RA RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RA RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1RA RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Indian Hedgehog Mouse Recombinant

Indian hedgehog protein, IHH, HHG-2, BDA1.

Product # :

CYT-398

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

IHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED₅₀ for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.

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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
Background
What is the molecular weight/Mw of IHH MOUSE Protein?
IHH MOUSE Protein has a total Mw of 19.8kDa.

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

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

What is the Biological Activity of IHH MOUSE Protein?
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.

What is the amino acid sequence of IHH MOUSE Protein?
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

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

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

HVEM Mouse Recombinant

Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

Product # :

CYT-1145

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Description

TNFRSF14 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 407 amino acids (39-206 aa) and having a molecular mass of 45.3kDa.TNFRSF14 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The TNFRSF14 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Herpesvirus entry mediator or HVEM or tumour necrosis factor receptor superfamily member 14 or TNFRSF14, is part of the TNF receptors family that is a receptor located on the cell surface. The cytoplasmic area of this receptor can bind all sorts of TNF receptor associated factor (TRAF) protein. Those proteins can mediate pathways activating an immune response. The MITF is regulating TNFRSF14 gene expression.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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
QPSCRQEEFL VGDECCPMCN PGYHVKQVCS EHTGTVCAPC PPQTYTAHAN GLSKCLPCGV
CDPDMGLLTW QECSSWKDTV CRCIPGYFCE NQDGSHCSTC LQHTTCPPGQ RVEKRGTHDQ
DTVCADCLTG TFSLGGTQEE CLPWTNCSAF QQEVRRGTNS TDTTCSSQLE PKSCDKTHTC
PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN
AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP
QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL
YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

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:

TNF Receptor Superfamily Member 4 Mouse Recombinant

Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.

Product # :

CYT-1179

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Description

TNFRSF4 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-211) containing 435 amino acids and having a molecular mass of 48.6kDa.TNFRSF4 is fused to a 243 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

TNFRSF4 protein (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤ 0.4 ug/ml which measured by its binding ability in a functional ELISA with Mouse OX40 Ligand/TNFSF4.

More Info

Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
Synonyms
Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.
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
DGSMVTARRL NCVKHTYPSG HKCCRECQPG HGMVSRCDHT RDTLCHPCET GFYNEAVNYD TCKQCTQCNH RSGSELKQNC TPTQDTVCRC RPGTQPRQDS GYKLGVDCVP CPPGHFSPGN NQACKPWTNC TLSGKQTRHP ASDSLDAVCE DRSLLATLLW ETQRPTFRPT TVQSTTVWPR TSELPSPPTL VTPEGPLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH

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:

CTACK Mouse Recombinant (CCL27)

C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

Product # :

CHM-013

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Description

CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

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Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
Synonyms
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK 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 CTACK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
Background
What is the molecular weight/Mw of CTACK MOUSE Protein?
CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

What is the Biological Activity of CTACK MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CTACK MOUSE Protein?
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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

Who supplies recombinant CTACK 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 CTACK 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:

Beta Defensin-14 Mouse Recombinant

Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.

Product # :

CYT-945

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Description

Beta Defensin-14 Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 45 amino acids and having a molecular mass of 5.2kDa.The BD14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.
Synonyms
Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse BD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-14 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 BD14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.
Background
What is the molecular weight/Mw of BD14 Protein?
BD14 Protein has a total Mw of 5.2kDa.

What is the source or expression system of BD14 Protein?
Escherichia Coli.

What is the Purity of BD14 Protein?
BD14 Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of BD14 Protein?
The biological functionality of BD14 Protein will be determined in the future.

What is the amino acid sequence of BD14 Protein?
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.

What applications can BD14 Protein be used in?
BD14 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD14 Protein?
The endotoxin level is minimal, BD14 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:

RELM-alpha Mouse Recombinant

Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

Product # :

CYT-309

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Shipped at Room temp

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Description

Mouse RELM-alpha Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10 kDa. The Mouse RELM-alpha is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Sterile filtered and lyophilized from 0.5mg/ml in 10mM sodium phosphate buffer, pH 7.5.

Purity

Greater than 98% as determined by SDS-PAGE & RP-HPLC.

More Info

Introduction
Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMF stimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation.
Synonyms
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
At 0.1mg/ml of deionized sterile water.
Amino Acid Sequence
MDETIEIIVE NKVKELLANP ANYPSTVTKT LSCTSVKTMN RWASCPAGMT ATGCACGFAC GSWEIQSGDT CNCLCLLVDW TTARCCQLS.

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

Description:

Interferon Alpha And Beta Receptor Mouse Recombinant

IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

Product # :

CYT-994

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Shipped with Ice Packs

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Description

IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.
Synonyms
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
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
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
Background
What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.

What is the source or expression system of IFNAR1 MOUSE Protein?
Sf9, Baculovirus cells.
What is the Purity of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNAR1 MOUSE Protein?
The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.

What is the amino acid sequence of IFNAR1 MOUSE Protein?
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

What applications can IFNAR1 MOUSE Protein be used in?
IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNAR1 MOUSE Protein?
The endotoxin level is minimal, IFNAR1 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-15 Rat Recombinant

IL-15, MGC9721.

Product # :

CYT-345

Price :

Quantity :

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of CTLL-2 was found to be < 10 ng/ml, corresponding to a Specific Activity of 100,000IU/mg.

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Introduction
The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.
Synonyms
IL-15, MGC9721.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-15 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asn-Trp-Ile-Asp.

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

Description:

Interleukin-22 Rat Recombinant

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-173

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL-22 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.6kDa.The IL22 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The biological activity is measured by its ability to induce IL-10 secretion in COLO 205 (human colon carcinoma cells). The expected ED₅₀ for this effect is 0.15-0.75ng/ml.

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Introduction
IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPINSQCKLE AANFQQPYIV NRTFMLAKEA SLADNNTDVR LIGEELFRGV KAKDQCYLMK QVLNFTLEDV LLPQSDRFQP YMQEVVPFLT KLSIHLSPCH ISGDDQNIQK NVRQLKETVQ KLGESGEIKA IGELDLLFMS LRNACV.

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

Description:

Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9

Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.

Product # :

CYT-912

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFA protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 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
LRSSSQNSSD KPVAHVVANH QVEEQLEWLS QRANALLANG MDLKDNQLVV PADGLYLVYS QVLFKGQGCP DYVLLTHTVS RFAISYQEKV NLLSAVKSPC PKDTPEGAEL KPWYEPIYLG GVFQLEKGDQ LSAEVNLPKY LDFAESGQVY FGVIALHHHH 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:

Thrombopoietin Mouse Recombinant, HEK

Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

Product # :

CYT-1157

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Description

TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293.

Formulation

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

Purity

Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

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Introduction
Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.
Synonyms
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 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
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH H.

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 Active

Interleukin-1 alpha, IL-1 alpha.

Product # :

CYT-1100

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Description

IL1A 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.IL1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL1A protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

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Introduction
IL-1 alpha is produced by activated macrophages.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and 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 YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
Background
What is the molecular weight/Mw of IL1A RAT, HIS ACTIVE Protein?
IL1A RAT, HIS ACTIVE Protein has a total Mw of 20.2kDa.

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

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

What is the Biological Activity of IL1A RAT, HIS ACTIVE Protein?
The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

What is the amino acid sequence of IL1A RAT, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
.What applications can IL1A RAT, HIS ACTIVE Protein be used in?
IL1A RAT, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Follistatin Mouse Recombinant

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

Product # :

CYT-124

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Quantity :

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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:

Endoglin (27-581) Mouse Recombinant

Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.

Product # :

CYT-972

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Description

Endoglin Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-581 a.a.) and having a molecular mass of 60.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).Endoglin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Endoglin protein solution (0.5mg/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
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.
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
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 60.9kDa.

What is the source or expression system of CD105 Protein?
Sf9, Baculovirus cells.

What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.

What is the amino acid sequence of CD105 Protein?
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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:

Eotaxin Mouse Recombinant (CCL11)

Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

Product # :

CHM-308

Price :

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Shipped at Room temp

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Description

Eotaxin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8403.2 Dalton. The CCL11 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.
Background
What is the molecular weight/Mw of EOTAXIN MOUSE Protein?
EOTAXIN MOUSE Protein has a total Mw of 8.4kDa.

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

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

What is the Biological Activity of EOTAXIN MOUSE Protein?
The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

What is the amino acid sequence of EOTAXIN MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.

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

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

Who supplies recombinant EOTAXIN 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 EOTAXIN 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:

Tumor Necrosis Factor Receptor Mouse Recombinant

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.

Product # :

CYT-774

Price :

Quantity :

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Shipped at Room temp

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Description

TNFR Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.1kDa.The TNFR is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR 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

The ED₅₀ as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg in the presence of 0.1 ng/mL of rMuTNF-a.

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Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
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. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFR although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNFR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IHPSGVTGLV PSLGDREKRD SLCPQGKYVH SKNNSICCTK CHKGTYLVSD CPSPGRDTVC RECEKGTFTA SQNYLRQCLS CKTCRKEMSQ VEISPCQADK DTVCGCKENQ FQRYLSETHF QCVDCSPCFN GTVTIPCKET QNTVCNCHAG FFLRESECVP CSHCKKNEEC MKLCLPPPLA NVTNPQDSGT A.

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

Description:

Desert Hedgehog (C23II) Mouse Recombinant

Desert hedgehog protein, DHH, HHG-3, C78960.

Product # :

CYT-773

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

DHH (C23II) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 20kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 1mM DTT and 0.05% Tween-80.

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 its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 µg/ml.

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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
Desert hedgehog protein, DHH, HHG-3, C78960.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASG PAEGRVTRGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG.

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:

Sonic Hedgehog Mouse Recombinant

SHH, HHG-1, HHG1, Sonic hedgehog protein.

Product # :

CYT-597

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Sonic Hedgehog Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The Mouse Sonic Hedgehog is 99% homologous to the human gene.Cysteine at position 25 has been substituted with Ile.The Sonic HedgeHog is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM Na2PO4 pH-7.5.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Determined by the dose-dependent induction of alkaline phosphatase production by C3H/10T1/2 (CCL-226) fibroblasts and is typically 0.48-0.72 µg/ml.

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Introduction
Recombinant Mouse Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Mouse Sonic Hedgehog is 99% homologous to the human gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog 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 Sonic Hedgehog in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG.

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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